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Production and microwave thermal processing considerations for a prototype reformed roast made from the beef forequarter

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Production and microwave thermal processing considerations for a prototype reformed roast made from the beef forequarter
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Yates, Joseph A., 1955-
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English
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ix, 195 leaves : ill. ; 28 cm.

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Subjects / Keywords:
Beef ( jstor )
Cooking ( jstor )
Fats ( jstor )
Food ( jstor )
Heating ( jstor )
Meats ( jstor )
Microwave ovens ( jstor )
Microwaves ( jstor )
Muscles ( jstor )
Ovens ( jstor )
Animal Science thesis Ph. D
Cooking (Beef) ( lcsh )
Dissertations, Academic -- Animal Science -- UF
Microwave cooking ( lcsh )
City of Miami ( local )
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bibliography ( marcgt )
non-fiction ( marcgt )

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Thesis:
Thesis (Ph. D.)--University of Florida, 1988.
Bibliography:
Includes bibliographical references (leaves 176-193).
General Note:
Typescript.
General Note:
Vita.
Statement of Responsibility:
Joseph A. Yates

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University of Florida
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Copyright [name of dissertation author]. Permission granted to the University of Florida to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder.
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PRODUCTION AND MICROWAVE THERMAL PROCESSING
CONSIDERATIONS FOR A PROTOTYPE REFORMED
ROAST MADE FROM THE BEEF FOREQUARTER




By

JOSEPH A. YATES


A DISSERTATION PRESENTED TO THE GRADUATE SCHOOL OF
THE UNIVERSITY OF FLORIDA
IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE
DEGREE OF DOCTOR OF PHILOSOPHY









UNIVERSITY OF FLORIDA


1988




PRODUCTION AND MICROWAVE THERMAL PROCESSING
CONSIDERATIONS FOR A PROTOTYPE REFORMED
ROAST MADE FROM THE BEEF FOREQUARTER
By
JOSEPH A. YATES
A DISSERTATION PRESENTED TO THE GRADUATE SCHOOL OF
THE UNIVERSITY OF FLORIDA
IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE
DEGREE OF DOCTOR OF PHILOSOPHY
UNIVERSITY OF FLORIDA
1988


This dissertation is dedicated
to my wife, Diana, and my son, Brandon,
whose never-ending love,
patience, and unselfish support
help make my dreams reality.
To my parents, Josephine and Joseph Yates,
my brothers, Christopher and Phillip,
and my mother-in-law, Betty Gene Mosel,
for their support and prayers,
throughout my college endeavors.


ACKNOWLEDGEMENTS
There were many people who assisted in the completion of
this project. The author expresses his appreciation to Dr.
Roger L. West, chair of the supervisory committee, and to Dr.
Rachel B. Shireman, cochair, for their guidance, supervision,
and contributions in preparation of this manuscript.
The contributions of Dr. S.C. Denham, Dr. D.D. Johnson,
Dr. J.W. Lamkey, Dr. F.W. Leak, Jr., Dr. M. Marshall, and Dr.
A. Teixeira are appreciated for the valued support,
encouragement, and assistance they provided during his
graduate program.
Appreciation is extended to Ms. Karen Christensen for
her support and willingness to help in getting this project
completed. Special thanks are also extended to Ms. Jannet
Eastridge, Ms. Debbie Neubauer, and Ms. Ana Zometa for their
technical help. I am very grateful to Mr. Larry Eubanks,
manager of the meat laboratory. Despite my impatience, his
friendship and expertise during this project have proven to
be invaluable. For his light-hearted attitude, while being
serious about his work, he will always be remembered.
iii


The author's appreciation is also extended to his fellow
graduate students for their friendship and assistance during
his graduate program.
The author wishes to extend his thanks to the Jet Net
Corporation and Viskase Corporation for their generosity in
providing equipment and supplies necessary for completion of
this research.
The author is grateful to the Beef Industry Council for
providing the monitary support required to conduct this
research.
Finally, his deepest thanks of appreciation and love are
extended to his wife Diana and son Brandon, for it has been
their never-ending encouragement that turned this dream into
reality.
iv


TABLE OF CONTENTS
Page
ACKNOWLEDGEMENTS iii
ABSTRACT vii
CHAPTERS
1 INTRODUCTION 1
2 LITERATURE REVIEW 8
Restructured Products 8
Manufacturing Considerations for Re
structured Beef Products 10
Muscle Selection Criterion 20
Muscle Protein Functionality 26
Mechanisms of Protein-Water Interactions.. 28
Influence on Protein-Water Interactions... 34
pH influence 34
Sodium chloride influence 35
Influence of phosphates... 39
Water Distribution 44
Heat-Induced Changes in Meat 51
Microwave Heating 70
3 PREDICTING FINAL INTERNAL TEMPERATURE THROUGH
THE USE OF POST-COOKING TEMPERATURE RISE IN
REFORMED BEEF ROASTS COOKED WITH VARIABLE
MICROWAVE POWER LEVELS 90
Introduction 90
Materials and Methods 92
Preparation of Sample 92
Microwave Cooking 94
Proximate Analysis 96
Statistical Analysis 96
Results and Discussion 98
Summary 116
v


Page
4 COMPARISON OF MICROWAVE AND CONVENTIONAL
COOKERY AND END-POINT TEMPERATURE ON CHEMICAL,
PHYSICAL, AND SENSORY PROPERTIES OF REFORMED
BEEF ROASTS PRODUCED FROM CHUCK MUSCLES 118
Introduction 118
Materials and Methods 121
Raw Material 122
Cooking Methods 123
Proximate Analysis and Sarcomere Length... 126
Shear Force 127
Bind Strength 127
Sensory analysis 128
Statistical analysis 129
Results and Discussion 130
Study 1 130
Cooking times 132
Cooking losses 138
Changes in sarcomere length 140
Proximate analysis 142
Texture measurements 144
Binding strength 146
Sensory evaluation 148
Study II 163
Overall Summary 170
APPENDIX INSTRON FORCE DEFORMATION CURVE 175
REFERENCES 176
BIOGRAPHICAL SKETCH 194
vi


Abstract of Dissertation Presented to the Graduate School
of the University of Florida in Partial Fulfillment of the
Requirements for the Degree of Doctor of Philosophy
PRODUCTION AND MICROWAVE THERMAL PROCESSING
CONSIDERATIONS FOR A PROTOTYPE REFORMED
ROAST MADE FROM THE BEEF FOREQUARTER
by
Joseph A. Yates
December 1988
Chair: R.L. West
Cochair: R.B. Shireman
Major Department: Animal Science
Latissimus dorsi (LD) and Serratis ventralis (SV)
muscles were removed from 48 USDA Choice, yield grade 3 beef
forequarters, processed into reformed roasts and used to
compare palatability, chemical and physical characteristics
resulting from conventional and microwave cooking. Equations
were developed for predicting the extent to which post
cooking temperature rise occurred within the roasts during
microwave cooking to control final internal end-point
temperature and allow comparison of methods.
Study I used a factorial arrangement to quantify changes
in meat components as related to heating rate (slow in
conventional vs fast in microwave cooking): three
replications by two roast types (LD and SV) by four cooking
methods (conventional, low, medium, and high power microwave
levels) by three end-point temperatures (60oC, 70C, and
75C). Study II used LD roasts in a factorial arrangement to
study changes in extracellular water space (ESC) as related
vii


to the method of heat production (conventional vs. microwave)
when heating rate was equivalent. Heating rates were made
equivalent by slowing the cooking rate in the microwave.
Results of Study I indicated microwave cooking required
less time than conventional cooking for all treatment
combinations tested. Total cooking loss was higher with high
power microwave cooking and lower (P < 0.05) for conventional
and low power microwave cooking. End-point temperature of
6O0C produced lower cooking losses than 70 or 75oC which were
not different (P < 0.05). Changes in chemical composition
indicated greater water losses for medium and high power
microwave cooking (P < 0.05) compared to other cooking
methods. The percentage change in sarcomere length from raw
to cooked samples increased as end-point temperature
increased. Kramer shear force values were lower for SV than
LD roasts, while cooking method and end-point temperature had
no effect. Instron assessment of the binding junction
indicated to difference in peak force, work, tensile
strength, strain, or modulus of rigidity due to cooking
method (P > 0.05). Sensory panelists rated SV roasts
superior in juiciness, connective tissue content, and overall
tenderness compared to LD roasts, but no differences were
detected among methods.
In Study II, ECS assessment was conducted using inulin
[14C] carboxylic acid. Thermal processing reduced ECS;
however, method of heat generation did not affect ECS.
viii


In summary, when final internal end-point temperature
is controlled differences in chemical and physical
characteristics due to cooking methods are minimized.
ix


CHAPTER 1
INTRODUCTION
The 1985/86 Annual Report of the National Live Stock and
Meat Board indicates that the beef industry must become more
consumer-oriented to maintain its market share. In the
present decade, one out of four American households consists
of a single individual, compared with one out of ten in 1955
(Anonymous, 1983). The annual report also indicated that
only seven percent of families in America consisted of one
breadwinner, indicating more and more households with two
incomes. Therefore, consumers have more active lifestyles
and an increasing need for convenience. A recent consumer
marketing survey conducted for the National Live Stock and
Meat Board and the American Meat Institute concluded that the
consumer's decision to serve red meat was determined
primarily by convenience, taste and economics (Anonymous,
1987).
As a result of changing lifestyles, consumers of the
eighties do not tend to have the same needs, wants, or
concerns as did consumers twenty years ago. The results of a
1984 Food Marketing Institute study indicated that 71% of
supermarket customers surveyed were concerned with diet and
health issues (Anonymous, 1984). This same study indicated
1


2
that 48% of the supermarket customers surveyed selected
recipes based on their nutritional content and 44% avoided
buying products that had no nutritional information.
A national consumer-retail beef study (Saveli et al.,
1986) suggested that beef products must be lean (free of
trimmable fat), high in quality and convenient to prepare in
order to attract today's consumer. To accomplish these
goals, many retailers have reduced trimmable fat levels on
retail cuts to 6.25 mm and others have removed all of the
outside fat. However, the 1987 Consumer Climate for Meat
Marketing Study indicated that, while per capita consumption
has responded slightly, future progress will be dependent on
continued development of products that meet the consumers'
criteria. In response to these consumer demands, many meat
processors are providing entrees in a ready-to-eat or
precooked form, requiring a reheating period which frequently
involves the use of a microwave oven.
The advent of the microwave oven has opened up a new
dimension in food preparation and management, both in the
home and in the food service industry. The greatest
advantage of microwave cooking is the time and energy saving
considerations. In 1984, 9.1 million microwave ovens
comprised the largest annual purchase of any home appliance
in history (Markov, 1985a).
A major challenge confronting progress toward
consumer-driven marketing approaches is the high price


3
charged for precooked items. This price level is
necessitated by the use of high valued muscles, cooking
losses and equipment for thermal processing and aseptic
packaging. However, consumers appear to resist this higher
price when buying a precooked beef roast, even though they
pay comparable prices for sliced roast beef at the
delicatessen. Perhaps a ready-to-cook roast product designed
for rapid microwave cooking would be more appealing.
In addition to price considerations, the occurrence of
off-flavors in precooked beef entrees is another source of
concern for meat processers. To help overcome the presence
of any off-flavors in a precooked entree, a package of gravy
or seasoned sauce is frequently included with most products.
Perhaps an alternative to precooked meat entrees is
producing a reformed meat product using muscles from the
chuck and plate that could be cooked rapidly in a microwave
oven. Muscles from the chuck and plate are traditionally
lower in economic value compared to muscles from the rib,
loin, and round. The lower economic value associated with
the chuck is due in part to compositional differences between
many of the muscles that make up the chuck. Numerous
researchers have documented significant differences in
connective tissue, contractile status, and intermuscular fat
between the many muscles of the chuck (Ramsbottom et al.,
1945; Ramsbottom and Stradine, 1947; Prost et al., 1975; Zinn
et al., 1970; McKeith et al., 1985; Paterson and Parrish,


4
1986; Recio et al., 1987). Therefore, raw materials from
these regions would provide a means of lowering production
costs and aid in producing a competitively priced product.
In addition, these muscles would provide a source of lean
meat since all surface fat and surface connective tissue
could be removed. This would provide the meat processor with
the ability to produce a boneless roast beef product in which
size, shape, and fat content could be controlled. A roast
beef product of this type could help the beef industry
provide entrees that address the diet-health issues and
fulfill the convenience needs of the consumer.
In contrast to traditional restructured products the
texture of this reformed product should be comparable to that
of a whole muscle entree. The convenience attribute could be
achieved by producing a portion size needed by a two or three
member family for one meal (340 to 450 g) that could be
cooked quickly in a microwave or conventional oven.
Several major obstacles currently hinder production of such a
product. First, little research has been conducted on
feasible procedures for producing reformed whole beef muscle
products that utilize lower valued muscles. Research is
needed to develop production procedures that consider:
1) Economically feasible methods for removal of heavy
surface layer connective tissue (epimysium).


5
2) Protein extraction methods that do not result in
loss of muscle integrity and yet produce acceptable
binding characteristics upon thermal processing.
3) Stuffing procedures that generate a uniformly shaped
product.
Also, previous attempts to cook meat entrees in a microwave
oven have failed to produce a product of acceptable quality.
Although the microwave oven has been shown to decrease
cooking time, labor and energy costs, it has not been readily
accepted by food service institutions or homemakers for
cooking beef entrees. The skepticism surrounding the use of
the microwave oven for preparation of beef entrees is thought
to be due in part to uneven cooking, greater cooking losses,
and less palatable meat (Headley and Jacobson, 1960; Kylem et
al., 1964; Law, 1967; Ream et al., 1974; Drew et al., 1980;
Moore et al., 1980; Griffin et al., 1981). However, many of
these studies have been "trial and error" rather than a
deliberate approach to understanding the microwave heating
process and its effect on muscle tissue. Major questions
still remain unanswered regarding microwave oven cookery of
beef entrees and the perceived relationship with toughness
and lack of product juiciness. Research is needed to
understand the effects on muscle tissue of rapid heating
rates, greater moisture losses and excessive post-cooking
temperature increases. Research emphasis should be directed
so as to study:


6
1) The rate at which heat is conducted into the
product as a result of different heating methods (microwave
or conventional). Knowledge of this information would be
useful in developing a computer aided model to predict
thermal processing conditions required to achieve a certain
degree of doneness.
2) The influence of different heating rates (rapid or
slow) when associated with different cooking methods,
(microwave or conventional) and their effects on the
chemical, textural, and sensory attributes of a meat product.
3) The effects of incorporating different amounts of
water into the meat product during production processes,
subsequent effects on water loss during thermal processing,
and the perceived juiciness and overall palatability of the
products.
The proposed research involves production of a reformed
whole muscle roast beef product and the systematic study of
microwave and conventional cookery effects on beef and
addresses the research needs listed previously.
The objectives of this study are
1) To develop feasible processing procedures for
reforming whole beef muscles, the serratus ventralis and
latissimus dorsi. These two muscles were chosen for several
reasons: a) currently they are not being used to their
highest potential; b) they are unipennate muscles with fibers
oriented in one direction; c) they contain mainly surface


7
connective tissue with no large septums of internal
connective tissue; d) they are two of the larger muscles
found in the forequarter; and e) they differ compositionally
in fat content (>10% and <5% fat for the serratus and
latissimus, respectively).
2) To quantify the changes in meat components that occur
during thermal processing with microwave and conventional
cooking at different cooking rates (low, medium, and high
power) and relate these to changes in physical and sensory
measures of tenderness and palatability.
3) To study changes in tissue fluid distribution, as
influenced by thermal processing (microwave versus
conventional) when beef roasts are cooked to the same
internal end point temperature at the same rate.


CHAPTER 2
LITERATURE REVIEW
Restructured Products
Breidenstein (1982) refers to restructuring as a
processing method by which raw meat materials are converted
into ready-to-cook products. This method of meat processing
has been extensively reviewed by Mandigo (1975), Huffman
(1979), Mandigo (1982a,b), and Breidenstein (1982). The
primary objective for utilizing restructuring technology is
to add economic value to under-utilized raw materials that
are currently considered to be of limited economic value. As
a result, restructuring methodology is considered to be a
means of enhancing the economic value of the raw materials,
and the enhanced value will be preceived as being greater
than the cost of its achievement (Breidenstein, 1982).
Restructured products created to date have been produced
from a variety of different meat species and formulated to
contain different types and levels of non-meat ingredients.
The phrase "intermediate value beef products" was used by
Breidenstein (1982) to refer to a group of restructured beef
products. This group of products is considered to have an
economic value preceived by the consumer to lie between that
of ground beef and that of intact muscle steaks and roasts.
8


9
Breidenstein (1982) warned that caution must be exercised
when selecting raw materials that contain heavy
concentrations of connective tissue embedded in the muscle
mass. Therefore, selection criteria of raw materials and
production methods used for producing restructured beef
products are very important to their acceptability. The
restructuring process typically requires the raw meat
materials to undergo a process of particle size reduction,
blending and reshaping. Several mechanical methods have been
developed to reduce particle size. They include grinding,
flaking, chunking, slicing, and emulsifying. Reducing the
particle size produces numerous meat pieces that must be
bound back together at the various meat interfaces. To
accomplish this, the intracellular protein, myosin, is
commonly used as a binding agent. Extraction of myosin to
the meat surface is accomplished by mechanical mixing,
massaging, or tumbling of the meat particles in the presence
of sodium chloride and phosphates. Maintaining a cohesive
bind in the uncooked product is accomplished by freezing,
while the bind in the cooked product is dependent upon a heat
induced bonding (Breidenstein, 1982).
As a result of the numerous mechanical methods used to
reduce particle size, a wide variety of products have
resulted. In an effort to categorize the various products
produced, Field (1982) identified four groups of restructured
products for retail and food service: 1) frozen, flaked and


10
formed restructured meats; 2) chunked and formed or sectioned
and formed restructured meats; 3) emulsified, ground or
chopped restructured meats; and 4) sliced restructured meats.
Mandigo (1982a) suggested that cured and smoked products also
represented a distinctive group of meat products produced by
restructuring technology.
Formulation considerations and manufacturing procedures
are vital components in the production of a restructured or
reformed roast beef product. The term "reformed," as used
throughout this dissertation, refers to a type of
restructuring process whereby no reduction in particle size
is imposed. Therefore, production methods used to
manufacture a reformed beef product are very important to its
acceptability. The focus of this review will discuss product
manufacturing, muscle selection, protein functionality,
distribution of cellular water and thermal processing of the
final product.
Manufacturing Considerations for Restructured
Beef Products
Through extensive research efforts, many variables have
been identified that influence manufacturing procedures and
organoleptic characteristics of a restructured meat product.
To date, restructured meat products have typically involved
reducing the particle size of the starting material. As
previously stated, particle reduction can be acheived by a
number of methods; flaking is one of the more recently


11
developed methods. This method is capable of using meat in
the fresh or frozen state; however, particle uniformity is
enhanced if the meat is crust frozen or frozen solid (Huffman
and Cordray, 1982). The meat is cut in a shaving-like manner
into flakes of varying particle sizes and texture (Fenters
and Ziemba, 1971; Mandigo et al., 1972; Pietraszek, 1972).
Advantages for products made from flaked meat include
improved texture, reduced drip loss, enhanced binding and
cohesive properties, decreased cooking losses and improved
sensory characteristics (color, flavor, juiciness, and
tenderness) over those products produced from sectioned meat
(Anonymous, 1973).
Reducing the particle size of meat by sectioning
involves cutting large muscles into chunks, which may or may
not be uniform in size. The primary advantage of this method
is that the resulting product should have the palatability
attributes that more nearly resemble that of intact muscle,
compared to products produced from flake cut particles
(Acton, 1972) The main disadvantage of this process is that
fat particles are easily detected. This effectively reduces
the amount of fat that could be incorporated into the
product.
Although most restructured products contain 12 to 25%
fat, increasing the fat content from 20 to 30% was reported
to improve the products sensory properties (Seideman, 1982).
Typically, formulating a product to contain a desired fat


12
content requires using at least two meat sources, one higher
and one lower in fat content.
Booren et al. (1981a) produced sectioned and formed beef
steaks to contain 12% fat in the final product. This
involved utilizing beef chucks trimmed of excess fat and
connective tissue, to provide a source of lean meat that
contained 8 to 10% fat and another source that contained 48
to 52% fat. However, the authors indicated that because of
the heterogenous nature of meat, the fat levels achieved in
the final product were deemed to be the most variable
component. The authors concluded that this was due to the
diverse amounts of inter- and intramuscular fat present in
Choice, Yield Grade 3 chucks. Previously vacuum packaged
beef chucks were allocated to vacuum or non-vacuum mixing
treatments for periods of 6 or 12 minutes. Under the
experimental conditions described by these authors, the added
fat source separated and accumulated on the sides of the
mixer or appeared as large fat pockets within the steak
product. Vacuum mixing was reported to produce a less
desirable surface color in the finished steak product, as
determined by spectrophotometric analysis. It was theorized
that low oxygen tension present during storage of the vacuum
packaged beef chuck and during vacuum mixing caused the
globin molecule to become denatured, which resulted in a less
desirable color. The occurence of this problem had been
previously reported by Lawrie (1974). Two-thiobarbituric


13
acid (TBA) values did not change following 60 d of freezer
storage, regardless of mixing treatment. Vacuum mixing
treatments had no effect on cooked yields, Kramer shear area
or Kramer shear force values. Sensory analysis indicated a
significant increase in bind between meat pieces for vacuum
mixed steaks. The authors reasoned that vacuumization may
function to remove tiny air bubbles from the extracted
protein exudate, resulting in a denser mass of the extracted
myofibrillar proteins at the bind area. Juiciness,
tenderness, flavor and connective tissue residue were not
different due to mixing treatments.
To help create acceptable product tenderness in a
sectioned and formed product, Huffman (1978) proposed a
restructuring process that combined both chunks and wafer
thin slices of meat. The process resulted in a product that
closely resembled whole muscle cuts of meat. A patent was
issued for this restructuring process. Huffman (1979)
concluded that raw meat materials to be used in sectioned and
formed products should be subjected to mechanical
tenderization prior to use. Mechanical tenderization would
help ensure maximum cell disruption and enhance the binding
characteristics of the product. However, this processing
step requires additional equipment, which, in turn, increases
the cost of production.
Independent of the methods utilized to obtain a
reduction in particle size is the importance of the actual


14
particle size. Acton (1972), in an effort to study the
effects of various particle sizes in the production of
poultry loaves, used muscles cut into strips, cubes, coarse
ground, finely ground and finely ground five times. He
reported that decreasing the particle size resulted in
increasing the amount of salt soluble proteins extracted, and
hence, the binding strength of the final product. This was
concluded to be a result of increased surface area associated
with decreasing the particle size. In addition, the author
reported a decrease in cooking loss as particle size
decreased.
In contrast, Chesney and co-workers (1978), in a study
of fabricated pork products, reported that particle size did
not significantly influence the water holding capacity, shear
force values or proximate chemical analysis values. However,
in accordance with Acton (1972), a significant decrease in
cooking loss percentage was also reported as particle size
decreased. Studies by Chesney and co-workers (1978) and
Acton (1972) also agreed on taste characteristics. These
studies indicated that products prepared from large particles
were inferior in cohesion, juiciness, tenderness and overall
acceptability when compared to products prepared from medium
or smaller particle sizes.
Variations in product bite, mouth feel and other sensory
properties can be achieved by altering the ratio of various
particle sizes, fat and moisture content, mixing time and


15
size and shape of the final product (Huffman, 1979).
Popenhagen et al. (1973) reported that combining meat flakes
of different sizes and varying temperatures yielded steaks
that were more desirable in texture and overall eating
quality than steaks made from a single size of flake and
temperature. Similarly, Mandigo (1974) reported that a meat
temperature of -5C at the time of flaking significantly
influenced the texture and appearance of the final product.
Mixing is a processing step required to achieve uniform
distribution of the lean, fat and nonmeat components. Mixing
also facilitates extraction of the intracellular myofibrillar
proteins to the surface of the meat. Extraction of the salt
soluble proteins (actin, myosin, and actomyosin) provides the
binding material necessary to bond the various meat
components together. Two of the most popular processing
methods used to extract the proteins needed to facilitate
binding are massaging and tumbling. Both of these methods
are physical processes designed to mix ingredients, enhance
quality attributes (tenderness) and accelerate meat product
manufacturing (Addis and Schanus, 1979).
Tumbling involves generating "impact energy" as a result
of meat striking the sides and bottom of a rotating drum or
being struck with paddles or baffles (Addis and Schanus,
1979). This action results in a transfer of kinetic energy
to the muscle mass and a resultant rise in temperature. The
tumbling process typically occurs within the confines of a


16
sealed vessel capable of operating while under vacuum.
Vacuumization of the tumbler is reported to help overcome
potential problems such as tissue softening and the
incorporation of air into the extracted protein matrix (Addis
and Schanus, 1979).
Massaging is considered to be a less vigorous process
when compared to the action of tumbling. It involves
generating frictional energy as a result of rubbing meat
surfaces together. Vacuumization of the massager is also
possible and is done to help overcome potential problems
previously stated. The primary purpose of massaging or
tumbling is to facilitate the extraction of the salt soluble
myofibrillar proteins, myosin, actin and actomyosin. The
physical actions associated with massaging or tumbling,
provide a tenderizing effect and help to incorporate added
fluids into the raw meat materials (Addis and Schanus, 1979).
Weiss (1974), in a report on ham tumbling and massaging,
indicated that Europeans categorize muscle tissue as either
firm or soft when selecting the appropriate method for
protein extraction. Beef, mutton and turkey are considered
firm muscles and are subjected to impact tumbling, while soft
muscles, pork and chicken, are subjected to massaging. The
basis for this segregation is due to differences in the
physiological and biochemical composition of the muscle
tissue, and the response of the tissue to various physical
and chemical processing techniques.


17
MacFarlane and coworkers (1977) measured the binding
strength between adjacent meat pieces using myosin,
actomyosin and sarcoplasmic proteins as binding agents.
These authors concluded that myosin exhibited the greatest
binding capability with or without the addition of salt. The
role of the myofibrillar proteins in binding chunk-type
products together has been demonstrated by a number of
researchers (Anonymous, 1971; Rahelic et al., 1974; Ford et
al., 1978; Siegel et al., 1978a,b; Booren et al., 1982).
Booren and coworkers (1981a) studied the effects of
blade tenderization, vacuum mixing, salt addition and mixing
time on the binding of meat pieces from A maturity (young),
Standard grade beef rounds when processed into sectioned and
formed steaks. All rounds were defatted and cut into 2-3 cm
pieces; one group of rounds was blade tenderized twice. Each
group was divided into 18 kg meat blocks and assigned to
treatments of vacuum and non-vacuum mixing. The groups were
further divided into 9 kg blocks and allocated to 0 and 0.5%
added salt. Salt was incorporated into the product by
sprinkling it over the meat during the first 30 sec of
mixing. Each block was sampled after 0, 8, 16, and 24 min
blending. Samples were stuffed into plastic bags, crust
frozen at -30C and pressed into logs in the shape of a strip
loin. Steaks 2.5 cm thick were cut, vacuum packaged and
frozen for futher analysis. All steaks for sensory
evaluation were oven broiled in a rotary hearth oven. The


18
oven was set to maintain an internal temperature of 150C,
and steaks were cooked to an internal temperature of 70C.
Analysis of beef steaks indicated that the percentage of ash
and salt was significantly higher in the 0.5% salt
treatments. Moisture, protein, fat percentage and pH were
not different for blade tenderization, vacuum mixing or salt
addition treatments. Mean fat content of the final product
was 1.65%. The percentage of fat measured during the various
mixing times was highest at 0 min and lowest at 8 min. The
authors indicated that fat accumulated on the sides of the
blender as mixing time progressed. Twenty-four minutes of
mixing time was reported to yield the lowest cooking loss
23.8% compared to 27.5% for 0 min of mixing time. The TBA
values increased due to salt addition over a 90-day frozen
storage period, but did not change due to mixing time. A
significant interaction between blade tenderization and salt
addition for TBA values was reported. Products that were not
subjected to blade tenderization and no added salt had the
lowest TBA value of 0.77 compared to a value of 1.03 when
salt was added. Blade tenderization, regardless of added
salt content, resulted in higher TBA values compared to
non-tenderized products. The authors indicated that blade
tenderization increased the surface area of the meat,
allowing oxygen to be more accessible to the cut surfaces. A
significant interaction between vacuum and salt level was
also reported to exist, whereby removal of oxygen by vacuum


19
mixing resulted in a lower TBA value (0.83), compared to no
vacuum mixing (0.90) in steaks processed with 0.0% added
salt. The effect of mixing time on binding strength
indicated a 60% increase in particle adhesion as mixing time
increased from 8 to 16 min. Tenderness, as measured by the
Kramer shear cell, increased with increasing mixing times.
The authors indicated that the increase in tenderness
associated with increased mixing time may be an advantage
when restructuring with lower quality meats. Sensory
evaluations for initial tenderness were more desirable
following 8 min of mixing. However, tenderness desirability
decreased with 16 and 24 min of mixing. The authors
theorized that increased protein exudate content, extracted
as a result of increased mixing time, may have produced a
case hardening effect on the product surface.
In a similar study, Booren et al. (1981b) investigated
the influence of muscle type on characteristics of sectioned
and formed beef steaks. The processing procedures for
product preparation were equivalent to the one described for
their previous experiment (Booren et al., 1981a), with some
exceptions. In this study (Booren et al., 1981b), a coarsely
ground lean meat source was obtained from beef rounds of "A"
maturity, Standard grade carcasses. A fat meat source was
obtained from the plate region of the corresponding beef
carcass. Beef plates were sliced thin to permit formulating
a steak product to contain 12% fat. They reported similar


20
results as described by their previous study (Booren et al.;
1981a). Cooking yields increased with increased mixing
times, from a low of 70.55% at 0 minutes to a high of 77.35%
after 18 minutes of mixing. Flavor and juiciness sensory
scores also increased with increased mixing time. Longer
mixing times accelerated the rate at which the fresh
(uncooked) meat color deteriorated. The product made from
beef top rounds and beef plates was found to be more tender
and to contain less connective tissue residue as measured by
sensory panelists, when compared to their previous experiment
(Booren et al., 1981a).
Muscle Selection Criterion
One of the primary objectives of producing a
restructured meat product is to enhance the economic value of
lower valued meat cuts and trimmings. Traditionally, the
beef chuck has been a wholesale cut of lower economic value
when compared to the round, loin or rib. The wholesale beef
chuck represents approximately 27% of the beef carcass and is
typically merchandised at the retail level in the form of low
priced roasts and steaks, or as ground chuck (Paterson and
Parrish, 1986). The lower economic value associated with the
chuck is due in part to compositional and palatability
differences that occur within and between many of the muscles
that make up the chuck. Numerous researchers have documented
significant differences in connective tissue content,


21
contractile status, and intermuscular fat between the many
muscles comprising the chuck (Ramsbottom et al., 1945;
Ramsbottom et al., 1947; Prost et al., 1975; Zinn et al.,
1970; Marsh, 1977; McKeith et al., 1985; Paterson and
Parrish, 1986) .
Marsh (1977) cited the contractile status of the muscle
fiber and the collagen content (connective tissue) of the
muscle as two primary structural components responsible for
variation in muscle tenderness. The muscle fiber component
is termed myofibrillar toughness, and it is thought to
respond to the handling procedures from the time of slaughter
(Rowe, 1977). It is this muscle fiber component that is
considered to be responsible for changes in meat tenderness
resulting from cold shortening, aging, Tenderstretching and
electrical stimulation. The contractile status of a muscle
refers to the sarcomere length of an individual muscle fiber.
A decreased sarcomere length caused by cold shortening is
associated with an increase in muscle toughness. Increasing
the sarcomere length of a muscle beyond its normal resting
length would be associated with stretched muscle fibers and
an increase in muscle tenderness.
The influence of connective tissue content, relative to
meat texture has been extensively reviewed by Tahir (1979).
Meat is classified as tender or less tender principally on
the basis of connective tissue content (McCrae and Paul,
1974). Connective tissue toughness is usually referred to as


22
background toughness and is regarded as not being
significantly influenced by treatments applied to the meat
from the point of slaughter up to the point of cooking (Rowe,
1977).
Collagen is the major protein in connective tissue and
was considered to be the single major factor influencing meat
tenderness (Tahir, 1979). However, Doty and Pierce (1961)
concluded that collagen content was not significantly related
to tenderness. In addition, Carpenter et al. (1963) found no
significant relationship between tenderness measurements and
the total amount of connective tissue.
Certain physical properties of collagen change with age.
The total quantity of collagen in muscle does not increase
with the age of the animal (Goll et al., 1963). However, the
number of crosslinkages between the collagen molecules within
the connective tissue increase with age. As the degree of
crosslinking increases, the structural stability of the
tissue increases. This increase in structural stability
decreases the ability of collagen to become solubilized
during thermal processing thereby influencing the tenderness
of the meat (Goll et al., 1963). Two types of crosslinking
structures are known to occur. Intramolecular bonds occur
within the collagen molecule, and intermolecular bonds link
one triple helix to another (Sims and Bailey, 1982). The
function of the intramolecular crosslink is as yet unknown;


23
however, intermolecular crosslinks provide the mechanical
stability of the collagen fiber.
Collagen contains a unique amino acid profile that is
high in glycine and hydroxyproline. Together, they comprise
about half of the total amino acids found in collagen (Sims
and Bailey, 1982). The presence of the amino acid
hydroxyproline in collagen (about 14%) is thought to be
confined almost exclusively to the stromal proteins of
collagen and elastin (Gross and Piez, 1960). Because of the
unique distribution of hydroxyproline in collagen, its
presence has been used as a means of determining the amount
of collagen present in tissue (Sims and Bailey, 1982).
Sensory and chemical analysis for moisture and fat
percentage, sarcomere length and total collagen content of
thirteen major beef muscles from the round, loin, rib and
chuck were reported by McKeith and co-workers (1985). The
infraspinatus, triceps, supraspinatus and deep pectoral were
evalulated from the chuck. Sensory panel tenderness scores
and Warner Bratzler shear force values (WBS) indicated that
the infraspinatus was the most tender and that the deep
pectoral was the least tender. From the 13 muscles
evalulated, only the psoas major (tenderloin) was ranked
higher than the infraspinatus in overall tenderness. Mean
collagen content of muscles from the chuck, round, loin and
rib were 11.44, 8.94, 5.33, and 4.66 (mg/g wet tissue basis),
respectively. Muscles from the round and chuck had lower


24
sensory scores than muscles from the loin and rib. However,
fat percentage, sarcomere length and collagen content from
each muscle were not significantly correlated to palatability
traits (McKeith et al., 1985). Although not determined in
the previous study, the authors concluded that soluble
collagen content may be a more important factor relating to
meat tenderness than total collagen content. In addition,
these authors concluded that some muscles would have a
potentially greater economic value if they were separated
from the wholesale primal and used independently.
Smith and coworkers (1978) reported on the tenderness of
20 different muscles from the chuck and other wholesale cuts.
They also indicated that the infraspinatus muscle when
prepared as a steak or roast had lower (more tender)
Warner-Bratzler Shear (WBS) values than the longissimus dorsi
from the chuck or rib. Results from these two studies
(McKeith et al., 1985 and Smith et al., 1978) indicate that
boning line production techniques should be developed and
implemented so as to facilitate removal of the more desirable
muscles from the chuck. Current industrial practices of
whole-muscle boning and merchandising boxed beef make single
muscle groups available to consumers and processors.
Therefore, knowledge of the palatability characteristics of
these muscles combined with current restructuring or
reforming technology could improve consumer acceptance of the
final product.


25
The serratus ventralis (SV) muscle is located
immediately ventral to the rib bones of both the wholesale
rib and chuck. The SV is a large, fanshaped muscle that
contains both surface and internal septums of connective
tissue. The SV contains about 10% fat and is one of the
larger muscles comprising approximately 5% of the wholesale
chuck (Huffman and Cecchi, 1986). The SV is intermediate in
palatability characteristics of the major chuck muscles
(Paterson and Parrish, 1986). However, no reports regarding
the characteristics of the latissimus dorsi (LD) have been
found. This large, thin muscle lies on the outside of the
plate and extends into the chuck. The LD is approximately
half the size and weight of the SV and contains about 5%
intramuscular fat.
Both the SV and LD muscles provide an excellent source
of raw material from which a reformed whole-muscle beef
product could be produced. Currently these two muscles are
not being used to their greatest economic potential. In
addition, both muscles are unipennate, with fibers oriented
in one direction, and contain mainly surface connective
tissue. Also, these muscles comprise a major portion of the
forequarter and differ compositionally in internal fat
composition (>10% and <5% for SV and LD, respectively) (Recio
et al., 1988) .


26
Muscle Protein Functionality
Muscle protein functionality denotes any physiochemical
property that affects the processing and behavior of protein
in food systems as judged by the quality attributes of the
final product (Hand, 1986). Three major protein
functionality interactions have been reported to occur in
processed meat products: 1) protein-water; 2) protein-lipid;
and 3) protein-protein (Acton et al., 1983; Acton and Dick,
1984; 1985).
It is generally accepted that the myofibrillar proteins,
actin and myosin, are the primary proteins that provide the
structural stability to processed meat products. Although
many other myofibrillar proteins are present in meat tissue,
their quantity and contribution to structural stability in a
processed meat product is insignificant. The ability to bind
meat pieces back together in a restructured meat product is a
heat induced phenomenon involving protein-protein
interactions (Asghar et al., 1985). Several researchers have
attempted to explain the mechanism by which meat binding
occurs.
Hamm (1966) studied the changes that occur in meat
proteins during cooking and concluded that thermal processing
caused the helical portions of the protein molecules to
denature into random chains. These unraveled proteins were
postulated to produce random crosslinkages that may be
responsible for binding.


27
Vadehra and Baker (1970) and Hotter and Fischer (1975)
theorized that the mechanism of binding involves structural
rearrangement of the soluble proteins. This resulted in a
loosely ordered protein structure that allowed the proteins
to become more reactive during thermal processing.
The extraction of myofibrillar proteins is required to
facilitate binding of meat pieces. The binding properties of
purified muscle proteins were studied by MacFarlane et al.
(1977). They determined the binding strength of myosin to be
superior to that of actomyosin at salt concentrations up to 1
M. However, increasing the myosin concentration did not
result in increased binding strength (MacFarlane et al.,
1977; Siegel and Schmidt, 1979a). Siegel and Schmidt (1979a)
concluded that the decreased binding associated with
increased myosin concentrations implied ionic interactions in
binding. MacFarlane et al. (1977) further reported that, in
the absence of salt, the binding strength of myosin was
enhanced by incorporating sarcoplasmic proteins. The
contribution of sarcoplasmic proteins to the binding strength
was reported to be similar to that for salt. However, it was
reported that as salt concentrations increased, the
sarcoplasmic proteins exerted a deleterious effect on the
binding strength of myosin. This was attributed to the
adsorption of denatured sarcoplasmic proteins onto the
myofibrillar protein molecules, which resulted in decreasing
the availability of the binding sites.


28
Theno et al. (1978a) studied the binding junctions of
thermally processed sectioned and formed ham products. Their
research detected the presence of aligned elements occurring
within the binding junctions of the meat pieces. Siegel and
Schmidt (1979b), in an effort to determine the mechanism of
binding between meat pieces, described the ultrastructure of
a crude myosin gel as affected by salt, phosphate, pH and
temperature. They concluded that the mechanism of binding
meat pieces involved the following events. Intact
myosin-heavy chains are extracted to the muscle surface where
they combine with heavy myofilaments located on or near the
surface of the muscle cells. This results in producing super
thick synthetic filaments that bind the meat pieces together.
Formation of super thick filaments at higher temperatures was
stated to be possible because heavy chains are freed from the
parent molecule at lower heating temperatures due to salt
solubilization (Siegel and Schmidt, 1979b).
From this discussion it becomes evident that the
mechanisms involved in binding meat pieces together are
multifaceted. The heat-induced protein-protein interactions
are influenced by salt, ionic strength, protein type and
protein guantity.
Mechanisms of Protein-Water Interactions
Myofibrillar proteins are primarily responsible for the
binding of water in muscle and that different types of water


29
and water binding occur in muscle tissue (Hamm, 1975a).
Fennema (1985) presented a classification system for water
occurring in food systems. Type I water, also referred to as
bound water, is the mono- and possibly the bimolecular layer
of water surrounding proteins and other substances having an
electrostatic charge affinity. Type I water is present in
small quantities (4.5% of total water), unfreezable, and
displays little mobility. Type II or restricted water exists
as multiple layers surrounding the bound Type I water. Type
II water is subject to freezing and can be removed by drying.
Type III water or free water represents the major portion of
water located in animal and plant tissues and is subject to
easy removal. Type IV water refers to water in the pure
state and does not naturally occur in biological matter.
Because Type I water is bound and Type IV water does not
naturally exist in muscle tissue, the types of water that are
of interest from a food processing standpoint are Types II
and III. Therefore, a primary objective of meat processing
is to reduce the amount of water in the free state (Type III)
and increase the amount in restricted (Type II) state.
Variations in water content can result from gains that
occur during processing (in the form of added water), or
losses from improper chilling, drip, evaporation or cooking.
Such gains or losses are important for two reasons: first,
economics (since meat is sold by weight); and second,
consumer satisfaction, (the juiciness and tenderness of meat


30
and meat products depends to a great extent on their water
content). Additionally, subsequent water losses that occur
during cooking act to reduce the edible portion size (Offer
and Trinick, 1983).
Hamm (1960) defined water-holding capacity as the
ability of meat to hold its own or added water during
application of any force (pressing, heating, grinding). Hamm
(1975b) defined swelling or water binding ability as the
spontaneous uptake of water by meat from any surrounding
fluid, resulting in an increase in muscle weight. Although
the forces that restrict the mobility of loose water are not
well understood, the factors that influence changes in the
water-holding capacity of meat have been described (Hamm,
1960; 1966; 1975a,b). Hamm (1975b) described the swelling of
muscle fibers in terms of colloidal chemistry. The amount of
water immobilized within the tissue is influenced by the
spatial molecular arrangements of the myofibrillar proteins,
or filaments, of actin and myosin (Hamm, 1975b). Decreasing
the cohesion between adjacent molecules or myofibrillar
filaments by increasing the electrostatic repulsion between
similarly charged groups or by weakening of hydrogen bonds,
causes the network to enlarge or swell. Increasing the
degree of swelling increases the amount of water that can be
immobilized within the filamentous network, thus
water-holding capacity increases. However, a continued
decreasing of intermolecular cohesion will result in network


31
collapse, and the gel becomes a colloid solution of
myofibrillar proteins. Increasing the electrostatic
attraction of oppositely charged groups between adjacent
molecules can produce new interlinking bonds. This results
in less space being available for the retention of
immobilized water. Therefore, when the myofibrillar network
tightens as a result of applied pressure, heat, or grinding,
shrinkage occurs. This causes part of the immobilized (Type
II) water to become free (Type III) water and flow out of the
product (Hamm, 1975a).
Wierbicki and Deatherage (1958) offered the following
hypothesis regarding the forces that immobilize and bind
water. The highly polar water molecules are attracted to the
muscle proteins by ionizable basic and acidic amino acids and
by polar nonionic amino acids.
Offer and Trinick (1983) redefined water-holding
capacity (WHO) as the ability of meat to retain its natural
water content. Their studies reported on the mechanism of
water holding in meat and the swelling and shrinking of
isolated myofibrils, which provided evidence that myofibrils
were able to swell to at least twice their original volume
using salt concentrations that are commonly used in the
processed meats industry. These authors suggested that
myofibrils were the site of water retention. In their study,
Offer and Trinick (1983) made the same basic assumptions as
Hamm (1960), i.e., that as chloride concentration increased,


32
chloride ions became bound to network filaments. This
interaction increased the repulsive force between filaments
and tended to cause expansion of the network lattice.
However, Offer and Trinick (1983), in their discussion of the
mechanism of water holding in meat, stated that Hamm's model
was not complete for two reasons. It did not consider that
only a part of the myofibril (the A-band) was solubilized, or
the high degree of structural order of the myofibrils (Hand,
1986). Their reasoning was based on the fact that myofibrils
occupy about 70% of the volume of lean meat, and the degree
of observed swelling was related to the amount of water
retained as a result of meat processing. An additional
factor supporting their claim was that the binding of water
to the surface of protein molecules was too small to account
for the observed changes in water content (Hamm, 1960). This
was also based on a protein content of 20% and the belief
that proteins only bind water to an extent of 0.5g of
hydration water per gram of protein (Kunz and Kauzmann,
1974). Therefore, water that is actually bound to protein
molecules represents a small fraction of the total water
present.
Offer and Trinick (1983) concluded that the transverse
linkages, more specifically the cross-bridges, act to
restrain myofibrillar expansion. They indicated that the
influence of attached cross-bridges could be removed in one
of two ways: 1) disruption of the thick filament (myosin)


33
backbone, would result in disrupting mechanical continuity
and 2) detachment of the cross-bridges from the filaments.
The concentration of sodium chloride (0.4 M) required to
yield maximum swelling was less when pyrophosphate (0.8 M)
was used compared to its absence. However, pyrophosphate did
not alter the maxium extent of swelling. Increasing the
concentrations of sodium chloride and/or pyrophosphate were
shown to 1) displace the equilibrium existing between the
myosin filament and the myosin molecules, in favor of the
myosin molecules and 2) decrease the binding strength of
myosin heads to actin molecules. These actions function to
remove effectively the influence of the protein-protein
cross-bridges and act to increase water-holding capacity.
The authors also reported that maximum myofibrillar swelling
occurred when a substantial part of the A-band had been
extracted, providing further evidence that a large degree of
myofibrillar swelling could occur under conditions where more
than half of the protein was lost.
In summary, the mechanisms of protein-water interactions
are complex. They involve chemical bonding, charge repulsion
and attraction forces, as well as molecular and structural
arrangement. As a result, all of these factors interact to
influence the water-holding capacity of the meat product.


34
Influences on Protein-Water Interactions
In a review of the factors influencing water-holding
capacity of proteins, Acton and co-workers (1983) indicated
that most factors function in one or more of these three
ways: 1) the ionization and charge density of the protein
(tissue pH); 2) the extent of physical tissue disruption
(particle size); and 3) the distance the water is located
from the protein surface.
pH influence
The relationship of muscle pH to water-holding capacity
is well understood (Briskey, 1964; Dutson, 1983; Honkel et
al., 1981a,b). The relationship of WHC to pH is a function
of the myofibrillar proteins losing their affinity for water
as the pH approaches the isoelectric point for the given
protein (Szent-Gyorgyi, 1960) The decrease in pH that
accompanies postmortem glycolysis of muscle tissue has an
important bearing on meat quality. The final pH attained is
called the "ultimate pH" and for many mammalian species this
is close to a pH of 5.5 (Hultin, 1985). When the ultimate pH
of meat (5.3 to 5.5) approaches the isoelectric point (5.2)
of actomyosin, the WHC of the muscle is decreased (Dutson,
1983). However, when the ultimate pH of beef remains
elevated approximately 1.0 pH unit above the normal
postmortem pH (5.3 to 5.5), more water is retained or bound.
Meat of this type appears darker in color and is referred to


35
as "dark cutting beef." The ultimate pH attained by beef
muscle has been reported to influence the quality and
textural properties of the meat (Dutson, 1983). He concluded
the ultimate pH of meat affected color development, marbling
perception, WHC, cooler shrinkage, texture, cooking loss,
tenderness and processing characteristics of comminuted and
restructured meats.
Bouton and co-workers (1975) reported a threefold
increase in tenderness scores for mutton at pH 7.0 when
comparing an ultimate pH of 5.9 to 7.0. These authors noted
that the amount of juice centrifugally expressed from a
cooked meat sample had a high positive correlation with
sensory organoleptic juiciness scores and increased linearly
with pH.
Sodium chloride influence
There exists a broad variety of salts found in nature,
but because of taste and toxicological considerations, the
two most commonly used in meat products are sodium chloride
and the sodium salts of polyphosphoric acids (Trout and
Schmidt, 1983) The addition of salt to meat has a
multi-functional affect. Salt was initially used as a
preservative to retard bacterial spoilage. Today, the
primary role of salts in a meat system is to influence the
ionic strength and alter the pH of the system (Trout and
Schmidt, 1983).


36
Closely related to water-holding capacity is the ability
of meat to absorb additional water at elevated salt
concentrations; this was termed water-binding capacity by
Hamm (1982). Salt concentrations of 0.8 to 1 M (4.6 to 5.8%)
sodium chloride (NaCl) have been reported to yield maximum
water uptake (Offer and Trinick, 1983). However, a somewhat
lower NaCl level (2%) is more often used in the manufacturing
of processed meat products. Hamm (1960) concluded that the
chloride ion (Cl~) from NaCl was the ion responsible for
myofibrillar swelling, as the ions from sodium acetate failed
to induce swelling. It was theorized by Hamm (1960) and
again by Offer and Trinick (1983) that if a substantial
number of Cl~ were bound to the filaments at high NaCl
concentrations, the negative charge on the filaments would
increase, resulting in an increased electrostatic repulsive
force that would induce filamental swelling. Offer and
Trinick (1983) further concluded that as the salt
concentration increases, the attachment of the cross-bridges
(actomyosin) weakened. At the same time, increased Cl~
binding causes increased electrostatic repulsive forces.
These authors concluded that as long as the cross-bridges
remain attached, the myofibrillar lattice network cannot
swell to the same degree, and that if the lattice does swell,
then the cross-bridges cannot remain attached. When the
lattice swells, the thick filament will depolymerize allowing
water uptake to occur.


37
The use of NaCl and phosphates in a restructured meat
product facilitates extraction of the salt soluble proteins
(Theno et al., 1978a). Salt and phosphate contribute to the
disruption of muscle fibers during mixing, solubilization of
the myofibrillar proteins and the production of an exudate
rich in solubilized proteins. Restructured products made
without added salt and phosphate did not possess the desired
textural properties and were rated as unacceptable by a
sensory panel. Theno and co-workers (1978a) demonstrated
that massaging raw meat for 24 hours without the addition of
salt and phosphate would not permit an acceptable binding
between meat pieces. The addition of salt or phosphate alone
was not sufficient to attain an acceptable binding, but when
both were used in the proper combination, there was a
positive synergistic effect on binding. However, Ford et al.
(1978), in an effort to reduce the added salt content of
restructured products, determined that additions of crude
myosin extracts with sarcoplasmic proteins had the ability to
bind meat pieces into a cohesive restructured product.
Further support of this work was reported by Siegel and
Schmidt (1979a) using isolated crude myosin extractions as a
binding agent between meat peices as stated previously.
Bard (1965) studied the influence of temperature, mixing
time, pre-rigor and post-rigor meat addition and level of
added salt on the extractability of salt soluble proteins
from muscle tissue. Temperatures in the range of -5 to 2C


38
provided maximum protein extraction and increasing mixing
times up to 16 hours increased protein extraction. Protein
was more readily extractable from pre-rigor meat than
post-rigor meat, and a sodium chloride content of 10%
extracted the greatest amount of protein. In contrast to
these findings, Gillett et al. (1977) reported the optimum
temperature for protein extraction to be 7.2C, with
extractability decreasing at 0C. However, this difference
is probably a result of the different experimental conditions
that existed between studies. Gillett et al. (1977) used a
shorter extraction time (6 min vs 30 min), a higher salt
concentration (6% vs. 3.9%) and a higher solvent to meat
ratio (3:1 vs. 2:1) than Bard (1965).
The addition of salt to processed meat products has also
been reported to increase the flavor, texture and/or
juiciness ratings of restructured steaks (Cross and
Stanfield, 1976; Huffman, 1979; Mandigo, 1974; Mandigo et
al., 1972; Neev and Mandigo, 1974; Schwartz, 1975). Salt has
been, and to many people still is, considered to be an
essential part of our everyday lives. However, research has
established a relationship between sodium intake and
hypertension (Altschut and Grommet,1980; Pearson and Wolzak,
1982). As a result, many health conscious consumers are
avoiding foods that contain elevated sodium levels, and in
particular, processed meat products. In response, meat
processors are reducing the sodium content of their products


39
by decreasing the amount of salt used during processing.
Reducing NaCl levels, however, has decreased the functional
properties and characteristics (water binding ability and
texture) of the product (Sofos, 1983; Trout and Schmidt,
1986). In an effort to regain some of the functional
properties without greatly increasing the sodium content of
the product, meat processors are utilizing food grade
phosphates (Trout and Schmidt, 1983).
Influence of phosphates
Mahon (1961) indicated that the type and amount of
alkaline polyphosphates added to meat would increase the pH
by 0.1 to 0.4 units. Trout and Schmidt (1983) theorized that
the alkaline nature of the polyphosphates was the primary
factor in producing the altered pH effect. However, when
NaCl was added, the pH of the meat system decreased by 0.1 to
0.2 units. These same researchers theorize that the effect
of NaCl on pH is due to the displacement of hydrogen ions by
sodium ions on the meat surface and that the liberated
hydrogen ions produce the change in pH.
The ability of phosphate compounds to enhance the uptake
of water by meat has been known for some time (Bendall,
1954; Hamm, 1960; Sherman, 1961; Ranken, 1976; Offer and
Trinick, 1983). Phosphates can be used to buffer, sequester
metal ions, and increase the ionic strength of solutions.
Phosphate compounds have also been reported to promote the


40
extraction of myofibrillar proteins from meat pieces (Kotter
and Fisher, 1975; MacFarlane et al., 1977; Siegel et al.,
1978a,b; Theno et al., 1978a,b,c; Offer and Trinick, 1983;
Trout and Schmidt, 1986) .
Phosphates are salts of phosphoric acid. The two
general classes of phosphates are orthophosphates and
polyphosphates (Shimp, 1983). Orthophosphates contain a
single phosphorus atom while the polyphosphates contain two
or more phosphorus atoms. Orthophosphates are made by
partial or complete neutralization of phosphoric acid with an
alkali source. This reaction replaces one or more of the
three available hydrogen atoms on phosphoric acid with alkali
metal ions (Shimp, 1983). Monobasic orthophosphates have one
hydrogen atom replaced with an alkali metal. Dibasic
orthophosphates have two hydrogen atoms replaced, and
tribasic orthophosphates have all three hydrogens replaced
with an alkali metal.
Polyphosphates are produced by heating mixtures of
orthophosphates to high temperatures causing them to condense
into phosphate chains. Pyrophosphate is the simplest
polyphosphate containing two phosphorus atoms, while sodium
hexametaphosphate is one of the largest containing 10 to 15
phosphorus atoms. Pyro- and tripolyphosphate are white
crystalline solids containing one or three phosphorus atoms,
respectively. When phosphorus atoms exceed three chain


41
lengths the atoms are no longer crystalline, but amorphous
structures, commonly called glassy phosphates.
Buffers have the ability to maintain a constant pH when
components of a different pH are added to the system.
According to Shimp (1983), orthophosphates provide the best
buffering capacity, while ability to buffer decreases as
chain length increases.
Sequestering metal ions refers to a chemical process of
tying up metal ions in solution so that the ions cannot
participate in chemical reactions. Long chain polyphosphates
are the best sequestering agents for metal ions such as
calcium and magnesium (Shimp, 1983).
The three basic chemical functions of phosphates-pH
buffering, sequestering metal ions, and polyvalent anionic
properties-provide many beneficial effects in food systems
(Shimp, 1983). These effects include color stabilization,
water binding, prevention of coagulation, texture
improvement, emulsification, dry acid leveling, fast curing,
nutritional enhancement, and easier processing (Shimp, 1983).
Pyrophosphate and tripolyphosphate are two common
phosphate compounds added to processed meat products. They
are used to reduce water loss during cooking and to improve
the texture of the product (Ellinger, 1972). Trout and
Schmidt (1986) stated that phosphates increase the functional
properties of meat products in one or more of the following
ways: (a) by increasing the pH and ionic strength of the


42
product; (b) by dissociating actomyosin into actin and
myosin; (c) by binding to the meat proteins. A
generalization or ranking of the ability of different food
grade phosphates to increase the functional properties of
meat occur in the following order: 1) pyrophosphate; 2)
tripolyphosphate; 3) tetrapolyphosphate; 4) hexametaphosphate
and orthophosphate (Bendall, 1954; Shults et al., 1972; Trout
and Schmidt, 1984; Trout and Schmidt, 1986).
Trout and Schmidt (1986) studied the effects of various
types of phosphates, at different pH and ionic strengths and
their ability to influence the functional properties of
restructured beef rolls. Semimembranosus muscles were
removed 48 hr postmortem and trimmed of all visual fat and
connective tissue. Initial pH of all muscles was between 5.4
and 5.8. Muscles were ground through a 2.5 cm plate and
mixed by hand. The additives used were deionized water (5%
of the product weight), sodium chloride and disodium
phosphate (as analytical reagent grade), and the following
food grade phosphates: tetrasodium pyrophosphate (PP), sodium
tripolyphosphate (TPP), sodium tetrapolyphosphate (TTPP) and
sodium hexametaphosphate (HMP). The treatments utilized the
six phosphate types, three ionic strength levels ((0.15,
0.29, and 0.43), and three pH levels (5.50, 5.95, and 6.35).
The phosphates were used at a constant ionic strength of
0.055 and the different ionic strengths were obtained by
varying the NaCl content. Product pH was controlled by


43
adding 1 M NaOH or HC1 during product mixing. Beef rolls
were thermally processed to an internal temperature of 70C
in an air agitated, thermostatically controlled retort.
Increasing the ionic strength (from 0.15 to 0.43) and pH
(from 5.50 to 6.35) produced increases in the cooking yields
and tensile strength. Both of these properties increased
linearly with increasing ionic strength and increasing pH
until reaching maximum values and then plateauing. These
maximum values occurred when the pH and ionic strength was
between 5.95 and 6.35 and 0.29 and 0.43, respectively (i.e.,
at NaCl concentrations between 1.7 to 2.5% and 1.4 to 2.4% in
the absence and presence of phosphates, respectively). The
majority of the increase in cooking yield (53%) was due to
the increase in ionic strength, while the increase in tensile
strength (26%) was attributed to the increase in pH. All
phosphate sources produced synergistic increases in cooking
yields and tensile strengths when ionic strengths were
greater than 0.15. The ability of phosphates to produce the
synergistic effects decreased as their chain length
increased. In addition, the ability of phosphates to
increase tensile strength at high ionic strengths could not
be reproduced simply by increasing the pH or by increasing
the ionic strength with only NaCl.


44
Water Distribution
Fresh meat at slaughter contains approximately 75%
water. The main structural component of meat is the
myofibril which occupies approximately 70% of the volume of
lean tissue (Offer and Trinick, 1983) The majority of the
water in meat is associated with the myofibrils, occupying
the spaces between the thick and thin filaments.
The tissue water of an animal can be divided into two
compartments: 55% intracellular (ICF) and 45% extracellular
(ECF). The extracellular space (ECS) is the fluid
compartment situated externally to the cells of the body
(Law, 1982). Law (1982) reviewed the techniques and
applications of determining ECS in mammalian tissues. The
ECS consists of the plasma component of the vascular space
and the interstitial fluid (Law, 1982). The volume of the
ECS within a tissue is calculated by adding the plasma
component to the interstitial fluid component.
Experimentally, this is determined by introducing a marker
molecule into the space and determining its concentration at
equilibrium. Law (1982) indicated a marker should have the
following characteristics: 1) ready and uniform distribution
throughout the entire anatomical ECS; 2) exclusion from the
cells; 3) no influence on the size of the ECS; 4) non-
metabolizable; 5) uniform molecular size and diffusion; 6)
easy and accurate estimation at low concentrations (i.e.,


45
involves use of radioisotopic labling); and 7) minimal loss
of the marker by urinary elimination or lymphatic draining.
Several different saccharides and ion molecules have
been tested in trying to satisify the requirements stated
above. Of these, the compound inulin (which is readily
available as the 3H-methoxy- or 14C-carboxylic acid compound)
has been the most widely used. Other radio labeled
saccharides that have been used include sorbitol, mannitol,
sucrose and raffinse.
The earliest reported attempts to measure ECS were those
of Fenn (1936) using tissue chloride levels. Although the
values obtained using this method were not grossly misleading
for whole body content or in tissues with low intracellular
chloride (e.g., skeletal muscle), they were unacceptable for
tissues with high concentrations of intracellular chloride
(e.g., intestinal, cardiac and vascular tissue) (Law, 1982).
Ions such as sulphate, bromide and iodide and compounds such
as thiosulphate and thiocyanate have been evaluated and found
to occupy spaces greater than those available for markers of
higher molecular weight (Law, 1982). Law (1982) indicated
that under a given set of physiological conditions, a unique
anatomical space will exist and the measured ECS will
decrease as the molecular weight of the marker increases.
This was explained on the basis that markers of high
molecular weight fail to penetrate fully the ECS or that
lower molecular weight markers penetrate the cell. Thus,


46
several factors are capable of contributing to the over- or
under-estimation of the ECS.
Law (1982) concluded that no conclusive evidence
currently exists that recognizes an ECS marker as being
rigidly excluded from cells. Also, in isolated tissue slices
in which markers do not have to cross a capillary wall, the
marker is not able to penetrate instantaneously the ECS.
This is viewed as a problem in classical equilibration
experiments. The measured ECS may also be over-estimated due
to the entry of marker into damaged peripheral cells. The
use of tritiated markers (3H) has presented some problems
because of their known ability to exchange H-atoms in
functional groups, resulting in an overestimation of the ECS.
Williams and Woodbury (1971) indicated that inulin may also
become bound by connective tissue causing an over-estimation
of the ECS. A lack of, or a reduction in, the normal
proportion of oxygen in skeletal muscle during ECS
measurements has been reported to cause measurable increases
in the interfiber space (Law, 1967). Law (1967) used an
oxygenated saline solution containing rat muscle to study the
distribution of 14C-labeled sucrose. Histological
examination of these muscles indicated distorted muscle fiber
patterns which were interpeted as indicating severe
physiological deterioration of the muscle. It was concluded
that even though previously oxygenated Ringer's solution was
utilized, tissue hypoxia was responsible for this occurrence,


47
and doubted the validity of such a method as a means of
extracellular space examination.
Law (1982) indicated several factors that could
contribute to an under-estimation of the ECS. Under
estimation normally occurs when the marker is not adequately
able to penetrate the ECS, or it does so at a very slow rate.
Ogston and Phelps (1961) reported that hyaluronic acid-rich
mucopolysaccharides present in connective tissue create a
partial resistance to inulin and possibly other large
markers, effectively reducing the ECS estimate. The use of
highly charged markers to estimate ECS, e.g., sulphate, may
be impeded or exaggerated by the presence of fixed charges
within the tissues (Law, 1982).
A variety of techniques, independent of or complimentary
to the use of marker molecules, have been reported for
estimation of the ECS. However, these alternative methods do
not seek to express ECS in precise quantitative terms. The
value of these methods lies in their ability to a) detect
rapid changes and b) to visualize small but significant
changes in specialized areas of the ECS (Law, 1982). These
methods include 1) autoradiography to follow uptake of
inulin (Stirling, 1972), 2) light or electron microscopy to
determine total tissue ECS outlined by chemical markers
(Prosser et al., 1960), and 3) electrical resistivity or
potential differences that rapidly occur in the dimensions of
lateral cellular interspaces (Schultz et al., 1974).


48
To date, the majority of mammalian skeletal tissue
studies designed to study ECS have relied on one of the
following methods: tissue perfusion, in situ or in isolation,
or determination of washout kinetics following marker
equilibration in nephrectomized animal models. The
equilibration procedures involves soaking or incubating small
muscles or strips of muscles in a Ringer-lactate solution
containing 0.3% inulin according to the procedure of Heffron
and Hagarty (1974), modified by the use of low oxygen tension
or incubating muscle strips in 14C-inulin as described by
Vaccari and Maura (1978).
Heffron and Hagarty (1974) studied the rate at which
fiber diameter changed during the development of rigor mortis
in the biceps brachii of the mouse. They reported a 14 to
16% decrease in fiber diameter when the muscle entered rigor,
followed by an increase in ECS. In addition, total muscle
volume (fibers + ECS) did not change during rigor
contraction. Measurements of the ECS determined at 1, 2, 3,
4 and 24 hr postmortem indicated increases of 49.7, 76.7,
83.5, 135.7 and 432.9 % respectively in ECS. The authors
concluded that the decrease in fiber diameter when the muscle
entered rigor mortis was associated with a depletion in ATP.
The authors describe two hypotheses to explain their results.
The first hypothesis was that ATP may act as a "plasticizer"
for the sarcolemma in the same manner it does for the
myofibrils, and that fiber shrinkage or contraction results


49
when ATP supplies are completely exhausted. The second is
that the interfiber fluid becomes hyperosmotic soon after
death, causing movement of the intrafiber water to the ECS
and resulting in a decrease in muscle fiber diameter.
A study designed to relate changes in the mechanical
properties and ECS of beef semitendinosus and biceps femoris
muscles during the onset of rigor mortis was presented by
Curri and Wolfe (1980). It was suggested that intrafiber
water was a significant factor contributing to the tensile
and adhesive properties of muscle; it should be considered as
equally important as the state of contraction and the
collagen angle of the connective tissue network when
assessing muscle tenderness. They presented the following
hypothesis to convey the importance of intrafiber water to
muscle tenderness: during early post-mortem, muscle pH is
high, water-binding capacity of the contractile proteins is
high and ATP levels are high. This results in low tensile
and extensibility properties. As the pH drops, the
water-binding capacity of the proteins decreases. In
addition, the ECS was shown to increase as rigor progressed
until pH 5.9, which agreed with observations of Heffron and
Hegarty (1974). Associated with this increase in ECS was an
increase in the tension and extensibility. Curri and Wolfe
(1980) indicated that the initial increase in ECS was
expected, but the occurrence of a brief unexpected decrease
in ECS near pH 5.95 followed by another increase in the ECS


50
back to its previous volume was not expected. In an
explanation of this occurrence, the authors hypothesized that
the release of Ca2+ from the sarcoplasmic reticulum or other
Ca2+ containing organelles within the fiber created a
hyperosmotic intracellular region, causing water to move from
the ECS back into the fiber. The secondary increase in ECS
was attributed to the continuing decline in pH. As the pH
continued to decline, the isoelectric point of the
sarcoplasmic and contractile proteins was approached, causing
some proteins to undergo denaturation and lose their ability
to bind water. The increase in "loose" water intracellularly
could cause a dilution effect of the Ca2+ ion and the
extracellular region becoming hyperosmotic again. This would
promote water movment out of the fiber and into the ECS. The
information obtained from these experiments helped to explain
the observed changes in tensile and adhesive measurements
that occur during the onset of rigor mortis.
The reagent grade inulin used in their previous work
(Currie and Wolfe, 1980) was not pure enough to provide
reasonable value estimations for the ECS and over estimated
the volume. To overcome this drawback, Currie and Wolfe
(1983) utilized the ECS procedure of Vaccari and Maura
(1978). Highly purified inulin [14C] carboxylic acid was
used as the extracellular marker to determine the location of
water in the post-mortem muscle. Incubating muscle strips in
inulin [14C] carboxylic acid provided a means in which to


51
assess the functionality of the muscle membranes. The
authors expressed hope that this research would provide an
avenue through which the variations in water-holding capacity
and the interfilamental spacing of meat and thus meat quality
could be futher advanced.
Heat-Induced Changes in Meat
It has been established that the heating of muscle
tissue during processing or cooking changes the chemical and
physical composition of muscle proteins and that these
changes influence the palatability characteristics of the
final product. When meat is heated to a certain temperature
range, the proteins in the muscle cells undergo
denaturation/coagulation with a subsequent loss in solubility
(Hamm and Deatherage, 1960; Hamm/ 1977; Cheng and Parrish,
1976; Leander et al., 1980; Moller, 1981; Martens et al.,
1982). "Denaturation" is a change in the specific steric
conformation of a protein, i.e., a change in the secondary
and tertiary structure without a chemical modification of the
amino acids (Hamm, 1977). Fennema (1985) described
denaturation as a process in which hydrogen bonds,
hydrophobic interactions, and salt linkages are broken and
the protein unfolds. A protein molecule in its natural state
consists of a backbone chain of amino acids intertwined in a
'native'1 structure. The native molecules may exist in
solution (i.e., sarcoplasmic proteins in meat) or as natural


52
aggregates (i.e., myofibrillar proteins and collagen fibers).
Intramolecular forces function to hold the native protein
structure together. However, these forces can become
strained or broken as the ambient temperature of the protein
increases, leading to thermal denaturation. Heat induced
protein denaturation does not occur as an "all or none"
process, but rather as a continuous process with various
regions of the protein molecule changing at different rates
depending on the rate and duration of heating (Paul and
Palmer, 1972). The application of heat to a native protein
structure is said to cause chain unfolding. Unfolding the
chain exposes the interior of the previously protected
internal chain which results in changing affinity for other
molecules (Martens et al., 1982). Thus, denaturation is
considered to be a physical process and not a chemical one.
When protein affinity increases, the degree of aggregation
between protein molecules will increase. Depending on the
physical properties of the native protein, the precipitating
or coagulating particles will form strong, continuous,
water-binding gels, as in egg white (Hegg et al., 1979).
However, if the affinity decreases, a solubilization of the
native components may result. Martens et al. (1982)
concluded that increases or decreases in affinity were
dependent upon which affinity was mechanically stronger.
In a meat protein system, the denaturation of protein
structures may result in changes in the physical properties


53
of meat such as water holding capacity (WHC), thermal
diffusivity, heat conductivity, porosity, etc. The influence
of heat on the structural components of meat has been the
subject of a number of studies (Hamm and Deatherage, 1960;
Trautman, 1966; Hamm, 1966; Hamm, 1977; Cheng and Parrish,
1976; Bouton et al., 1981; Bouton and Harris, 1981; Moller,
1981; Martens et al., 1982; Ziegler and Acton, 1984a,b).
Hamm (1966) reported on various physical and chemical changes
that muscle tissue undergo as it is heated from 20C to above
80C. Heating of beef muscle produces a stepwise series of
physical and chemical changes as it undergoes thermal
denaturation. From 20 to 30C, no changes occurred in the
physical or chemical properties of muscle proteins. Heating
from 30-50C resulted in an increase in tissue pH and
rigidity, followed by a decrease in water-holding capacity.
During heating, peptide chains initially undergo an unfolding
process, yielding new unstable cross-links which results in a
tighter protein structure. Between 50-55C rearrangement of
myofibrillar proteins continues, and newly formed cross
linkages become stable. At 65C most of the myofibrillar and
globular muscle proteins are coagulated. Collagen shrinks at
temperatures around 63C and may be practically transformed
into gelatin. Between 70C and 90C disulfide bonds are
formed due to the oxidization of sulfhydryl groups
originating from actomyosin. Disulfide bond formation
continues to occur with increasing temperatures between 70


54
and 90C. Above 90C, hydrogen sulfide (H2S) is split off
from the sulfhydryl groups of actomyosin and collagen is
transformed to gelatin, resulting in an increase of
tenderness.
Hamm (1977) reviewed the changes muscle proteins undergo
during heating of meat. Heating actomyosin to temperatures
above 40C removed the Ca2+ sensitivity of actomyosin, which
resulted in an increase in ATPase activity. The heating
effect on actomyosin ATPase was theorized to be responsible
for producing conformational changes in the actomyosin
complex. The temperature of maximum ATPase activity was
reported to occur between 43 and 47C, however increasing
the temperature above this range resulted in inactivation and
irreversible denaturation. Heating actomyosin to 60 to 70C
produced an increase in sulfhydryl (SH) groups. The increase
in SH group content was thought to occur as a result of an
unfolding of the protein molecules during heating. The
temperature at which actomyosin begins to release SH groups
was reported to coincide with the temperature at which
maximum ATPase activity and maximum change in conformational
changes occurred (45C). Increasing the temperature to 70C
did not produce additional SH groups, but between 70 and
120C the total number of SH groups was reported to decrease
as a result of oxidation of SH to disulfide (SS) groups.
Heat coagulation of myofibrillar proteins was not considered
to occur as a result of SH oxidation, but rather as a result


55
of intermolecular association of other side-groups on the
molecules. In summary, between 30 and 50C, the
myofibrillar proteins undergo an unfolding of the protein
molecule, followed by protein coagulation and a loss of
enzyme activity.
Because isolated myofibrillar proteins might not respond
the same as those in the intact fiber, Hamm (1977) reviewed
the changes incurred during the heating of muscle fibers or
tissue. At temperatures between 40 and 60C, myosin
proteins reportedly broke down into smaller compounds, while
actin molecules underwent changes in its helical structure.
Myofibrillar proteins reportedly underwent their greatest
decrease in solubility at temperatures between 40 and 60C
and became essentially insoluble at temperatures above 60C.
This decrease in protein solubility coincided with a decrease
in Ca2+-activated ATPase and Mg2+-activated ATPase in
myofibrils. However continuous heating for 7 hr at 55C did
not result in complete solubilization. It was concluded that
the temperature range yielding the maximum change in
solubility seemed to be about the same in the intact muscle
fiber or the isolated state. However, ATPase activity did
not follow this trend. ATPase activity decreased faster in
solution than in the muscle fiber when stored at 35C.
Heating of muscle from 30 to 70C increased the number of SH
groups, indicating an unfolding of the protein molecules as
previously observed for isolated myosin and actomyosin. The


56
relative changes in SH and SS groups occurring in meat was
considered to be important because 97% of the SH and SS
content of muscle tissue is bound to myofibrillar proteins.
At temperatures above 80C, SH and SS content decreased due
to oxidation to cysteic acid or by the splitting off of H2S.
The amount of H2S released increases exponentially with
increasing temperatures. In addition, the amount of H2S
produced increased significantly as the fat content of the
meat increased. Problems arise when the the production of
H2S occurs during the heating of processed canned meat
products. H2S can corrode the interior of a tin can,
discolor the contents and produce an unfavorable or offensive
smell when the can is opened.
When muscle tissue was heated to temperatures between
40 and 60C, the pH of the system increased in a manner
similar to that reported for myofibrillar proteins.
Associated with the shift in pH is a simultaneous shift in
the isoelectric point of the myofibrillar proteins (when
measured as the pH at which water-holding capacity is at a
minimum). The increase in pH and isoelectric point was
reportedly due to an increase in available basic protein
groups. It was theorized that some imidazolinium groups of
histidine are initially masked in the native myofibrils, and
become uncovered as actomyosin unfolds due to heating (Hamm,
1977).


57
The decrease in myofibrillar solubility between 30 and
60C was attributed to the unfolding of the protein chain
followed by protein coagulation. Protein coagulation was not
attributed to the formation of SS bonds resulting from SH
group oxidation because coagulation occurred at temperatures
below the temperature at which the formation of SS begins.
The influence of pH on the water-holding capacity of raw meat
and meat heated to between 30 and 50C revealed the presence
of unstable cross-linkages. These occurred between unfolded
protein chains that tightened as the isoelectric point of the
proteins was approached (Hamm, 1977).
Hamm (1977) in the same review also reported on the
changes that connective tissue proteins undergo when
subjected to heat. Collagen fibers shrink from a quarter to
a third of their initial length at 60C while at higher
temperatures collagen is transformed into water-soluble
gelatin. Although meat contains several types of connective
tissue proteins, collagen is considered to be the most
important thermolabile protein of this type because of its
ability to influence the eating quality of the final product.
Paul (1963), Hamm (1966) and Draudt (1972) theorized
that heat-related changes which influence meat tenderness
result from two opposite effects. First, the changes that
connective tissue undergoes apparently has a tenderizing
effect and second, hardening of myofibrillar proteins imparts
a toughening effect. Dutson and co-workers (1976) utilized


58
two muscles that had been stretched to various sarcomere
lengths (1.35-2.60 um and 1.70-3.25 um) and differed in
collagen content (13.13 and 2.47 mg collagen/g of muscle).
Differences in tenderness of these muscles were related to
differences in connective tissue content at all sarcomere
lengths measured. This finding was thought to be due to a
shortening of both connective and muscle tissue fibers, which
resulted in decreased muscle tenderness, whereas in the low
connective tissue muscle, only the shortening of muscle
fibers influenced tenderness. Martens et al. (1982)
concluded that the resultant strength of connective tissue in
meat was dependent upon several factors: the amount of
collagen in the sample (as influenced by animal type and
muscle type), the case of collagen gelatinization during
heating (varied with the age of the animal) and the method of
cooking in terms of time and temperature. Lawrie (1985)
reported myofibrillar tenderness to be dependent on several
factors: the extensibility of fibrils
(stretching/shortening) as influenced by the state of rigor
mortis contraction, pH of post-rigor muscle and time and
temperature used to cook meat.
Deng et al. (1976) hypothesized that protein
denaturation produced an intramolecular swelling and
structural loosening of the protein as opposed to an
unfolding of the protein structure. The shrinkage of tissue
and the release of juice during heating of muscle tissue is


59
due to changes in myofibrillar proteins. Hamm and Deathrage
(1960) and Hamm (1960, 1966) studied WHC of muscle protein as
a function of temperature. The WHC started to decrease
slightly at 30C, decreased significantly between 40 and
50C, remained constant from 50 to 55C, decreased again in
the range of 55 to 70C, and was considered to be at its
lowest level at 80C. However, later reports indicate that
weight loss from meat started to be significant at 60C or
higher (Bengtsson et al., 1976; Nykvist and Decareau, 1976;
Godslave et al., 1977a,b). This implies a weak relationship
between weight loss and WHC.
Bengtsson et al. (1976) measured temperature and water
distribution in bovine semimembranosus muscle as functions of
cooking time. Muscles were oven roasted at 175 or 225C
from initial temperatures of -20 and +5C. Temperature
profiles as related to heating time were reported, as were
corresponding moisture and fat content profiles. Moisture
and temperature profiles were inversely related to each
other, with temperature minimum and moisture mximums
occurring near the sample center. Fat content had no
significant influence on any parameters measured. Heating
time was shorter and yield was lower at 225C than at the
175C cooking temperatures. Cooking time increased 50% when
cooking from the frozen state. Weight loss was reported to
occur almost entirely by evaporation from the product surface
up to 65C. Above 65C, weight loss became significant due


60
to liquid drip. Time/temperature profiles of weight loss for
thin slices of meat indicated that cooking temperature was
more important than the time required to produce the first
drip loss. The importance of this issue to meat tenderness
warrants additional detailed discussion.
Godslave et al. (1977a) studied water emission rates and
the mechanism of water loss (drip) from the surface of frozen
bovine semitendinosus muscle samples during oven roasting
(dry heating) temperatures between 121C and 204C and an air
flow rate of 13.7 m3/h. Muscle fiber direction was oriented
parallel to the direction of air flow within the cooking
environment. The moisture (drip) emission rate data
contained two constant rate periods followed by a falling
rate period. In general, moisture emission rate curves for
the samples exhibited peaks rather than plateaus, and in both
studies, temperature and time were found to be related to the
amount of weight lost (Godslave et al., 1977a). The
magnitude and duration of both the first and second constant
rate periods were reported to be dependent on the oven
temperature. Oven temperatures of 177C or 204C produced
greater water emission rates that were shorter in duration
when compared to oven temperatures of 121C or 149C. The
first constant rate period occurred when the surface
temperature of the product was 100C. This was said to
produce moisture loss resulting from water vaporizing from a
boiling front that moved slowly inward. The second constant


61
rate period began when the protein at the interior of the
sample started to heat denature in the temperature range of
57C to 67C. The water released by denaturation flowed to
the surface of the sample. This action was said to wash out
the effect of the inwardly traveling boiling front and more
surface evaporation. The second constant rate period was
reported to end and the first period begin again when the
weight ratio of water to protein decreased to two. During
this time period water was still evaporating near or at the
product surface but the fraction of wetted surface was
continuously decreasing. The second falling rate period
started when the weight to water ratio was approximately one
(Godslave et al., 1977a). The rate at which the falling rate
period occurred was temperature dependent, with the higher
temperatures approaching zero more rapidly (Godslave et al.,
1977a).
A basis for understanding water emission behavior from
muscle tissue during cooking has been provided by Godslave et
al. (1977a). Muscle was viewed as a wet porous medium with
protein forming the porous matrix and water the wetting
fluid. Water emission from cooking muscle (as a heated
porous medium) occurs when protein transformation gives rise
to an increase in water mobility and matrix shrinkage. In
porous material, water flows by capillary action such that
inside a porous body there exists a complicated network of
interconnected pores and passages with some opening to the


62
surface of the solid. When the solid is wet, the pores are
filled with water. During drying, water evaporates from the
surface at the mouths of pores. This process produces a
meniscus at the product surface that draws water from the
internal network to the exterior of the solid by surface
tension forces. Hence, a smaller pore with a large meniscus
curvature will have a greater interfacial tension capable of
drawing water from the larger pores. Thus, during drying the
larger pores will drain first, provided they do not collapse
on themselves and the empty pores will fill with air.
Because the amount of moisture in a solid is finite, there
comes a point in time when the larger pores run out of water
and the water layer on the surface starts to recede into the
sample in the vicinity of the larger pores. Therefore as the
drying process procedes, air occupies more of the pore space
and eventually the water no longer covers the walls of the
pores with a continuous film. As a result, pool structures
occur within isolated areas of the pore network (Godslave et
al., 1977a). Knowledge of the processes that influence the
rate at which heat penetration occurs within a meat product
is important to minimize the energy required for thermal
processing and yield losses.
Hung (1980) using a modified version of the oven
previously utilized by Godslave et al. (1977a,b), studied the
relationship of water loss to muscle shortening and protein
denaturation during oven roasting of frozen bovine


63
sexnitendinosus muscle. Muscles were cut into cylindrically
shaped samples with fibers oriented parallel to the axis of
the cylinder. Two sample sizes were used, 100 g and 600 g.
The respective dimensions (length x diameter) of these
samples were 10.8 cm x 3.49 cm for the 100 g sample and 19.1
cm x 6.35 cm for the 600 g sample. In agreement with the
previous work of Godslave et al. (1977a,b), Hung (1980)
concluded that increasing the oven temperature increased the
amount and rate at which water was lost. However, the amount
of weight loss was not dependent on the orientation of the
sample fibers. Because of this finding, it was hypothesized
that the majority of weight loss was not due to the effect of
gravity. Hung (1980) also reported observing two distinct
drip periods which agreed with previous reports by Godslave
et al. (1977a,b). During the first drip period, the drip
amount for vertical or 45 oriented samples was greater than
for horizontal samples. It was suggested that, it is more
difficult for water to migrate across the fibers than along
the fibers and that gravity played a role in determining the
amount of drip in this period. When previously frozen
samples were allowed to partially thaw, only one drip period
occurred. The amount of drip was small, red in color and
appeared viscous and turbid. Hung (1980) concluded that the
first drip period occurred when the interfiber ice crystals
near the surface or cut ends thawed. Part of this liquid was
absorbed by the muscle fibers, and the rest migrated parallel


64
in the direction of the fibers or reached the bottom and/or
ends of the sample where it either formed a drip or
evaporated. If the rate of thawing is slow compared to the
rate of absorption, it is possible that absorption could be
sufficiently effective to pick up most of the thawed liquid.
According to Ramsbottom and Koonz (1939) and Wang et al.
(1954), if meat samples are rapidly frozen (e.g., -150C),
both interfiber and intrafiber ice crystals occur. If the
meat samples are slowly frozen (e.g., -17C), only interfiber
freezing takes place and the muscle fibers are partially
dehydrated. Slow freezing also results in larger ice crystal
formations, which can act as tiny knives to cut or rupture
myofiber cell membranes and contribute to muscle dehydration.
During the second drip period, the drip was clear and
evaporated explosively when contacting the pan. Thus it was
considered to be composed mostly of water. Meat surfaces
appeared dry, or at least partically dry corresponding to the
first peak of the drying curve. However, as the cooking
process continued, liquid drops appeared on the previously
dry surface and continued to grow until they dripped from the
sample. Hung (1980) implied that the liquid drops were
squeezed out of the meat samples due to shrinkage and
gravity. As muscle protein is heat denatured, the rate of
mass transfer increases greatly, possibly due to 1) cracking
across muscle fibers and 2) damage to muscle cell membranes
(Paul, 1963; Davey and Gilbert, 1976).


65
Changes in tenderness of meat that occur during cooking
are considered to be influenced by heat-induced changes in
the myofibrillar and stromal structural protein components of
muscle tissue. In mammalian skeletal tissue, the myofibrillar
proteins, i.e., actin and myosin, constitute 50 to 55% of the
total protein. Myosin is the predominant protein in prerigor
meat, whereas actomyosin is the predominant protein complex
in postrigor meat. The fibrous actin and myosin in
myofibrils can be histologically identified in raw and cooked
(time and temperature dependent) muscle samples. Hung (1980)
employed transmission electron microscopy (TEM) to evalulate
structural changes that occurred during cooking of bovine
semitendinosus muscle and found a normal distribution of
sarcomere lengths for raw samples (mean = 2.5 microns).
However, a two peak distribution for cooked samples appeared
at 2.05 microns and 1.55 microns. These peak values
suggested that two chemical reactions were involved in
sarcomere shortening. The first reaction caused a decrease
of sarcomere length from 2.5 urn to 2.05 um. The second
reaction caused a shortening from 2.05 um to 1.55 um and was
thought to be responsible for water loss during cooking.
Cooked muscle samples that contained long sarcomers had
fibrous looking I-bands (actin filaments), while short
sarcomeres contained nonfibrous looking I-bands. The two
sarcomere distribution peaks that were previously described


66
(2.05 and 1.55 microns) were reported to represent the two
types of I-band structures (fibrous and nonfibrous).
Disruption of myofibrils upon heating has been reported
(Giles, 1969; Jones et al., 1977; Hung, 1980; Leander et al.,
1980). Myofibrillar breaking points were reported either at
Z-I junctions (Giles, 1969; Hung, 1980; Leander et al., 1980)
or at A-I junctions (Giles, 1969; Jones et al., 1977).
Therefore, breaks in myofibrils occurring during heating are
thought to involve the I-band region of a sarcomere (perhaps
at the weak link point).
Draudt (1972) suggested that heat acted to solubilize
connective tissue providing a tenderizing effect, while
toughening myofibrillar proteins. These changes were
temperature dependent, such that myofibrillar protein
coagulation offsets the tenderization effect of any
additional collagen solubilization at temperatures above 60C
and results in a decrease in tenderness of beef cooked beyond
the rare to medium-rare state.
Numerous researchers (Machlik and Draudt, 1963; Bouton
and Harris, 1972a,b; Davy and Gilbert, 1974; Hamm, 1977;
Bouton and Harris, 1981) have reported that meat tenderness
was greater at final internal temperature of 60C than at
50C. Draudt (1972), in a review, stated that the decrease
in shear force value that occurred as internal temperature
increased from 50C to 60C was due to the shrinkage of
collagen. However, Bouton and Harris (1972b) concluded that


67
the effect was dependent on the age of the animal and related
it to changes in connective tissue strength. Davey and
Neiderer (1977) suggested that heating muscle tissue to 65C
increased proteolytic enzyme activity and improved meat
tenderness by reducing myofibrillar tensile strength.
Futhurmore, heating to temperatures above 65C improved
tenderness through a reduction in the structural contribution
of the connective tissue. From this discussion, it is
obvious that some disagreement exists between the earlier
work of Machlik and Draudt (1963), Bouton and Harris (1972b)
and Davey and Gilbert (1974). It has also been reported by
Bouton and Harris (1981) that Warner-Bratzler (WB) shear
force values decreased for veal muscles as cooking
temperatures were increased from 50C to 60C. Increased
proteolytic enzyme activity at these temperatures, which may
produce an accelerated aging condition, did not appear to
explain the effect since there was a substantial decrease in
shear force when cooking temperatures were increased from
50C to 60C, even when the meat had been aged (7 wk at
5-6C) or when cooked for 24 hr. Bouton and Harris (1981)
concluded that even at these relatively low temperatures,
changes in connective tissue were involved since: 1) the
magnitude and direction of the changes in shear force with
increasing temperature was dependent on animal age and
cooking time, and 2) the effects of increasing cooking
temperature and/or time on the adhesion strength between the


68
meat fibers was significantly greater for samples from
younger animals.
The most dramatic changes that occur in meat as a result
of heating are the shrinkage and hardening of tissue, release
of juice and discoloration caused by changes in the muscle
proteins (Hamm, 1977).
Cheng and Parrish (1979) used SDS-polyacrylamide gel
electrophoresis to study the heat induced changes in the
solubility of myofibrillar proteins from bovine longissimus
muscle. Muscle samples were diced (particles size of 1 cm3),
placed into glass test tubes and heated in a water bath to
45, 50, 55, 60, 70, and 80C and held at the designated
temperature for 30 min. In addition, a control (raw) muscle
sample was also included for comparison. The heated and
control muscle tissues were homogenized and the myofibrillar
proteins extracted with 25 ml of 0.6M KC1, 0.1M K phosphate,
pH 7.4 for 1 hr and centrifuged at 15,000 x G for 15 min.
Because the control (raw) sample and samples heated to 45,
50, and 55C contained residue of unheated protein, 1 mM
MgCl2 and 1 mM sodium pyrophosphate were added to aid in
suspension and separation of the protein supernatant. The
SDS-polyacrylamide gels indicated that the extractability of
actin, myosin and Z-disk myofibrillar proteins react
differently to heat. The heavy and light chains of myosin
were reported to be the first major proteins to become
insoluble at 55C. This was in agreement with the earlier


69
work of Locker (1956) who heated purified myosin and reported
that 82 to 92% of the protein became coagulated at 53C.
However the thin filament proteins, including actin,
tropomysin and troponin T and I, became more extractable with
heating and were reported to be more heat resistant than
myosin. Troponin T and tropomyosin bands were more intensive
between 45 and 60C than in unheated samples or samples
heated at 70 or 80C, indicating their ability to resist
denaturation. The appearance of a 30,000 dalton component
within the gels was used as an indication that troponin T had
been degraded. The presence of this 30,000 dalton component
was reported to occur in samples heated at 55 and 60C. The
observation that this 30,000 dalton component was more
prominent after heating led the authors to conclude that
calcium-activated factor (CAF) activity was stimulated during
heating. Actin was reported to become insoluble between 70
and 80C and tropomyosin and troponin became insoluble above
80C. In response to these findings the authors theorized
the following possible explanations: a) the loss of
alpha-actinin solubility at 50C results in weakening the
I-Z-I protein bonds and allows release of thin-filament
proteins; b) because actin was still soluble and myosin
insoluble at 55C, a weakening or dissociation of the thin
filament proteins occurred allowing their release into
solution; and c) the action of CAF activity on Z-disks
permits an increase in the extractability of thin filament


70
proteins. It was concluded that the state of the Z-disk and
thin filament proteins were a major factor to be considered
when determining the level of tenderness in bovine
longissimus muscle. Knowledge of these changes and the study
of protein denaturation are important when trying to
understand the mechanisms by which heat and mass transfer
occur in meat during heating.
Microwave Heating
Copson (1975) and Decareau (1985) provides an excellent
source of basic references for heating with microwaves and
microwave power engineering. Together these two books
provide invaluable background information regarding microwave
heating properties as related to food.
Decareau (1985) described microwaves as a form of low
frequency non-ionizing electromagnetic energy, like radio and
television waves. In terms of frequency, microwaves lie
between television waves and infrared waves. The two ISM
(Industrial, Scientific and Medical) frequencies assigned by
the FCC (Federal Communications Commission) for microwave
heating in the U.S. are 915 and 2450 MHz. Microwaves are
capable of penetrating materials such as wood, water and
food. In addition, they are capable of passing through air,
vacuum, glass, paper and some plastics such as teflon.
However, they are reflected by metals or perforated metals
with holes much smaller than the wavelengths of the


71
microwaves. A 3.2 mm hole (1/8 inch) in metal is small
enough to reflect 2450 MHz microwaves.
Hung (1980) described the three basic components
contained within a microwave heating apparatus: the
generator, the waveguide assembly and the cavity. The
generator is considered to be the major part of the microwave
oven. Two types of microwave generating tubes are presently
used: the klystron and the magnetron. The klystron tube
possess higher or stronger power than a magnetron.
The waveguide is a rectangular piece of metal tubing
that transmits the power from one end to the other. A
waveguide assembly can be either a single component or a
combination of several components. Each component can be a
waveguide equipped with particular microwave hardware
capable of controlling or monitoring microwave transmission.
The design of the cavity is related to the uniformity of
the microwave field in it. The cavity is the chamber that
accepts the microwave energy and holds the product that is to
be heated. Another device associated with the cavity is
called a mode stirrer and functions to improve distribution
and uniformity of the microwave field. It consists of a
rotating metal fan that acts to reflect and distribute the
microwaves that contact it.
Electromagnetic waves produced by microwave ovens are
rapidly absorbed by water molecules present in food. This
form of energy is transformed into a random thermal motion of


72
water molecules. A water molecule will rotate in the
presence of the electric field of a microwave oven due to the
electric charge within the molecule. Walker (1987) offered
the following explanation on the physics of microwaves and
the water molecule. The electrons associated with hydrogen
atoms are shifted toward the eight protons in the oxygen
atom. The shift leaves the oxygen end of the molecule
negative and the hydrogen ends positive, resulting in a
charge distribution called an electric dipole. Normally the
dipole moments in water are randomly oriented. If an
electrical field is imposed, however, it creates a torque on
each molecule. The torque causes the molecule to rotate in
an effort to align its dipole moment with the imposed
electrical field. Therefore, a microwave oven operating at a
frequency of 2450 MHz attempts to rotate a water molecule at
2.45 X 109 rotations per second, and as a result the
temperature increases. Bakanowski and Zoller (1984)
described how this heating process occurs within foods. Some
molecules within food are electrically polarized and will
respond to the applied electromagnetic field by oscillating
in synchronization with it. These molecules are electrically
coupled to the rest of the food, and through this coupling,
the energy of oscillation is passed on as an increased
thermal motion. If the source of the electromagnetic field
is removed, the polar molecules stop oscillating in
synchronization with the field and no additional heating


73
occurs. However, a redistribution of the heat already
deposited will occur as a result of temperature gradients
established during the microwave heating. The redistribution
of heat results from thermal conduction and is not due to
microwaves "left behind" after the magnetron is turned off.
In a microwave oven when the magnetron is turned off, the
production of microwave energy ceases to exist in both the
oven and the food.
Microwave ovens have only been on the market for a
little more than two decades, yet they appear to have
revolutionized the way Americans prepare food. Microwave
ovens have opened up a new dimension in food preparation and
management both in the home and in food service processing.
In 1984, the largest annual shipment of any home appliance in
history was claimed for microwave ovens at 9.1 million units
(Markov, 1985a). In a survey of 2000 American households
nationwide, nearly 60% had microwave ovens, while about 50%
had dish washers (MRCA, 1987).
The greatest advantages of microwave cooking are its
time and energy savings. Meat can be cooked four or five
times faster and require approximately 75% less energy in
comparison with conventional methods (Moore et al., 1980;
Hoffman and Zabik, 1985). Markov (1985b), in an overview,
reported of the microwave oven market concluded that
excellent meals could be prepared with microwave technology.
However, the majority of consumers reported that they use


74
their ovens primarily for reheating and defrosting of foods.
The microwave has not been well accepted by homemakers and
food services for reheating or cooking of muscle tissue due
to uneven cooking, greater cooking losses, and less palatable
meat (Markov, 1985b). It is important to realize that the
microwave heating characteristics of a food product may vary
considerably with the processing frequency, temperature,
chemical composition, and physical state of the product
(Mudgett, 1982).
In developing products for microwave processing,
Schiffmann (1986) stressed that microwaves are a form of
energy, not a form of heat. The energy is only manifested as
heat upon interaction with a material as a result of one or
more energy transfer mechanisms. The heating of materials by
microwave energy is influenced by the oven equipment and the
material being heated (Schiffmann, 1986). Designing a
microwave cooking process involves understanding the thermal
properties of the food in question, and a number of
interrelated electrical properties. These properties vary
extensively with the processing frequency and product
time-temperature profiles which can affect transmission of
microwave energy at the products surface and energy
absorption by the product (Mudgett, 1986).
In a review, Schiffmann (1986) indicated the following
factors that must be considered when developing a
product/processing system: processing frequency, power


75
level, moisture content, product density, product geometery,
conductivity properties and specific heat of the product.
The depth to which microwave energy is capable of
penetrating into a food product is dependent upon the
frequency used to produce the electromagnetic microwave
energy. The primary difference between heating at 915 MHz
and 2450 MHz is in the differing penetration depths. The 915
MHz frequency has a longer wavelength which produces a
greater effective penetration depth of 33 cm compared to 12.2
cm for the shorter 2450 MHz frequency. Microwave energy at
915 MHz has an initial advantage in penetration depth but
loses penetration depth as the temperature of the product
increases. Nykvist and Decareau (1976) stated that 44 times
more energy reached the center of a 12 cm thick beef slab at
915 MHz compared to 2450 MHz. The frequency selected is
important, because it relates to the size of the object being
heated. In general, a large 220 kg block of frozen material
would be processed better at 915 MHz, while cooking an
individual sausage patty should be done at 2450 MHz.
The speed of microwave heating (power output) is usually
controlled by varying the power level setting. The speed or
rate at which microwaves heat is often the most attractive
feature of microwave heating. However, it is possible to
heat too rapidly, such that heat can be generated faster
than the product can keep up with it. When this occurs, the
outer regions of the product become over heated, which


76
results in excessive loss of product moisture and decreased
palatability. Another problem associated with excessive
heating rates is non uniform temperature distribution. This
occurs because the heating rate may be so fast as to prevent
effective thermal conductivity of the heat to the cooler
interior regions. The author suggested "heating fast; but as
slow as possible" (Schiffmann, 1986).
Nykvist and Decareau (1976) studied the effect of roast
diameter (6 to 14 cm) on the resulting temperature profiles
when appling 275 W of effective heating power generated at
915 MHz or 2450 MHz. These researches concluded that greater
energy dissipation occurred near the roast surface for the
2450 MHz frequency, resulting in higher surface temperatures,
in less power penetration and less energy being "focused"
and in relatively low center temperatures. However, for 915
MHz as the surface heated up the penetration depth decreased,
thus decreasing the amount of energy reaching the roast
center. From these results it would appear that to attain
optimum microwaving conditions for meat entrees the product
should initially be heated at 915 MHz to attain interior
heating followed by 2450 MHz for surface heating. The
authors stated that methods that promoted radial (uniform)
microwave penetration, such as a perfect cylindrical shape
roast would provide a more uniform temperature profile.
Schiffmann (1986) also agreed that the physical geometry
(size and shape) of a product influences the heating


77
properties of the product in several ways. He indicated that
the size of an individual product should be considered when
selecting a microwave frequency for heating. For example,
915 MHz would be more effective at thawing a 200 kg block of
meat because of greater penetrating characteristics than to
2450 MHz which produces greater surface heating. In
addition, sharp edges and corners should be avoided because
of their tendency to overheat. Schiffmann (1986) stated that
cylindrical shaped products tend to avoid this problem and
should therefore be considered when designing a microwavable
product.
The moisture content of a product is considered to be
one of the most important factors influencing how well the
product will absorb microwave energy. Usually, the more
water present in a product, the higher the dielectric loss
factor will be for the product. This should result in
superior heating of the product. At very low moisture
levels, the water is considered bound and not available to be
affected by the rapidly alternating microwave field. Product
density affects the dielectric constant properties and hence,
the heating of the product. As the density of the material
increases, so does its dielectric constant.
The transmission properties of electromagnetic energy
relate to the depth of penetration from the product surface
inward. Penetration depths are reported to increase as the
moisture content of the product and processing frequency are


78
decreased. Very porous materials, such as bread, because of
the air inclusions, are considered good insulators. As a
result heat transfer into these products is difficult and
slow.
The conductivity of a product describes the ability of a
material to conduct electric currents by displacing electrons
and ions. In a microwave system, dipolar rotation is the
most frequently discussed means of generating heat. The
presence of sodium chloride ions in the water matrix of a
product acts to increase the heating rate. When sodium
chloride dissociates in water, the positive and negative ends
of a water molecule are electrically attracted to the charged
ions. The electric field of a microwave drives the hydrated
ions through the water, pushing the sodium ions in the
direction of the field and the chloride ions in the opposite
direction. Whenever hydrated ions bump into water molecules,
energy is transferred, and the water is subjected to
additional heating.
The specific heating properties of a product can cause a
material which has a relatively low dielectric loss value
(low water content) to heat well in a microwave field. An
example of this effect is the ability of oils to heat faster
than water because of their lower specific heat.
The dielectric properties collectively reflect the
ability of a material to store and dissipate electrical
energy and, consequently, determine the product's ability to


79
act as an insulator. However, most foods are poor
insulators. As a result, they typically absorb a large
portion of the energy produced in a microwave field. Energy
absorption by the product is said to be instantaneous and
causes internal heating of the product. As a result the
dielectric properties and subsequent cooking properties of
food products in the liquid or semisolid state depend
primarily on their moisture, salt, and solid contents (Kent
and Jason, 1975,* Mudgett et al., 1980; Mudgett, 1982).
Microwave cookery has been shown to decrease cooking
time, labor and energy costs, but has not been well accepted
by food services or homemakers for cooking beef roasts due to
uneven cooking, greater cooking losses, and less palatable
meat when compared to conventional heating methods (Headley
and Jacobson, 1960; Marshall, 1960; Kylem et al., 1964; Law
et al., 1967; Ream et al., 1974; Drew et al., 1980; Moore et
al., 1980; Griffin et al., 1981). In further support of
this, Taki (1986) reported that homemakers still approach
meat cookery in a microwave oven by a trial and error
approach.
The scientific literature on microwave cooking of beef
or other muscle tissues has not been overly complimentary.
Comparisons between microwave and conventionally cooked meat
has indicated differences in sensory attributes, cooked
yields, microbial quality, and physical or chemical
characteristics of the final product, depending upon the


80
cooking method (Pollack and Foin, 1960; Marshall, 1960;
Korschgen et al., 1976; Drew et al., 1980; Moore et al.,
1980; Bodrero et al., 1980; Zimmermann, 1983; Sawyer et al.,
1984; Sawyer, 1985).
Marshall (1960) reported on the use of an "electronic
oven" in meat cookery. In her study, paired five pound
pieces of choice grade top round of beef were roasted in an
"electronic oven" or in a conventional oven. The author
indicated that in previous studies utilizing the "electronic
oven" the internal temperature of the product would rise
approximately 11C after removal from the oven. Therefore,
roasts cooked in the "electronic ovens" were cooked fat side
down for one-half to two-thirds of the time and then turned
fat side up until an internal temperature of 80C was reached
and then removed. The other half of the paired roasts were
cooked in a 148C electric oven fat side up until an internal
temperature of 80C was reached. The average cooking time
for roasts prepared in the "electronic oven" was 23.5 minutes
per kilogram compared to 100.0 minutes for the conventional
oven. The author also indicated that the shape of each roast
was such that one end was smaller than the other. As a
result of this uneven shape, the small end on roasts prepared
in the "electronic oven" became excessively brittle and
porous and it was deemed unpalatable. In addition, the fiber
hardening effect was reported to occur along all of the edges
and corners of the these roasts. Cooking losses included


81
losses due to drip, evaporation, and trimming of cooked
surface fat. "Electronic oven" prepared roasts averaged
60.6% cooking loss compared to 34.7% for conventional
cookery. Appearance and palatability of the roasts as judged
by a six-member taste panel indicated that roasts prepared in
the "electronic oven" were rated lower in appearance,
tenderness, juiciness, and flavor when compared to those
cooked conventionally. The author concluded that a method of
cooking whereby a more satisfactory product is obtained is
needed before the "electronic oven" will be practical for
roasting top round of beef to a well-done degree of doneness.
Korschgen and coworkers (1976) compared quality factors
in beef, pork, and lamb cooked by microwave and conventional
means. Regardless of meat species cooked, microwave cooked
roasts were prepared in less than half the time required to
prepare conventionally cooked roasts. The cooking loss
percentage for all three species indicated that the greatest
losses occurred via evaporation. Microwave cooked beef had
a smaller cooking loss compared to conventional cooking,
while there was no difference between pork and lamb roasts.
Shear force values indicated no difference due to cooking
method for beef and lamb, however, microwave cooked pork
roasts had lower shear force values than conventionally
prepared roasts. Sensory analysis indicated that no one
cooking method was superior for all three species. Beef and
lamb samples were significantly less tender when cooked by


82
microwaves compared to conventional cookery. No meaningful
trends were apparent in sensory scores for juiciness across
meat species. However, the interior portion of
conventionally cooked beef roasts was scored significantly
juicier than were those from microwave cookery. The authors
concluded that aside from the time-saving advantage for
microwave cooking, there were no major advantages for
microwave cooking over conventional cooking.
Drew and coworkers (1980) compared the effects of
cooking top round beef roasts from the frozen and thawed
states at different microwave power levels and conventional
methods on energy consumption, cooking times, cooking losses,
and palatability. The microwave oven used in this study
operated at 2450 MHz and on power levels of "high" (553
watts) or "simmer" (237 watts). Conventionally cooked roasts
were prepared using a still-air electric oven set at 163C.
Roasts were cooked uncovered in the conventional oven and
were loosely covered with waxed paper when cooked in the
microwave oven. When compared to the conventional oven less
time was required to cook frozen or thawed roasts to the same
internal temperature when the roasts were cooked in the
microwave oven regardless of power level. Energy consumption
data indicated that about half as much electricity was
required to cook roasts in a microwave oven as compared to
conventional oven cookery. In addition, there was no
difference in the amount of electrical energy used between


83
"high" and "simmer" power levels. Cooking losses included
drip and volatile components and when added together yielded
a total cooking loss. Roasts cooked conventionally from the
frozen state had less drip (3%) and volatile losses (30.3%)
than microwave cooked roasts which had 5.6% and 36.4%,
respectively, for drip and volatile losses at high power and
8.4% and 29.2%, respectively, on low power. Roasts cooked
from the thawed state had less drip (8.3%) and volatile
losses (23.2%) than microwave cooked roasts which had 15.0%
and 26.4%, respectively, on high power. Total cooking losses
were significantly higher for roasts cooked at the "high"
microwave power level than for those cooked in a conventional
oven. However, when roasts were cooked at the "simmer"
microwave power level, the total loss was not significantly
different from those cooked in the conventional oven.
Sensory evaluation scores and shear force values for roasts
cooked from the thawed state did not differ for overall
acceptability, flavor, juiciness, and tenderness due to
microwave cooking method ("high" or "simmer") versus
conventional cooking. Roasts prepared from the frozen state,
regardless of cooking method had lower scores compared to
scores for thawed roasts. There was no difference between
conventional and microwaved "simmer" cooked roasts prepared
from the frozen state for sensory characteristics. However,
shear force values were lower for conventionally cooked
roasts than for roast cooked at either microwave power level.


84
In general, roasts cooked from the frozen state using "high"
microwave power had lower (less desirable) sensory scores
when compared to all other cooking methods.
Moore and coworkers (1980) studied differences among top
round steaks cooked by dry or moist heat in a conventional or
a microwave oven. The authors used a Gardner Color
Difference Meter to access the degree of doneness of each
steak and concluded that steaks were heated more evenly by
conventional dry heat than by conventional moist or by
microwave dry or moist heat. In addition, cooking time,
evaporative cooking losses, total moisture content, and
sensory juiciness and tenderness scores were less, and total
and drip cooking losses, and ether extract were greater for
steaks cooked by microwaves than for conventionally cooked
steaks.
Korschgen and Baldwin (1980) compared the quality of
beef rib roasts cooked by manually cycling a microwave oven
on and off so as to simulate the automatic cycling control
for microwave energy. Both microwave cooking methods were
compared to conventionally cooked beef rib roasts as a
control. Sensory panel scores indicated that regardless of
cooking method used, all roasts were deemed acceptable in
flavor and juiciness. Mean sensory scores for tenderness
indicated significantly lower (less desirable) scores for
roasts cooked by the manual pulsing procedure compared to
conventionally cooked roasts. There was no difference in


85
tenderness scores for automatically cycled microwave energy
compared to conventional cooking. Energy requirements were
lower and total cooking losses were higher for meat prepared
by microwave power regardless of cycling method (Korschgen
and Baldwin, 1980). The authors concluded that automatic
cycling permitted equilibration of heat developed within the
product. This transfer of heat within the product is due to
conduction from one region of the roast to another.
The issue of bacteria in food surviving in large numbers
after thermal processing by microwave radiation compared to
conventional hot air processing was studied by Sawyer and
coworkers (1984). The purpose of their study was to
determine the effect of plastic wrapping on the internal
end-point temperature and on the survival of bacteria in food
subjected to thermal processing in a microwave oven. Single
serving sized portions of chicken drumsticks, ham slices and
pork loin slices were cooked from the frozen state in a
microwave oven using 630 watts of power. Microbiological
counts of wrapped-vented and unwrapped foods were made before
and after microwave processing for Staphylococcus aureus
surface inoculated on to chicken drumsticks and ham slices.
Salmonella senftenbera surface inoculated on to ham and pork
slices indicated that wrapping did not have a statistically
significant effect on internal end-point temperature or on
counts of bacteria per gram of product tested. Wrapping
generally provided a slight improvement in microbial quality


86
when mean counts were considered. Schiffmann (1981) and
Ohlsson (1983) both indicated that the increased occurrence
of bacteria surviving in foods processed in microwave ovens
was due to a lack of a uniform microwave field. The lack of
field uniformity results in hot and cold spots occurring
within the microwave oven.
Zimmermann (1983) studied the effects of microwave
thermal processing on the survival of Trichinella spiralis.
the causative agent of trichinosis. In this study the author
indicated the difficulty in attaining 76.7C throughout a
pork roast when subjected to microwave thermal processing.
Zimmermann (1983), in an attempt to cook pork roasts in a
microwave oven to 76.7C, failed to do so 149 out of 189
attempts when following the oven manufactures and pork
industry recommendations. Zimmermann (1983) suggested that
low wattage cooking at 50% or less would give any trichina
present longer exposure to heat and, thus, provide an
approach to safe cooking methods. In this study some roasts
were still infective after cooking at 30% power for 46.2
t
min/kg. This research futhur emphasizes the lack of
uniformity in heat distribution in microwave cooked products.
In a recent report, Welke et al. (1986) evaluated the
effect of microwave, convection and conventional cooking
methods on the texture of top round roasts when epimysial
tissue from one to eight year old animals was physically
inserted into the roasts (approximately 2000 g each).


87
Results of their study were that Warner-Bratzler shear values
for old epimysial tissue cooked in the microwave oven was
lower than shear values for old epimysial tissue cooked by
convection or conventional ovens (5.0, 7.7, and 8.4 kg,
respectively). Roasts cooked by the microwave method
required significantly shorter cooking times than did roasts
cooked by convection or conventional methods (97, 146, or 186
min, respectively). Microwave and convection cooked roasts
cooked to an internal temperature of 63C experienced an 8C
post-cooking temperature rise over a 30-min period, whereas
conventionally cooked roasts were heated to an end-point
temperature of 71C. These authors suggested that lower
shear values from epimysial tissue from old animals for the
microwave method was due to an increase in collagen
hydrolysis when compared with convection and conventional
cooking methods. This supports the work of Law et al.
(1967), McCrae and Paul (1974) and Hutton et al. (1981), but
is in contrast to the theories of Van Zante (1973), Roberts
and Lawrie (1974) and Peckham and Freeland-Graves (1979) who
suggested that use of the microwave oven does not allow time
for collagen solubilization and tenderization. Factors to be
considered when producing a microwavable meat product are fat
percentage within the product and post-cooking temperature
rise. The effect of cooking method on fat percentage and
cooking yields for ground beef patties was reported by Berry
and Leddy (1984). Beef patties from ground round, ground


88
chuck and regular ground beef containing 14, 19, and 24% fat,
respectively, were cooked by six different methods and
analyzed for compositional differences. Percentage of
cooking yield, fat, and moisture of cooked patties were
significantly affected by the interaction of fat level and
cooking method. Except for patties cooked by broiling or
convection heating, patty yields decreased with increasing
fat levels. Microwave cooking always produced patties
containing the least fat and caloric content in comparison
with other methods since cooking losses were greater.
The duration and extent of post-cooking temperature
elevation in microwave cooking were reported by Ruyack and
Paul (1972), Sawyer (1985), and Welke et al. (1986). Ruyack
and Paul (1972) cooked choice beef semitendinosus muscles in
a 915 MHz, 1600 W microwave oven and reported a 2C/min
post-cooking temperature elevation in roasts covered with a
polyester film and an 1.6C/min increase in uncovered roasts.
Sawyer (1985) reported that experimental product processed in
a hot air oven did not exhibit post-cooking temperature
elevations. However, chicken frankfurters processed in a
microwave oven at 50% power had a 2.1C greater post-cooking
temperature elevation than frankfurters processed at 100%
power. It was concluded that the extent of post-cooking
temperature rise may be related to power level used during
processing. Thus, post-cooking temperature elevation may be
more commonly associated with microwave heating than with


89
conventional heating when time of processing is kept constant
(Ruyack and Paul, 1972).
When beef is cooked in a microwave oven, water heats the
solid material. However, the surface temperature never
reaches a temperature greater than 100C. This temperature
is not high enough to denature fully oxymyoglobin, thus the
surface never becomes dark brown. Also, the meat seldom
develops the flavor and aroma of meat cooked in a
conventional oven (Walker, 1987).
Even though microwave technology has made great strides
forward in the areas of increased speed, convenience and
futuristic computerized programmed appliances, this technical
sophistication has not been matched by the development of
beef entrees compatible with the microwave oven. A recent
survey indicated that one-third of the microwave oven owners
prepare more than three-quarters of their meals in their
microwave ovens and another one-fourth prepare more than half
of their meals that way (Taki, 1986). While consumers are
cooking more meals in their microwave ovens, research
indicates that the incidence of cooking meat entrees is
seldom (Taki, 1986).


CHAPTER 3
PREDICTING FINAL INTERNAL TEMPERATURE THROUGH THE USE
OF POST-COOKING TEMPERATURE RISE IN REFORMED BEEF ROASTS
COOKED WITH VARIABLE MICROWAVE POWER LEVELS
Introduction
As a result of changing life styles, consumers are
demanding convenience in meat entrees. One possibility is a
ready-to-cook roast beef product reformed from denuded chuck
muscle that can be cooked with microwave energy. Previous
work has indicated that microwave cooking of meat results in
greater cooking losses and less palatable meat than
conventional methods (Korschgen and Baldwin, 1976; Nykvist
and Decareau, 1976; Sawyer, 1985). Nykvist and Decareau
(1976) indicated that early research efforts on microwave
roasting of beef did not take into consideration the high
post-cooking temperature rise (PCTR) associated with
microwave roasting. As a result, roasts were often
overcooked when compared to controls, and therefore deemed
lower in palatability.
Moore et al. (1980) indicated that conventional oven
roasting of top round steaks with moist heat produced a 2C
post-cooking temperature rise compared to a 10C increase for
moist microwave cooking. Drew and coworkers (1980)
90


Full Text
PRODUCTION AND MICROWAVE THERMAL PROCESSING
CONSIDERATIONS FOR A PROTOTYPE REFORMED
ROAST MADE FROM THE BEEF FOREQUARTER
By
JOSEPH A. YATES
A DISSERTATION PRESENTED TO THE GRADUATE SCHOOL OF
THE UNIVERSITY OF FLORIDA
IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE
DEGREE OF DOCTOR OF PHILOSOPHY
UNIVERSITY OF FLORIDA
1988

This dissertation is dedicated
to my wife, Diana, and my son, Brandon,
whose never-ending love,
patience, and unselfish support
help make my dreams reality.
To my parents, Josephine and Joseph Yates,
my brothers, Christopher and Phillip,
and my mother-in-law, Betty Gene Mosel,
for their support and prayers,
throughout my college endeavors.

ACKNOWLEDGEMENTS
There were many people who assisted in the completion of
this project. The author expresses his appreciation to Dr.
Roger L. West, chair of the supervisory committee, and to Dr.
Rachel B. Shireman, cochair, for their guidance, supervision,
and contributions in preparation of this manuscript.
The contributions of Dr. S.C. Denham, Dr. D.D. Johnson,
Dr. J.W. Lamkey, Dr. F.W. Leak, Jr., Dr. M. Marshall, and Dr.
A. Teixeira are appreciated for the valued support,
encouragement, and assistance they provided during his
graduate program.
Appreciation is extended to Ms. Karen Christensen for
her support and willingness to help in getting this project
completed. Special thanks are also extended to Ms. Jannet
Eastridge, Ms. Debbie Neubauer, and Ms. Ana Zometa for their
technical help. I am very grateful to Mr. Larry Eubanks,
manager of the meat laboratory. Despite my impatience, his
friendship and expertise during this project have proven to
be invaluable. For his light-hearted attitude, while being
serious about his work, he will always be remembered.
iii

The author's appreciation is also extended to his fellow
graduate students for their friendship and assistance during
his graduate program.
The author wishes to extend his thanks to the Jet Net
Corporation and Viskase Corporation for their generosity in
providing equipment and supplies necessary for completion of
this research.
The author is grateful to the Beef Industry Council for
providing the monitary support required to conduct this
research.
Finally, his deepest thanks of appreciation and love are
extended to his wife Diana and son Brandon, for it has been
their never-ending encouragement that turned this dream into
reality.
iv

TABLE OF CONTENTS
Page
ACKNOWLEDGEMENTS iii
ABSTRACT vii
CHAPTERS
1 INTRODUCTION 1
2 LITERATURE REVIEW 8
Restructured Products 8
Manufacturing Considerations for Re¬
structured Beef Products 10
Muscle Selection Criterion 20
Muscle Protein Functionality 26
Mechanisms of Protein-Water Interactions.. 28
Influence on Protein-Water Interactions... 34
pH influence 34
Sodium chloride influence 35
Influence of phosphates... 39
Water Distribution 44
Heat-Induced Changes in Meat 51
Microwave Heating 70
3 PREDICTING FINAL INTERNAL TEMPERATURE THROUGH
THE USE OF POST-COOKING TEMPERATURE RISE IN
REFORMED BEEF ROASTS COOKED WITH VARIABLE
MICROWAVE POWER LEVELS 90
Introduction 90
Materials and Methods 92
Preparation of Sample 92
Microwave Cooking 94
Proximate Analysis 96
Statistical Analysis 96
Results and Discussion 98
Summary 116
v

Page
4 COMPARISON OF MICROWAVE AND CONVENTIONAL
COOKERY AND END-POINT TEMPERATURE ON CHEMICAL,
PHYSICAL, AND SENSORY PROPERTIES OF REFORMED
BEEF ROASTS PRODUCED FROM CHUCK MUSCLES 118
Introduction 118
Materials and Methods 121
Raw Material 122
Cooking Methods 123
Proximate Analysis and Sarcomere Length... 126
Shear Force 127
Bind Strength 127
Sensory analysis 128
Statistical analysis 129
Results and Discussion 130
Study 1 130
Cooking times 132
Cooking losses 138
Changes in sarcomere length 140
Proximate analysis 142
Texture measurements 144
Binding strength 146
Sensory evaluation 148
Study II 163
Overall Summary 170
APPENDIX INSTRON FORCE DEFORMATION CURVE 175
REFERENCES 176
BIOGRAPHICAL SKETCH 194
vi

Abstract of Dissertation Presented to the Graduate School
of the University of Florida in Partial Fulfillment of the
Requirements for the Degree of Doctor of Philosophy
PRODUCTION AND MICROWAVE THERMAL PROCESSING
CONSIDERATIONS FOR A PROTOTYPE REFORMED
ROAST MADE FROM THE BEEF FOREQUARTER
by
Joseph A. Yates
December 1988
Chair: R.L. West
Cochair: R.B. Shireman
Major Department: Animal Science
Latissimus dorsi (LD) and Serratis ventralis (SV)
muscles were removed from 48 USDA Choice, yield grade 3 beef
forequarters, processed into reformed roasts and used to
compare palatability, chemical and physical characteristics
resulting from conventional and microwave cooking. Equations
were developed for predicting the extent to which post¬
cooking temperature rise occurred within the roasts during
microwave cooking to control final internal end-point
temperature and allow comparison of methods.
Study I used a factorial arrangement to quantify changes
in meat components as related to heating rate (slow in
conventional vs fast in microwave cooking): three
replications by two roast types (LD and SV) by four cooking
methods (conventional, low, medium, and high power microwave
levels) by three end-point temperatures (60oC, 70°C, and
75°C). Study II used LD roasts in a factorial arrangement to
study changes in extracellular water space (ESC) as related
vii

to the method of heat production (conventional vs. microwave)
when heating rate was equivalent. Heating rates were made
equivalent by slowing the cooking rate in the microwave.
Results of Study I indicated microwave cooking required
less time than conventional cooking for all treatment
combinations tested. Total cooking loss was higher with high
power microwave cooking and lower (P < 0.05) for conventional
and low power microwave cooking. End-point temperature of
6O0C produced lower cooking losses than 70 or 75oC which were
not different (P < 0.05). Changes in chemical composition
indicated greater water losses for medium and high power
microwave cooking (P < 0.05) compared to other cooking
methods. The percentage change in sarcomere length from raw
to cooked samples increased as end-point temperature
increased. Kramer shear force values were lower for SV than
LD roasts, while cooking method and end-point temperature had
no effect. Instron assessment of the binding junction
indicated to difference in peak force, work, tensile
strength, strain, or modulus of rigidity due to cooking
method (P > 0.05). Sensory panelists rated SV roasts
superior in juiciness, connective tissue content, and overall
tenderness compared to LD roasts, but no differences were
detected among methods.
In Study II, ECS assessment was conducted using inulin
[14C] carboxylic acid. Thermal processing reduced ECS;
however, method of heat generation did not affect ECS.
viii

In summary, when final internal end-point temperature
is controlled differences in chemical and physical
characteristics due to cooking methods are minimized.
ix

CHAPTER 1
INTRODUCTION
The 1985/86 Annual Report of the National Live Stock and
Meat Board indicates that the beef industry must become more
consumer-oriented to maintain its market share. In the
present decade, one out of four American households consists
of a single individual, compared with one out of ten in 1955
(Anonymous, 1983). The annual report also indicated that
only seven percent of families in America consisted of one
breadwinner, indicating more and more households with two
incomes. Therefore, consumers have more active lifestyles
and an increasing need for convenience. A recent consumer
marketing survey conducted for the National Live Stock and
Meat Board and the American Meat Institute concluded that the
consumer's decision to serve red meat was determined
primarily by convenience, taste and economics (Anonymous,
1987).
As a result of changing lifestyles, consumers of the
eighties do not tend to have the same needs, wants, or
concerns as did consumers twenty years ago. The results of a
1984 Food Marketing Institute study indicated that 71% of
supermarket customers surveyed were concerned with diet and
health issues (Anonymous, 1984). This same study indicated
1

2
that 48% of the supermarket customers surveyed selected
recipes based on their nutritional content and 44% avoided
buying products that had no nutritional information.
A national consumer-retail beef study (Saveli et al.,
1986) suggested that beef products must be lean (free of
trimmable fat), high in quality and convenient to prepare in
order to attract today's consumer. To accomplish these
goals, many retailers have reduced trimmable fat levels on
retail cuts to 6.25 mm and others have removed all of the
outside fat. However, the 1987 Consumer Climate for Meat
Marketing Study indicated that, while per capita consumption
has responded slightly, future progress will be dependent on
continued development of products that meet the consumers'
criteria. In response to these consumer demands, many meat
processors are providing entrees in a ready-to-eat or
precooked form, requiring a reheating period which frequently
involves the use of a microwave oven.
The advent of the microwave oven has opened up a new
dimension in food preparation and management, both in the
home and in the food service industry. The greatest
advantage of microwave cooking is the time and energy saving
considerations. In 1984, 9.1 million microwave ovens
comprised the largest annual purchase of any home appliance
in history (Markov, 1985a).
A major challenge confronting progress toward
consumer-driven marketing approaches is the high price

3
charged for precooked items. This price level is
necessitated by the use of high valued muscles, cooking
losses and equipment for thermal processing and aseptic
packaging. However, consumers appear to resist this higher
price when buying a precooked beef roast, even though they
pay comparable prices for sliced roast beef at the
delicatessen. Perhaps a ready-to-cook roast product designed
for rapid microwave cooking would be more appealing.
In addition to price considerations, the occurrence of
off-flavors in precooked beef entrees is another source of
concern for meat processers. To help overcome the presence
of any off-flavors in a precooked entree, a package of gravy
or seasoned sauce is frequently included with most products.
Perhaps an alternative to precooked meat entrees is
producing a reformed meat product using muscles from the
chuck and plate that could be cooked rapidly in a microwave
oven. Muscles from the chuck and plate are traditionally
lower in economic value compared to muscles from the rib,
loin, and round. The lower economic value associated with
the chuck is due in part to compositional differences between
many of the muscles that make up the chuck. Numerous
researchers have documented significant differences in
connective tissue, contractile status, and intermuscular fat
between the many muscles of the chuck (Ramsbottom et al.,
1945; Ramsbottom and Stradine, 1947; Prost et al., 1975; Zinn
et al., 1970; McKeith et al., 1985; Paterson and Parrish,

4
1986; Recio et al., 1987). Therefore, raw materials from
these regions would provide a means of lowering production
costs and aid in producing a competitively priced product.
In addition, these muscles would provide a source of lean
meat since all surface fat and surface connective tissue
could be removed. This would provide the meat processor with
the ability to produce a boneless roast beef product in which
size, shape, and fat content could be controlled. A roast
beef product of this type could help the beef industry
provide entrees that address the diet-health issues and
fulfill the convenience needs of the consumer.
In contrast to traditional restructured products the
texture of this reformed product should be comparable to that
of a whole muscle entree. The convenience attribute could be
achieved by producing a portion size needed by a two or three
member family for one meal (340 to 450 g) that could be
cooked quickly in a microwave or conventional oven.
Several major obstacles currently hinder production of such a
product. First, little research has been conducted on
feasible procedures for producing reformed whole beef muscle
products that utilize lower valued muscles. Research is
needed to develop production procedures that consider:
1) Economically feasible methods for removal of heavy
surface layer connective tissue (epimysium).

5
2) Protein extraction methods that do not result in
loss of muscle integrity and yet produce acceptable
binding characteristics upon thermal processing.
3) Stuffing procedures that generate a uniformly shaped
product.
Also, previous attempts to cook meat entrees in a microwave
oven have failed to produce a product of acceptable quality.
Although the microwave oven has been shown to decrease
cooking time, labor and energy costs, it has not been readily
accepted by food service institutions or homemakers for
cooking beef entrees. The skepticism surrounding the use of
the microwave oven for preparation of beef entrees is thought
to be due in part to uneven cooking, greater cooking losses,
and less palatable meat (Headley and Jacobson, 1960; Kylem et
al., 1964; Law, 1967; Ream et al., 1974; Drew et al., 1980;
Moore et al., 1980; Griffin et al., 1981). However, many of
these studies have been "trial and error" rather than a
deliberate approach to understanding the microwave heating
process and its effect on muscle tissue. Major questions
still remain unanswered regarding microwave oven cookery of
beef entrees and the perceived relationship with toughness
and lack of product juiciness. Research is needed to
understand the effects on muscle tissue of rapid heating
rates, greater moisture losses and excessive post-cooking
temperature increases. Research emphasis should be directed
so as to study:

6
1) The rate at which heat is conducted into the
product as a result of different heating methods (microwave
or conventional). Knowledge of this information would be
useful in developing a computer aided model to predict
thermal processing conditions required to achieve a certain
degree of doneness.
2) The influence of different heating rates (rapid or
slow) when associated with different cooking methods,
(microwave or conventional) and their effects on the
chemical, textural, and sensory attributes of a meat product.
3) The effects of incorporating different amounts of
water into the meat product during production processes,
subsequent effects on water loss during thermal processing,
and the perceived juiciness and overall palatability of the
products.
The proposed research involves production of a reformed
whole muscle roast beef product and the systematic study of
microwave and conventional cookery effects on beef and
addresses the research needs listed previously.
The objectives of this study are
1) To develop feasible processing procedures for
reforming whole beef muscles, the serratus ventralis and
latissimus dorsi. These two muscles were chosen for several
reasons: a) currently they are not being used to their
highest potential; b) they are unipennate muscles with fibers
oriented in one direction; c) they contain mainly surface

7
connective tissue with no large septums of internal
connective tissue; d) they are two of the larger muscles
found in the forequarter; and e) they differ compositionally
in fat content (>10% and <5% fat for the serratus and
latissimus, respectively).
2) To quantify the changes in meat components that occur
during thermal processing with microwave and conventional
cooking at different cooking rates (low, medium, and high
power) and relate these to changes in physical and sensory
measures of tenderness and palatability.
3) To study changes in tissue fluid distribution, as
influenced by thermal processing (microwave versus
conventional) when beef roasts are cooked to the same
internal end point temperature at the same rate.

CHAPTER 2
LITERATURE REVIEW
Restructured Products
Breidenstein (1982) refers to restructuring as a
processing method by which raw meat materials are converted
into ready-to-cook products. This method of meat processing
has been extensively reviewed by Mandigo (1975), Huffman
(1979), Mandigo (1982a,b), and Breidenstein (1982). The
primary objective for utilizing restructuring technology is
to add economic value to under-utilized raw materials that
are currently considered to be of limited economic value. As
a result, restructuring methodology is considered to be a
means of enhancing the economic value of the raw materials,
and the enhanced value will be preceived as being greater
than the cost of its achievement (Breidenstein, 1982).
Restructured products created to date have been produced
from a variety of different meat species and formulated to
contain different types and levels of non-meat ingredients.
The phrase "intermediate value beef products" was used by
Breidenstein (1982) to refer to a group of restructured beef
products. This group of products is considered to have an
economic value preceived by the consumer to lie between that
of ground beef and that of intact muscle steaks and roasts.
8

9
Breidenstein (1982) warned that caution must be exercised
when selecting raw materials that contain heavy
concentrations of connective tissue embedded in the muscle
mass. Therefore, selection criteria of raw materials and
production methods used for producing restructured beef
products are very important to their acceptability. The
restructuring process typically requires the raw meat
materials to undergo a process of particle size reduction,
blending and reshaping. Several mechanical methods have been
developed to reduce particle size. They include grinding,
flaking, chunking, slicing, and emulsifying. Reducing the
particle size produces numerous meat pieces that must be
bound back together at the various meat interfaces. To
accomplish this, the intracellular protein, myosin, is
commonly used as a binding agent. Extraction of myosin to
the meat surface is accomplished by mechanical mixing,
massaging, or tumbling of the meat particles in the presence
of sodium chloride and phosphates. Maintaining a cohesive
bind in the uncooked product is accomplished by freezing,
while the bind in the cooked product is dependent upon a heat
induced bonding (Breidenstein, 1982).
As a result of the numerous mechanical methods used to
reduce particle size, a wide variety of products have
resulted. In an effort to categorize the various products
produced, Field (1982) identified four groups of restructured
products for retail and food service: 1) frozen, flaked and

10
formed restructured meats; 2) chunked and formed or sectioned
and formed restructured meats; 3) emulsified, ground or
chopped restructured meats; and 4) sliced restructured meats.
Mandigo (1982a) suggested that cured and smoked products also
represented a distinctive group of meat products produced by
restructuring technology.
Formulation considerations and manufacturing procedures
are vital components in the production of a restructured or
reformed roast beef product. The term "reformed," as used
throughout this dissertation, refers to a type of
restructuring process whereby no reduction in particle size
is imposed. Therefore, production methods used to
manufacture a reformed beef product are very important to its
acceptability. The focus of this review will discuss product
manufacturing, muscle selection, protein functionality,
distribution of cellular water and thermal processing of the
final product.
Manufacturing Considerations for Restructured
Beef Products
Through extensive research efforts, many variables have
been identified that influence manufacturing procedures and
organoleptic characteristics of a restructured meat product.
To date, restructured meat products have typically involved
reducing the particle size of the starting material. As
previously stated, particle reduction can be acheived by a
number of methods; flaking is one of the more recently

11
developed methods. This method is capable of using meat in
the fresh or frozen state; however, particle uniformity is
enhanced if the meat is crust frozen or frozen solid (Huffman
and Cordray, 1982). The meat is cut in a shaving-like manner
into flakes of varying particle sizes and texture (Fenters
and Ziemba, 1971; Mandigo et al., 1972; Pietraszek, 1972).
Advantages for products made from flaked meat include
improved texture, reduced drip loss, enhanced binding and
cohesive properties, decreased cooking losses and improved
sensory characteristics (color, flavor, juiciness, and
tenderness) over those products produced from sectioned meat
(Anonymous, 1973).
Reducing the particle size of meat by sectioning
involves cutting large muscles into chunks, which may or may
not be uniform in size. The primary advantage of this method
is that the resulting product should have the palatability
attributes that more nearly resemble that of intact muscle,
compared to products produced from flake cut particles
(Acton, 1972) . The main disadvantage of this process is that
fat particles are easily detected. This effectively reduces
the amount of fat that could be incorporated into the
product.
Although most restructured products contain 12 to 25%
fat, increasing the fat content from 20 to 30% was reported
to improve the products sensory properties (Seideman, 1982).
Typically, formulating a product to contain a desired fat

12
content requires using at least two meat sources, one higher
and one lower in fat content.
Booren et al. (1981a) produced sectioned and formed beef
steaks to contain 12% fat in the final product. This
involved utilizing beef chucks trimmed of excess fat and
connective tissue, to provide a source of lean meat that
contained 8 to 10% fat and another source that contained 48
to 52% fat. However, the authors indicated that because of
the heterogenous nature of meat, the fat levels achieved in
the final product were deemed to be the most variable
component. The authors concluded that this was due to the
diverse amounts of inter- and intramuscular fat present in
Choice, Yield Grade 3 chucks. Previously vacuum packaged
beef chucks were allocated to vacuum or non-vacuum mixing
treatments for periods of 6 or 12 minutes. Under the
experimental conditions described by these authors, the added
fat source separated and accumulated on the sides of the
mixer or appeared as large fat pockets within the steak
product. Vacuum mixing was reported to produce a less
desirable surface color in the finished steak product, as
determined by spectrophotometric analysis. It was theorized
that low oxygen tension present during storage of the vacuum
packaged beef chuck and during vacuum mixing caused the
globin molecule to become denatured, which resulted in a less
desirable color. The occurence of this problem had been
previously reported by Lawrie (1974). Two-thiobarbituric

13
acid (TBA) values did not change following 60 d of freezer
storage, regardless of mixing treatment. Vacuum mixing
treatments had no effect on cooked yields, Kramer shear area
or Kramer shear force values. Sensory analysis indicated a
significant increase in bind between meat pieces for vacuum
mixed steaks. The authors reasoned that vacuumization may
function to remove tiny air bubbles from the extracted
protein exudate, resulting in a denser mass of the extracted
myofibrillar proteins at the bind area. Juiciness,
tenderness, flavor and connective tissue residue were not
different due to mixing treatments.
To help create acceptable product tenderness in a
sectioned and formed product, Huffman (1978) proposed a
restructuring process that combined both chunks and wafer
thin slices of meat. The process resulted in a product that
closely resembled whole muscle cuts of meat. A patent was
issued for this restructuring process. Huffman (1979)
concluded that raw meat materials to be used in sectioned and
formed products should be subjected to mechanical
tenderization prior to use. Mechanical tenderization would
help ensure maximum cell disruption and enhance the binding
characteristics of the product. However, this processing
step requires additional equipment, which, in turn, increases
the cost of production.
Independent of the methods utilized to obtain a
reduction in particle size is the importance of the actual

14
particle size. Acton (1972), in an effort to study the
effects of various particle sizes in the production of
poultry loaves, used muscles cut into strips, cubes, coarse
ground, finely ground and finely ground five times. He
reported that decreasing the particle size resulted in
increasing the amount of salt soluble proteins extracted, and
hence, the binding strength of the final product. This was
concluded to be a result of increased surface area associated
with decreasing the particle size. In addition, the author
reported a decrease in cooking loss as particle size
decreased.
In contrast, Chesney and co-workers (1978), in a study
of fabricated pork products, reported that particle size did
not significantly influence the water holding capacity, shear
force values or proximate chemical analysis values. However,
in accordance with Acton (1972), a significant decrease in
cooking loss percentage was also reported as particle size
decreased. Studies by Chesney and co-workers (1978) and
Acton (1972) also agreed on taste characteristics. These
studies indicated that products prepared from large particles
were inferior in cohesion, juiciness, tenderness and overall
acceptability when compared to products prepared from medium
or smaller particle sizes.
Variations in product bite, mouth feel and other sensory
properties can be achieved by altering the ratio of various
particle sizes, fat and moisture content, mixing time and

15
size and shape of the final product (Huffman, 1979).
Popenhagen et al. (1973) reported that combining meat flakes
of different sizes and varying temperatures yielded steaks
that were more desirable in texture and overall eating
quality than steaks made from a single size of flake and
temperature. Similarly, Mandigo (1974) reported that a meat
temperature of -5°C at the time of flaking significantly
influenced the texture and appearance of the final product.
Mixing is a processing step required to achieve uniform
distribution of the lean, fat and nonmeat components. Mixing
also facilitates extraction of the intracellular myofibrillar
proteins to the surface of the meat. Extraction of the salt
soluble proteins (actin, myosin, and actomyosin) provides the
binding material necessary to bond the various meat
components together. Two of the most popular processing
methods used to extract the proteins needed to facilitate
binding are massaging and tumbling. Both of these methods
are physical processes designed to mix ingredients, enhance
quality attributes (tenderness) and accelerate meat product
manufacturing (Addis and Schanus, 1979).
Tumbling involves generating "impact energy" as a result
of meat striking the sides and bottom of a rotating drum or
being struck with paddles or baffles (Addis and Schanus,
1979). This action results in a transfer of kinetic energy
to the muscle mass and a resultant rise in temperature. The
tumbling process typically occurs within the confines of a

16
sealed vessel capable of operating while under vacuum.
Vacuumization of the tumbler is reported to help overcome
potential problems such as tissue softening and the
incorporation of air into the extracted protein matrix (Addis
and Schanus, 1979).
Massaging is considered to be a less vigorous process
when compared to the action of tumbling. It involves
generating frictional energy as a result of rubbing meat
surfaces together. Vacuumization of the massager is also
possible and is done to help overcome potential problems
previously stated. The primary purpose of massaging or
tumbling is to facilitate the extraction of the salt soluble
myofibrillar proteins, myosin, actin and actomyosin. The
physical actions associated with massaging or tumbling,
provide a tenderizing effect and help to incorporate added
fluids into the raw meat materials (Addis and Schanus, 1979).
Weiss (1974), in a report on ham tumbling and massaging,
indicated that Europeans categorize muscle tissue as either
firm or soft when selecting the appropriate method for
protein extraction. Beef, mutton and turkey are considered
firm muscles and are subjected to impact tumbling, while soft
muscles, pork and chicken, are subjected to massaging. The
basis for this segregation is due to differences in the
physiological and biochemical composition of the muscle
tissue, and the response of the tissue to various physical
and chemical processing techniques.

17
MacFarlane and coworkers (1977) measured the binding
strength between adjacent meat pieces using myosin,
actomyosin and sarcoplasmic proteins as binding agents.
These authors concluded that myosin exhibited the greatest
binding capability with or without the addition of salt. The
role of the myofibrillar proteins in binding chunk-type
products together has been demonstrated by a number of
researchers (Anonymous, 1971; Rahelic et al., 1974; Ford et
al., 1978; Siegel et al., 1978a,b; Booren et al., 1982).
Booren and coworkers (1981a) studied the effects of
blade tenderization, vacuum mixing, salt addition and mixing
time on the binding of meat pieces from A maturity (young),
Standard grade beef rounds when processed into sectioned and
formed steaks. All rounds were defatted and cut into 2-3 cm
pieces; one group of rounds was blade tenderized twice. Each
group was divided into 18 kg meat blocks and assigned to
treatments of vacuum and non-vacuum mixing. The groups were
further divided into 9 kg blocks and allocated to 0 and 0.5%
added salt. Salt was incorporated into the product by
sprinkling it over the meat during the first 30 sec of
mixing. Each block was sampled after 0, 8, 16, and 24 min
blending. Samples were stuffed into plastic bags, crust
frozen at -30°C and pressed into logs in the shape of a strip
loin. Steaks 2.5 cm thick were cut, vacuum packaged and
frozen for futher analysis. All steaks for sensory
evaluation were oven broiled in a rotary hearth oven. The

18
oven was set to maintain an internal temperature of 150°C,
and steaks were cooked to an internal temperature of 70°C.
Analysis of beef steaks indicated that the percentage of ash
and salt was significantly higher in the 0.5% salt
treatments. Moisture, protein, fat percentage and pH were
not different for blade tenderization, vacuum mixing or salt
addition treatments. Mean fat content of the final product
was 1.65%. The percentage of fat measured during the various
mixing times was highest at 0 min and lowest at 8 min. The
authors indicated that fat accumulated on the sides of the
blender as mixing time progressed. Twenty-four minutes of
mixing time was reported to yield the lowest cooking loss
23.8% compared to 27.5% for 0 min of mixing time. The TBA
values increased due to salt addition over a 90-day frozen
storage period, but did not change due to mixing time. A
significant interaction between blade tenderization and salt
addition for TBA values was reported. Products that were not
subjected to blade tenderization and no added salt had the
lowest TBA value of 0.77 compared to a value of 1.03 when
salt was added. Blade tenderization, regardless of added
salt content, resulted in higher TBA values compared to
non-tenderized products. The authors indicated that blade
tenderization increased the surface area of the meat,
allowing oxygen to be more accessible to the cut surfaces. A
significant interaction between vacuum and salt level was
also reported to exist, whereby removal of oxygen by vacuum

19
mixing resulted in a lower TBA value (0.83), compared to no
vacuum mixing (0.90) in steaks processed with 0.0% added
salt. The effect of mixing time on binding strength
indicated a 60% increase in particle adhesion as mixing time
increased from 8 to 16 min. Tenderness, as measured by the
Kramer shear cell, increased with increasing mixing times.
The authors indicated that the increase in tenderness
associated with increased mixing time may be an advantage
when restructuring with lower quality meats. Sensory
evaluations for initial tenderness were more desirable
following 8 min of mixing. However, tenderness desirability
decreased with 16 and 24 min of mixing. The authors
theorized that increased protein exudate content, extracted
as a result of increased mixing time, may have produced a
case hardening effect on the product surface.
In a similar study, Booren et al. (1981b) investigated
the influence of muscle type on characteristics of sectioned
and formed beef steaks. The processing procedures for
product preparation were equivalent to the one described for
their previous experiment (Booren et al., 1981a), with some
exceptions. In this study (Booren et al., 1981b), a coarsely
ground lean meat source was obtained from beef rounds of "A"
maturity, Standard grade carcasses. A fat meat source was
obtained from the plate region of the corresponding beef
carcass. Beef plates were sliced thin to permit formulating
a steak product to contain 12% fat. They reported similar

20
results as described by their previous study (Booren et al.,
1981a). Cooking yields increased with increased mixing
times, from a low of 70.55% at 0 minutes to a high of 77.35%
after 18 minutes of mixing. Flavor and juiciness sensory
scores also increased with increased mixing time. Longer
mixing times accelerated the rate at which the fresh
(uncooked) meat color deteriorated. The product made from
beef top rounds and beef plates was found to be more tender
and to contain less connective tissue residue as measured by
sensory panelists, when compared to their previous experiment
(Booren et al., 1981a).
Muscle Selection Criterion
One of the primary objectives of producing a
restructured meat product is to enhance the economic value of
lower valued meat cuts and trimmings. Traditionally, the
beef chuck has been a wholesale cut of lower economic value
when compared to the round, loin or rib. The wholesale beef
chuck represents approximately 27% of the beef carcass and is
typically merchandised at the retail level in the form of low
priced roasts and steaks, or as ground chuck (Paterson and
Parrish, 1986). The lower economic value associated with the
chuck is due in part to compositional and palatability
differences that occur within and between many of the muscles
that make up the chuck. Numerous researchers have documented
significant differences in connective tissue content,

21
contractile status, and intermuscular fat between the many
muscles comprising the chuck (Ramsbottom et al., 1945;
Ramsbottom et al., 1947; Prost et al., 1975; Zinn et al.,
1970; Marsh, 1977; McKeith et al., 1985; Paterson and
Parrish, 1986) .
Marsh (1977) cited the contractile status of the muscle
fiber and the collagen content (connective tissue) of the
muscle as two primary structural components responsible for
variation in muscle tenderness. The muscle fiber component
is termed myofibrillar toughness, and it is thought to
respond to the handling procedures from the time of slaughter
(Rowe, 1977). It is this muscle fiber component that is
considered to be responsible for changes in meat tenderness
resulting from cold shortening, aging, Tenderstretchingâ„¢ and
electrical stimulation. The contractile status of a muscle
refers to the sarcomere length of an individual muscle fiber.
A decreased sarcomere length caused by cold shortening is
associated with an increase in muscle toughness. Increasing
the sarcomere length of a muscle beyond its normal resting
length would be associated with stretched muscle fibers and
an increase in muscle tenderness.
The influence of connective tissue content, relative to
meat texture has been extensively reviewed by Tahir (1979).
Meat is classified as tender or less tender principally on
the basis of connective tissue content (McCrae and Paul,
1974). Connective tissue toughness is usually referred to as

22
background toughness and is regarded as not being
significantly influenced by treatments applied to the meat
from the point of slaughter up to the point of cooking (Rowe,
1977).
Collagen is the major protein in connective tissue and
was considered to be the single major factor influencing meat
tenderness (Tahir, 1979). However, Doty and Pierce (1961)
concluded that collagen content was not significantly related
to tenderness. In addition, Carpenter et al. (1963) found no
significant relationship between tenderness measurements and
the total amount of connective tissue.
Certain physical properties of collagen change with age.
The total quantity of collagen in muscle does not increase
with the age of the animal (Goll et al., 1963). However, the
number of crosslinkages between the collagen molecules within
the connective tissue increase with age. As the degree of
crosslinking increases, the structural stability of the
tissue increases. This increase in structural stability
decreases the ability of collagen to become solubilized
during thermal processing thereby influencing the tenderness
of the meat (Goll et al., 1963). Two types of crosslinking
structures are known to occur. Intramolecular bonds occur
within the collagen molecule, and intermolecular bonds link
one triple helix to another (Sims and Bailey, 1982). The
function of the intramolecular crosslink is as yet unknown;

23
however, intermolecular crosslinks provide the mechanical
stability of the collagen fiber.
Collagen contains a unique amino acid profile that is
high in glycine and hydroxyproline. Together, they comprise
about half of the total amino acids found in collagen (Sims
and Bailey, 1982). The presence of the amino acid
hydroxyproline in collagen (about 14%) is thought to be
confined almost exclusively to the stromal proteins of
collagen and elastin (Gross and Piez, 1960). Because of the
unique distribution of hydroxyproline in collagen, its
presence has been used as a means of determining the amount
of collagen present in tissue (Sims and Bailey, 1982).
Sensory and chemical analysis for moisture and fat
percentage, sarcomere length and total collagen content of
thirteen major beef muscles from the round, loin, rib and
chuck were reported by McKeith and co-workers (1985). The
infraspinatus, triceps, supraspinatus and deep pectoral were
evalulated from the chuck. Sensory panel tenderness scores
and Warner Bratzler shear force values (WBS) indicated that
the infraspinatus was the most tender and that the deep
pectoral was the least tender. From the 13 muscles
evalulated, only the psoas major (tenderloin) was ranked
higher than the infraspinatus in overall tenderness. Mean
collagen content of muscles from the chuck, round, loin and
rib were 11.44, 8.94, 5.33, and 4.66 (mg/g wet tissue basis),
respectively. Muscles from the round and chuck had lower

24
sensory scores than muscles from the loin and rib. However,
fat percentage, sarcomere length and collagen content from
each muscle were not significantly correlated to palatability
traits (McKeith et al., 1985). Although not determined in
the previous study, the authors concluded that soluble
collagen content may be a more important factor relating to
meat tenderness than total collagen content. In addition,
these authors concluded that some muscles would have a
potentially greater economic value if they were separated
from the wholesale primal and used independently.
Smith and coworkers (1978) reported on the tenderness of
20 different muscles from the chuck and other wholesale cuts.
They also indicated that the infraspinatus muscle when
prepared as a steak or roast had lower (more tender)
Warner-Bratzler Shear (WBS) values than the longissimus dorsi
from the chuck or rib. Results from these two studies
(McKeith et al., 1985 and Smith et al., 1978) indicate that
boning line production techniques should be developed and
implemented so as to facilitate removal of the more desirable
muscles from the chuck. Current industrial practices of
whole-muscle boning and merchandising boxed beef make single
muscle groups available to consumers and processors.
Therefore, knowledge of the palatability characteristics of
these muscles combined with current restructuring or
reforming technology could improve consumer acceptance of the
final product.

25
The serratus ventralis (SV) muscle is located
immediately ventral to the rib bones of both the wholesale
rib and chuck. The SV is a large, fanshaped muscle that
contains both surface and internal septums of connective
tissue. The SV contains about 10% fat and is one of the
larger muscles comprising approximately 5% of the wholesale
chuck (Huffman and Cecchi, 1986). The SV is intermediate in
palatability characteristics of the major chuck muscles
(Paterson and Parrish, 1986). However, no reports regarding
the characteristics of the latissimus dorsi (LD) have been
found. This large, thin muscle lies on the outside of the
plate and extends into the chuck. The LD is approximately
half the size and weight of the SV and contains about 5%
intramuscular fat.
Both the SV and LD muscles provide an excellent source
of raw material from which a reformed whole-muscle beef
product could be produced. Currently these two muscles are
not being used to their greatest economic potential. In
addition, both muscles are unipennate, with fibers oriented
in one direction, and contain mainly surface connective
tissue. Also, these muscles comprise a major portion of the
forequarter and differ compositionally in internal fat
composition (>10% and <5% for SV and LD, respectively) (Recio
et al., 1988) .

26
Muscle Protein Functionality
Muscle protein functionality denotes any physiochemical
property that affects the processing and behavior of protein
in food systems as judged by the quality attributes of the
final product (Hand, 1986). Three major protein
functionality interactions have been reported to occur in
processed meat products: 1) protein-water; 2) protein-lipid;
and 3) protein-protein (Acton et al., 1983; Acton and Dick,
1984; 1985).
It is generally accepted that the myofibrillar proteins,
actin and myosin, are the primary proteins that provide the
structural stability to processed meat products. Although
many other myofibrillar proteins are present in meat tissue,
their quantity and contribution to structural stability in a
processed meat product is insignificant. The ability to bind
meat pieces back together in a restructured meat product is a
heat induced phenomenon involving protein-protein
interactions (Asghar et al., 1985). Several researchers have
attempted to explain the mechanism by which meat binding
occurs.
Hamm (1966) studied the changes that occur in meat
proteins during cooking and concluded that thermal processing
caused the helical portions of the protein molecules to
denature into random chains. These unraveled proteins were
postulated to produce random crosslinkages that may be
responsible for binding.

27
Vadehra and Baker (1970) and Hotter and Fischer (1975)
theorized that the mechanism of binding involves structural
rearrangement of the soluble proteins. This resulted in a
loosely ordered protein structure that allowed the proteins
to become more reactive during thermal processing.
The extraction of myofibrillar proteins is required to
facilitate binding of meat pieces. The binding properties of
purified muscle proteins were studied by MacFarlane et al.
(1977). They determined the binding strength of myosin to be
superior to that of actomyosin at salt concentrations up to 1
M. However, increasing the myosin concentration did not
result in increased binding strength (MacFarlane et al.,
1977; Siegel and Schmidt, 1979a). Siegel and Schmidt (1979a)
concluded that the decreased binding associated with
increased myosin concentrations implied ionic interactions in
binding. MacFarlane et al. (1977) further reported that, in
the absence of salt, the binding strength of myosin was
enhanced by incorporating sarcoplasmic proteins. The
contribution of sarcoplasmic proteins to the binding strength
was reported to be similar to that for salt. However, it was
reported that as salt concentrations increased, the
sarcoplasmic proteins exerted a deleterious effect on the
binding strength of myosin. This was attributed to the
adsorption of denatured sarcoplasmic proteins onto the
myofibrillar protein molecules, which resulted in decreasing
the availability of the binding sites.

28
Theno et al. (1978a) studied the binding junctions of
thermally processed sectioned and formed ham products. Their
research detected the presence of aligned elements occurring
within the binding junctions of the meat pieces. Siegel and
Schmidt (1979b), in an effort to determine the mechanism of
binding between meat pieces, described the ultrastructure of
a crude myosin gel as affected by salt, phosphate, pH and
temperature. They concluded that the mechanism of binding
meat pieces involved the following events. Intact
myosin-heavy chains are extracted to the muscle surface where
they combine with heavy myofilaments located on or near the
surface of the muscle cells. This results in producing super
thick synthetic filaments that bind the meat pieces together.
Formation of super thick filaments at higher temperatures was
stated to be possible because heavy chains are freed from the
parent molecule at lower heating temperatures due to salt
solubilization (Siegel and Schmidt, 1979b).
From this discussion it becomes evident that the
mechanisms involved in binding meat pieces together are
multifaceted. The heat-induced protein-protein interactions
are influenced by salt, ionic strength, protein type and
protein guantity.
Mechanisms of Protein-Water Interactions
Myofibrillar proteins are primarily responsible for the
binding of water in muscle and that different types of water

29
and water binding occur in muscle tissue (Hamm, 1975a).
Fennema (1985) presented a classification system for water
occurring in food systems. Type I water, also referred to as
bound water, is the mono- and possibly the bimolecular layer
of water surrounding proteins and other substances having an
electrostatic charge affinity. Type I water is present in
small quantities (4.5% of total water), unfreezable, and
displays little mobility. Type II or restricted water exists
as multiple layers surrounding the bound Type I water. Type
II water is subject to freezing and can be removed by drying.
Type III water or free water represents the major portion of
water located in animal and plant tissues and is subject to
easy removal. Type IV water refers to water in the pure
state and does not naturally occur in biological matter.
Because Type I water is bound and Type IV water does not
naturally exist in muscle tissue, the types of water that are
of interest from a food processing standpoint are Types II
and III. Therefore, a primary objective of meat processing
is to reduce the amount of water in the free state (Type III)
and increase the amount in restricted (Type II) state.
Variations in water content can result from gains that
occur during processing (in the form of added water), or
losses from improper chilling, drip, evaporation or cooking.
Such gains or losses are important for two reasons: first,
economics (since meat is sold by weight); and second,
consumer satisfaction, (the juiciness and tenderness of meat

30
and meat products depends to a great extent on their water
content). Additionally, subsequent water losses that occur
during cooking act to reduce the edible portion size (Offer
and Trinick, 1983).
Hamm (1960) defined water-holding capacity as the
ability of meat to hold its own or added water during
application of any force (pressing, heating, grinding). Hamm
(1975b) defined swelling or water binding ability as the
spontaneous uptake of water by meat from any surrounding
fluid, resulting in an increase in muscle weight. Although
the forces that restrict the mobility of loose water are not
well understood, the factors that influence changes in the
water-holding capacity of meat have been described (Hamm,
1960; 1966; 1975a,b). Hamm (1975b) described the swelling of
muscle fibers in terms of colloidal chemistry. The amount of
water immobilized within the tissue is influenced by the
spatial molecular arrangements of the myofibrillar proteins,
or filaments, of actin and myosin (Hamm, 1975b). Decreasing
the cohesion between adjacent molecules or myofibrillar
filaments by increasing the electrostatic repulsion between
similarly charged groups or by weakening of hydrogen bonds,
causes the network to enlarge or swell. Increasing the
degree of swelling increases the amount of water that can be
immobilized within the filamentous network, thus
water-holding capacity increases. However, a continued
decreasing of intermolecular cohesion will result in network

31
collapse, and the gel becomes a colloid solution of
myofibrillar proteins. Increasing the electrostatic
attraction of oppositely charged groups between adjacent
molecules can produce new interlinking bonds. This results
in less space being available for the retention of
immobilized water. Therefore, when the myofibrillar network
tightens as a result of applied pressure, heat, or grinding,
shrinkage occurs. This causes part of the immobilized (Type
II) water to become free (Type III) water and flow out of the
product (Hamm, 1975a).
Wierbicki and Deatherage (1958) offered the following
hypothesis regarding the forces that immobilize and bind
water. The highly polar water molecules are attracted to the
muscle proteins by ionizable basic and acidic amino acids and
by polar nonionic amino acids.
Offer and Trinick (1983) redefined water-holding
capacity (WHO) as the ability of meat to retain its natural
water content. Their studies reported on the mechanism of
water holding in meat and the swelling and shrinking of
isolated myofibrils, which provided evidence that myofibrils
were able to swell to at least twice their original volume
using salt concentrations that are commonly used in the
processed meats industry. These authors suggested that
myofibrils were the site of water retention. In their study,
Offer and Trinick (1983) made the same basic assumptions as
Hamm (1960), i.e., that as chloride concentration increased,

32
chloride ions became bound to network filaments. This
interaction increased the repulsive force between filaments
and tended to cause expansion of the network lattice.
However, Offer and Trinick (1983), in their discussion of the
mechanism of water holding in meat, stated that Hamm's model
was not complete for two reasons. It did not consider that
only a part of the myofibril (the A-band) was solubilized, or
the high degree of structural order of the myofibrils (Hand,
1986). Their reasoning was based on the fact that myofibrils
occupy about 70% of the volume of lean meat, and the degree
of observed swelling was related to the amount of water
retained as a result of meat processing. An additional
factor supporting their claim was that the binding of water
to the surface of protein molecules was too small to account
for the observed changes in water content (Hamm, 1960). This
was also based on a protein content of 20% and the belief
that proteins only bind water to an extent of 0.5g of
hydration water per gram of protein (Kunz and Kauzmann,
1974). Therefore, water that is actually bound to protein
molecules represents a small fraction of the total water
present.
Offer and Trinick (1983) concluded that the transverse
linkages, more specifically the cross-bridges, act to
restrain myofibrillar expansion. They indicated that the
influence of attached cross-bridges could be removed in one
of two ways: 1) disruption of the thick filament (myosin)

33
backbone, would result in disrupting mechanical continuity
and 2) detachment of the cross-bridges from the filaments.
The concentration of sodium chloride (0.4 M) required to
yield maximum swelling was less when pyrophosphate (0.8 M)
was used compared to its absence. However, pyrophosphate did
not alter the maxium extent of swelling. Increasing the
concentrations of sodium chloride and/or pyrophosphate were
shown to 1) displace the equilibrium existing between the
myosin filament and the myosin molecules, in favor of the
myosin molecules and 2) decrease the binding strength of
myosin heads to actin molecules. These actions function to
remove effectively the influence of the protein-protein
cross-bridges and act to increase water-holding capacity.
The authors also reported that maximum myofibrillar swelling
occurred when a substantial part of the A-band had been
extracted, providing further evidence that a large degree of
myofibrillar swelling could occur under conditions where more
than half of the protein was lost.
In summary, the mechanisms of protein-water interactions
are complex. They involve chemical bonding, charge repulsion
and attraction forces, as well as molecular and structural
arrangement. As a result, all of these factors interact to
influence the water-holding capacity of the meat product.

34
Influences on Protein-Water Interactions
In a review of the factors influencing water-holding
capacity of proteins, Acton and co-workers (1983) indicated
that most factors function in one or more of these three
ways: 1) the ionization and charge density of the protein
(tissue pH); 2) the extent of physical tissue disruption
(particle size); and 3) the distance the water is located
from the protein surface.
pH influence
The relationship of muscle pH to water-holding capacity
is well understood (Briskey, 1964; Dutson, 1983; Honkel et
al., 1981a,b). The relationship of WHC to pH is a function
of the myofibrillar proteins losing their affinity for water
as the pH approaches the isoelectric point for the given
protein (Szent-Gyorgyi, 1960). The decrease in pH that
accompanies postmortem glycolysis of muscle tissue has an
important bearing on meat quality. The final pH attained is
called the "ultimate pH" and for many mammalian species this
is close to a pH of 5.5 (Hultin, 1985). When the ultimate pH
of meat (5.3 to 5.5) approaches the isoelectric point (5.2)
of actomyosin, the WHC of the muscle is decreased (Dutson,
1983). However, when the ultimate pH of beef remains
elevated approximately 1.0 pH unit above the normal
postmortem pH (5.3 to 5.5), more water is retained or bound.
Meat of this type appears darker in color and is referred to

35
as "dark cutting beef." The ultimate pH attained by beef
muscle has been reported to influence the quality and
textural properties of the meat (Dutson, 1983). He concluded
the ultimate pH of meat affected color development, marbling
perception, WHC, cooler shrinkage, texture, cooking loss,
tenderness and processing characteristics of comminuted and
restructured meats.
Bouton and co-workers (1975) reported a threefold
increase in tenderness scores for mutton at pH 7.0 when
comparing an ultimate pH of 5.9 to 7.0. These authors noted
that the amount of juice centrifugally expressed from a
cooked meat sample had a high positive correlation with
sensory organoleptic juiciness scores and increased linearly
with pH.
Sodium chloride influence
There exists a broad variety of salts found in nature,
but because of taste and toxicological considerations, the
two most commonly used in meat products are sodium chloride
and the sodium salts of polyphosphoric acids (Trout and
Schmidt, 1983) . The addition of salt to meat has a
multi-functional affect. Salt was initially used as a
preservative to retard bacterial spoilage. Today, the
primary role of salts in a meat system is to influence the
ionic strength and alter the pH of the system (Trout and
Schmidt, 1983).

36
Closely related to water-holding capacity is the ability
of meat to absorb additional water at elevated salt
concentrations; this was termed water-binding capacity by
Hamm (1982). Salt concentrations of 0.8 to 1 M (4.6 to 5.8%)
sodium chloride (NaCl) have been reported to yield maximum
water uptake (Offer and Trinick, 1983). However, a somewhat
lower NaCl level (2%) is more often used in the manufacturing
of processed meat products. Hamm (1960) concluded that the
chloride ion (Cl~) from NaCl was the ion responsible for
myofibrillar swelling, as the ions from sodium acetate failed
to induce swelling. It was theorized by Hamm (1960) and
again by Offer and Trinick (1983) that if a substantial
number of Cl~ were bound to the filaments at high NaCl
concentrations, the negative charge on the filaments would
increase, resulting in an increased electrostatic repulsive
force that would induce filamental swelling. Offer and
Trinick (1983) further concluded that as the salt
concentration increases, the attachment of the cross-bridges
(actomyosin) weakened. At the same time, increased Cl~
binding causes increased electrostatic repulsive forces.
These authors concluded that as long as the cross-bridges
remain attached, the myofibrillar lattice network cannot
swell to the same degree, and that if the lattice does swell,
then the cross-bridges cannot remain attached. When the
lattice swells, the thick filament will depolymerize allowing
water uptake to occur.

37
The use of NaCl and phosphates in a restructured meat
product facilitates extraction of the salt soluble proteins
(Theno et al., 1978a). Salt and phosphate contribute to the
disruption of muscle fibers during mixing, solubilization of
the myofibrillar proteins and the production of an exudate
rich in solubilized proteins. Restructured products made
without added salt and phosphate did not possess the desired
textural properties and were rated as unacceptable by a
sensory panel. Theno and co-workers (1978a) demonstrated
that massaging raw meat for 24 hours without the addition of
salt and phosphate would not permit an acceptable binding
between meat pieces. The addition of salt or phosphate alone
was not sufficient to attain an acceptable binding, but when
both were used in the proper combination, there was a
positive synergistic effect on binding. However, Ford et al.
(1978), in an effort to reduce the added salt content of
restructured products, determined that additions of crude
myosin extracts with sarcoplasmic proteins had the ability to
bind meat pieces into a cohesive restructured product.
Further support of this work was reported by Siegel and
Schmidt (1979a) using isolated crude myosin extractions as a
binding agent between meat peices as stated previously.
Bard (1965) studied the influence of temperature, mixing
time, pre-rigor and post-rigor meat addition and level of
added salt on the extractability of salt soluble proteins
from muscle tissue. Temperatures in the range of -5° to 2°C

38
provided maximum protein extraction and increasing mixing
times up to 16 hours increased protein extraction. Protein
was more readily extractable from pre-rigor meat than
post-rigor meat, and a sodium chloride content of 10%
extracted the greatest amount of protein. In contrast to
these findings, Gillett et al. (1977) reported the optimum
temperature for protein extraction to be 7.2°C, with
extractability decreasing at 0°C. However, this difference
is probably a result of the different experimental conditions
that existed between studies. Gillett et al. (1977) used a
shorter extraction time (6 min vs 30 min), a higher salt
concentration (6% vs. 3.9%) and a higher solvent to meat
ratio (3:1 vs. 2:1) than Bard (1965).
The addition of salt to processed meat products has also
been reported to increase the flavor, texture and/or
juiciness ratings of restructured steaks (Cross and
Stanfield, 1976; Huffman, 1979; Mandigo, 1974; Mandigo et
al., 1972; Neev and Mandigo, 1974; Schwartz, 1975). Salt has
been, and to many people still is, considered to be an
essential part of our everyday lives. However, research has
established a relationship between sodium intake and
hypertension (Altschut and Grommet,1980; Pearson and Wolzak,
1982). As a result, many health conscious consumers are
avoiding foods that contain elevated sodium levels, and in
particular, processed meat products. In response, meat
processors are reducing the sodium content of their products

39
by decreasing the amount of salt used during processing.
Reducing NaCl levels, however, has decreased the functional
properties and characteristics (water binding ability and
texture) of the product (Sofos, 1983; Trout and Schmidt,
1986) . In an effort to regain some of the functional
properties without greatly increasing the sodium content of
the product, meat processors are utilizing food grade
phosphates (Trout and Schmidt, 1983).
Influence of phosphates
Mahon (1961) indicated that the type and amount of
alkaline polyphosphates added to meat would increase the pH
by 0.1 to 0.4 units. Trout and Schmidt (1983) theorized that
the alkaline nature of the polyphosphates was the primary
factor in producing the altered pH effect. However, when
NaCl was added, the pH of the meat system decreased by 0.1 to
0.2 units. These same researchers theorize that the effect
of NaCl on pH is due to the displacement of hydrogen ions by
sodium ions on the meat surface and that the liberated
hydrogen ions produce the change in pH.
The ability of phosphate compounds to enhance the uptake
of water by meat has been known for some time (Bendall,
1954; Hamm, 1960; Sherman, 1961; Ranken, 1976; Offer and
Trinick, 1983). Phosphates can be used to buffer, sequester
metal ions, and increase the ionic strength of solutions.
Phosphate compounds have also been reported to promote the

40
extraction of myofibrillar proteins from meat pieces (Kotter
and Fisher, 1975; MacFarlane et al., 1977; Siegel et al.,
1978a,b; Theno et al., 1978a,b,c; Offer and Trinick, 1983;
Trout and Schmidt, 1986) .
Phosphates are salts of phosphoric acid. The two
general classes of phosphates are orthophosphates and
polyphosphates (Shimp, 1983). Orthophosphates contain a
single phosphorus atom while the polyphosphates contain two
or more phosphorus atoms. Orthophosphates are made by
partial or complete neutralization of phosphoric acid with an
alkali source. This reaction replaces one or more of the
three available hydrogen atoms on phosphoric acid with alkali
metal ions (Shimp, 1983). Monobasic orthophosphates have one
hydrogen atom replaced with an alkali metal. Dibasic
orthophosphates have two hydrogen atoms replaced, and
tribasic orthophosphates have all three hydrogens replaced
with an alkali metal.
Polyphosphates are produced by heating mixtures of
orthophosphates to high temperatures causing them to condense
into phosphate chains. Pyrophosphate is the simplest
polyphosphate containing two phosphorus atoms, while sodium
hexametaphosphate is one of the largest containing 10 to 15
phosphorus atoms. Pyro- and tripolyphosphate are white
crystalline solids containing one or three phosphorus atoms,
respectively. When phosphorus atoms exceed three chain

41
lengths the atoms are no longer crystalline, but amorphous
structures, commonly called glassy phosphates.
Buffers have the ability to maintain a constant pH when
components of a different pH are added to the system.
According to Shimp (1983), orthophosphates provide the best
buffering capacity, while ability to buffer decreases as
chain length increases.
Sequestering metal ions refers to a chemical process of
tying up metal ions in solution so that the ions cannot
participate in chemical reactions. Long chain polyphosphates
are the best sequestering agents for metal ions such as
calcium and magnesium (Shimp, 1983).
The three basic chemical functions of phosphates-pH
buffering, sequestering metal ions, and polyvalent anionic
properties-provide many beneficial effects in food systems
(Shimp, 1983). These effects include color stabilization,
water binding, prevention of coagulation, texture
improvement, emulsification, dry acid leveling, fast curing,
nutritional enhancement, and easier processing (Shimp, 1983).
Pyrophosphate and tripolyphosphate are two common
phosphate compounds added to processed meat products. They
are used to reduce water loss during cooking and to improve
the texture of the product (Ellinger, 1972) . Trout and
Schmidt (1986) stated that phosphates increase the functional
properties of meat products in one or more of the following
ways: (a) by increasing the pH and ionic strength of the

42
product; (b) by dissociating actomyosin into actin and
myosin; (c) by binding to the meat proteins. A
generalization or ranking of the ability of different food
grade phosphates to increase the functional properties of
meat occur in the following order: 1) pyrophosphate; 2)
tripolyphosphate; 3) tetrapolyphosphate; 4) hexametaphosphate
and orthophosphate (Bendall, 1954; Shults et al., 1972; Trout
and Schmidt, 1984; Trout and Schmidt, 1986).
Trout and Schmidt (1986) studied the effects of various
types of phosphates, at different pH and ionic strengths and
their ability to influence the functional properties of
restructured beef rolls. Semimembranosus muscles were
removed 48 hr postmortem and trimmed of all visual fat and
connective tissue. Initial pH of all muscles was between 5.4
and 5.8. Muscles were ground through a 2.5 cm plate and
mixed by hand. The additives used were deionized water (5%
of the product weight), sodium chloride and disodium
phosphate (as analytical reagent grade), and the following
food grade phosphates: tetrasodium pyrophosphate (PP), sodium
tripolyphosphate (TPP), sodium tetrapolyphosphate (TTPP) and
sodium hexametaphosphate (HMP). The treatments utilized the
six phosphate types, three ionic strength levels ((0.15,
0.29, and 0.43), and three pH levels (5.50, 5.95, and 6.35).
The phosphates were used at a constant ionic strength of
0.055 and the different ionic strengths were obtained by
varying the NaCl content. Product pH was controlled by

43
adding 1 M NaOH or HC1 during product mixing. Beef rolls
were thermally processed to an internal temperature of 70°C
in an air agitated, thermostatically controlled retort.
Increasing the ionic strength (from 0.15 to 0.43) and pH
(from 5.50 to 6.35) produced increases in the cooking yields
and tensile strength. Both of these properties increased
linearly with increasing ionic strength and increasing pH
until reaching maximum values and then plateauing. These
maximum values occurred when the pH and ionic strength was
between 5.95 and 6.35 and 0.29 and 0.43, respectively (i.e.,
at NaCl concentrations between 1.7 to 2.5% and 1.4 to 2.4% in
the absence and presence of phosphates, respectively). The
majority of the increase in cooking yield (53%) was due to
the increase in ionic strength, while the increase in tensile
strength (26%) was attributed to the increase in pH. All
phosphate sources produced synergistic increases in cooking
yields and tensile strengths when ionic strengths were
greater than 0.15. The ability of phosphates to produce the
synergistic effects decreased as their chain length
increased. In addition, the ability of phosphates to
increase tensile strength at high ionic strengths could not
be reproduced simply by increasing the pH or by increasing
the ionic strength with only NaCl.

44
Water Distribution
Fresh meat at slaughter contains approximately 75%
water. The main structural component of meat is the
myofibril which occupies approximately 70% of the volume of
lean tissue (Offer and Trinick, 1983) . The majority of the
water in meat is associated with the myofibrils, occupying
the spaces between the thick and thin filaments.
The tissue water of an animal can be divided into two
compartments: 55% intracellular (ICF) and 45% extracellular
(ECF). The extracellular space (ECS) is the fluid
compartment situated externally to the cells of the body
(Law, 1982). Law (1982) reviewed the techniques and
applications of determining ECS in mammalian tissues. The
ECS consists of the plasma component of the vascular space
and the interstitial fluid (Law, 1982). The volume of the
ECS within a tissue is calculated by adding the plasma
component to the interstitial fluid component.
Experimentally, this is determined by introducing a marker
molecule into the space and determining its concentration at
equilibrium. Law (1982) indicated a marker should have the
following characteristics: 1) ready and uniform distribution
throughout the entire anatomical ECS; 2) exclusion from the
cells; 3) no influence on the size of the ECS; 4) non-
metabolizable; 5) uniform molecular size and diffusion; 6)
easy and accurate estimation at low concentrations (i.e.,

45
involves use of radioisotopic labling); and 7) minimal loss
of the marker by urinary elimination or lymphatic draining.
Several different saccharides and ion molecules have
been tested in trying to satisify the requirements stated
above. Of these, the compound inulin (which is readily
available as the 3H-methoxy- or 14C-carboxylic acid compound)
has been the most widely used. Other radio labeled
saccharides that have been used include sorbitol, mannitol,
sucrose and raffinóse.
The earliest reported attempts to measure ECS were those
of Fenn (1936) using tissue chloride levels. Although the
values obtained using this method were not grossly misleading
for whole body content or in tissues with low intracellular
chloride (e.g., skeletal muscle), they were unacceptable for
tissues with high concentrations of intracellular chloride
(e.g., intestinal, cardiac and vascular tissue) (Law, 1982).
Ions such as sulphate, bromide and iodide and compounds such
as thiosulphate and thiocyanate have been evaluated and found
to occupy spaces greater than those available for markers of
higher molecular weight (Law, 1982). Law (1982) indicated
that under a given set of physiological conditions, a unique
anatomical space will exist and the measured ECS will
decrease as the molecular weight of the marker increases.
This was explained on the basis that markers of high
molecular weight fail to penetrate fully the ECS or that
lower molecular weight markers penetrate the cell. Thus,

46
several factors are capable of contributing to the over- or
under-estimation of the ECS.
Law (1982) concluded that no conclusive evidence
currently exists that recognizes an ECS marker as being
rigidly excluded from cells. Also, in isolated tissue slices
in which markers do not have to cross a capillary wall, the
marker is not able to penetrate instantaneously the ECS.
This is viewed as a problem in classical equilibration
experiments. The measured ECS may also be over-estimated due
to the entry of marker into damaged peripheral cells. The
use of tritiated markers (3H) has presented some problems
because of their known ability to exchange H-atoms in
functional groups, resulting in an overestimation of the ECS.
Williams and Woodbury (1971) indicated that inulin may also
become bound by connective tissue causing an over-estimation
of the ECS. A lack of, or a reduction in, the normal
proportion of oxygen in skeletal muscle during ECS
measurements has been reported to cause measurable increases
in the interfiber space (Law, 1967). Law (1967) used an
oxygenated saline solution containing rat muscle to study the
distribution of 14C-labeled sucrose. Histological
examination of these muscles indicated distorted muscle fiber
patterns which were interpeted as indicating severe
physiological deterioration of the muscle. It was concluded
that even though previously oxygenated Ringer's solution was
utilized, tissue hypoxia was responsible for this occurrence,

47
and doubted the validity of such a method as a means of
extracellular space examination.
Law (1982) indicated several factors that could
contribute to an under-estimation of the ECS. Under¬
estimation normally occurs when the marker is not adequately
able to penetrate the ECS, or it does so at a very slow rate.
Ogston and Phelps (1961) reported that hyaluronic acid-rich
mucopolysaccharides present in connective tissue create a
partial resistance to inulin and possibly other large
markers, effectively reducing the ECS estimate. The use of
highly charged markers to estimate ECS, e.g., sulphate, may
be impeded or exaggerated by the presence of fixed charges
within the tissues (Law, 1982).
A variety of techniques, independent of or complimentary
to the use of marker molecules, have been reported for
estimation of the ECS. However, these alternative methods do
not seek to express ECS in precise quantitative terms. The
value of these methods lies in their ability to a) detect
rapid changes and b) to visualize small but significant
changes in specialized areas of the ECS (Law, 1982). These
methods include 1) autoradiography to follow uptake of
inulin (Stirling, 1972), 2) light or electron microscopy to
determine total tissue ECS outlined by chemical markers
(Prosser et al., 1960), and 3) electrical resistivity or
potential differences that rapidly occur in the dimensions of
lateral cellular interspaces (Schultz et al., 1974).

48
To date, the majority of mammalian skeletal tissue
studies designed to study ECS have relied on one of the
following methods: tissue perfusion, in situ or in isolation,
or determination of washout kinetics following marker
equilibration in nephrectomized animal models. The
equilibration procedures involves soaking or incubating small
muscles or strips of muscles in a Ringer-lactate solution
containing 0.3% inulin according to the procedure of Heffron
and Hagarty (1974), modified by the use of low oxygen tension
or incubating muscle strips in 14C-inulin as described by
Vaccari and Maura (1978).
Heffron and Hagarty (1974) studied the rate at which
fiber diameter changed during the development of rigor mortis
in the biceps brachii of the mouse. They reported a 14 to
16% decrease in fiber diameter when the muscle entered rigor,
followed by an increase in ECS. In addition, total muscle
volume (fibers + ECS) did not change during rigor
contraction. Measurements of the ECS determined at 1, 2, 3,
4 and 24 hr postmortem indicated increases of 49.7, 76.7,
83.5, 135.7 and 432.9 % respectively in ECS. The authors
concluded that the decrease in fiber diameter when the muscle
entered rigor mortis was associated with a depletion in ATP.
The authors describe two hypotheses to explain their results.
The first hypothesis was that ATP may act as a "plasticizer"
for the sarcolemma in the same manner it does for the
myofibrils, and that fiber shrinkage or contraction results

49
when ATP supplies are completely exhausted. The second is
that the interfiber fluid becomes hyperosmotic soon after
death, causing movement of the intrafiber water to the ECS
and resulting in a decrease in muscle fiber diameter.
A study designed to relate changes in the mechanical
properties and ECS of beef semitendinosus and biceps femoris
muscles during the onset of rigor mortis was presented by
Curri and Wolfe (1980). It was suggested that intrafiber
water was a significant factor contributing to the tensile
and adhesive properties of muscle; it should be considered as
equally important as the state of contraction and the
collagen angle of the connective tissue network when
assessing muscle tenderness. They presented the following
hypothesis to convey the importance of intrafiber water to
muscle tenderness: during early post-mortem, muscle pH is
high, water-binding capacity of the contractile proteins is
high and ATP levels are high. This results in low tensile
and extensibility properties. As the pH drops, the
water-binding capacity of the proteins decreases. In
addition, the ECS was shown to increase as rigor progressed
until pH 5.9, which agreed with observations of Heffron and
Hegarty (1974). Associated with this increase in ECS was an
increase in the tension and extensibility. Curri and Wolfe
(1980) indicated that the initial increase in ECS was
expected, but the occurrence of a brief unexpected decrease
in ECS near pH 5.95 followed by another increase in the ECS

50
back to its previous volume was not expected. In an
explanation of this occurrence, the authors hypothesized that
the release of Ca2+ from the sarcoplasmic reticulum or other
Ca2+ containing organelles within the fiber created a
hyperosmotic intracellular region, causing water to move from
the ECS back into the fiber. The secondary increase in ECS
was attributed to the continuing decline in pH. As the pH
continued to decline, the isoelectric point of the
sarcoplasmic and contractile proteins was approached, causing
some proteins to undergo denaturation and lose their ability
to bind water. The increase in "loose" water intracellularly
could cause a dilution effect of the Ca2+ ion and the
extracellular region becoming hyperosmotic again. This would
promote water movment out of the fiber and into the ECS. The
information obtained from these experiments helped to explain
the observed changes in tensile and adhesive measurements
that occur during the onset of rigor mortis.
The reagent grade inulin used in their previous work
(Currie and Wolfe, 1980) was not pure enough to provide
reasonable value estimations for the ECS and over estimated
the volume. To overcome this drawback, Currie and Wolfe
(1983) utilized the ECS procedure of Vaccari and Maura
(1978). Highly purified inulin [14C] carboxylic acid was
used as the extracellular marker to determine the location of
water in the post-mortem muscle. Incubating muscle strips in
inulin [14C] carboxylic acid provided a means in which to

51
assess the functionality of the muscle membranes. The
authors expressed hope that this research would provide an
avenue through which the variations in water-holding capacity
and the interfilamental spacing of meat and thus meat quality
could be futher advanced.
Heat-Induced Changes in Meat
It has been established that the heating of muscle
tissue during processing or cooking changes the chemical and
physical composition of muscle proteins and that these
changes influence the palatability characteristics of the
final product. When meat is heated to a certain temperature
range, the proteins in the muscle cells undergo
denaturation/coagulation with a subsequent loss in solubility
(Hamm and Deatherage, 1960; Hamm/ 1977; Cheng and Parrish,
1976; Leander et al., 1980; Moller, 1981; Martens et al.,
1982). "Denaturation" is a change in the specific steric
conformation of a protein, i.e., a change in the secondary
and tertiary structure without a chemical modification of the
amino acids (Hamm, 1977). Fennema (1985) described
denaturation as a process in which hydrogen bonds,
hydrophobic interactions, and salt linkages are broken and
the protein unfolds. A protein molecule in its natural state
consists of a backbone chain of amino acids intertwined in a
•'native'1 structure. The native molecules may exist in
solution (i.e., sarcoplasmic proteins in meat) or as natural

52
aggregates (i.e., myofibrillar proteins and collagen fibers).
Intramolecular forces function to hold the native protein
structure together. However, these forces can become
strained or broken as the ambient temperature of the protein
increases, leading to thermal denaturation. Heat induced
protein denaturation does not occur as an "all or none"
process, but rather as a continuous process with various
regions of the protein molecule changing at different rates
depending on the rate and duration of heating (Paul and
Palmer, 1972). The application of heat to a native protein
structure is said to cause chain unfolding. Unfolding the
chain exposes the interior of the previously protected
internal chain which results in changing affinity for other
molecules (Martens et al., 1982). Thus, denaturation is
considered to be a physical process and not a chemical one.
When protein affinity increases, the degree of aggregation
between protein molecules will increase. Depending on the
physical properties of the native protein, the precipitating
or coagulating particles will form strong, continuous,
water-binding gels, as in egg white (Hegg et al., 1979).
However, if the affinity decreases, a solubilization of the
native components may result. Martens et al. (1982)
concluded that increases or decreases in affinity were
dependent upon which affinity was mechanically stronger.
In a meat protein system, the denaturation of protein
structures may result in changes in the physical properties

53
of meat such as water holding capacity (WHC), thermal
diffusivity, heat conductivity, porosity, etc. The influence
of heat on the structural components of meat has been the
subject of a number of studies (Hamm and Deatherage, 1960;
Trautman, 1966; Hamm, 1966; Hamm, 1977; Cheng and Parrish,
1976; Bouton et al., 1981; Bouton and Harris, 1981; Moller,
1981; Martens et al., 1982; Ziegler and Acton, 1984a,b).
Hamm (1966) reported on various physical and chemical changes
that muscle tissue undergo as it is heated from 20°C to above
80°C. Heating of beef muscle produces a stepwise series of
physical and chemical changes as it undergoes thermal
denaturation. From 20° to 30°C, no changes occurred in the
physical or chemical properties of muscle proteins. Heating
from 30°-50°C resulted in an increase in tissue pH and
rigidity, followed by a decrease in water-holding capacity.
During heating, peptide chains initially undergo an unfolding
process, yielding new unstable cross-links which results in a
tighter protein structure. Between 50°-55°C rearrangement of
myofibrillar proteins continues, and newly formed cross
linkages become stable. At 65°C most of the myofibrillar and
globular muscle proteins are coagulated. Collagen shrinks at
temperatures around 63°C and may be practically transformed
into gelatin. Between 70°C and 90°C disulfide bonds are
formed due to the oxidization of sulfhydryl groups
originating from actomyosin. Disulfide bond formation
continues to occur with increasing temperatures between 70°

54
and 90°C. Above 90°C, hydrogen sulfide (H2S) is split off
from the sulfhydryl groups of actomyosin and collagen is
transformed to gelatin, resulting in an increase of
tenderness.
Hamm (1977) reviewed the changes muscle proteins undergo
during heating of meat. Heating actomyosin to temperatures
above 40°C removed the Ca2+ sensitivity of actomyosin, which
resulted in an increase in ATPase activity. The heating
effect on actomyosin ATPase was theorized to be responsible
for producing conformational changes in the actomyosin
complex. The temperature of maximum ATPase activity was
reported to occur between 43° and 47°C, however increasing
the temperature above this range resulted in inactivation and
irreversible denaturation. Heating actomyosin to 60° to 70°C
produced an increase in sulfhydryl (SH) groups. The increase
in SH group content was thought to occur as a result of an
unfolding of the protein molecules during heating. The
temperature at which actomyosin begins to release SH groups
was reported to coincide with the temperature at which
maximum ATPase activity and maximum change in conformational
changes occurred (45°C). Increasing the temperature to 70°C
did not produce additional SH groups, but between 70° and
120°C the total number of SH groups was reported to decrease
as a result of oxidation of SH to disulfide (SS) groups.
Heat coagulation of myofibrillar proteins was not considered
to occur as a result of SH oxidation, but rather as a result

55
of intermolecular association of other side-groups on the
molecules. In summary, between 30° and 50°C, the
myofibrillar proteins undergo an unfolding of the protein
molecule, followed by protein coagulation and a loss of
enzyme activity.
Because isolated myofibrillar proteins might not respond
the same as those in the intact fiber, Hamm (1977) reviewed
the changes incurred during the heating of muscle fibers or
tissue. At temperatures between 40° and 60°C, myosin
proteins reportedly broke down into smaller compounds, while
actin molecules underwent changes in its helical structure.
Myofibrillar proteins reportedly underwent their greatest
decrease in solubility at temperatures between 40° and 60°C
and became essentially insoluble at temperatures above 60°C.
This decrease in protein solubility coincided with a decrease
in Ca2+-activated ATPase and Mg2+-activated ATPase in
myofibrils. However continuous heating for 7 hr at 55°C did
not result in complete solubilization. It was concluded that
the temperature range yielding the maximum change in
solubility seemed to be about the same in the intact muscle
fiber or the isolated state. However, ATPase activity did
not follow this trend. ATPase activity decreased faster in
solution than in the muscle fiber when stored at 35°C.
Heating of muscle from 30° to 70°C increased the number of SH
groups, indicating an unfolding of the protein molecules as
previously observed for isolated myosin and actomyosin. The

56
relative changes in SH and SS groups occurring in meat was
considered to be important because 97% of the SH and SS
content of muscle tissue is bound to myofibrillar proteins.
At temperatures above 80°C, SH and SS content decreased due
to oxidation to cysteic acid or by the splitting off of H2S.
The amount of H2S released increases exponentially with
increasing temperatures. In addition, the amount of H2S
produced increased significantly as the fat content of the
meat increased. Problems arise when the the production of
H2S occurs during the heating of processed canned meat
products. H2S can corrode the interior of a tin can,
discolor the contents and produce an unfavorable or offensive
smell when the can is opened.
When muscle tissue was heated to temperatures between
40° and 60°C, the pH of the system increased in a manner
similar to that reported for myofibrillar proteins.
Associated with the shift in pH is a simultaneous shift in
the isoelectric point of the myofibrillar proteins (when
measured as the pH at which water-holding capacity is at a
minimum). The increase in pH and isoelectric point was
reportedly due to an increase in available basic protein
groups. It was theorized that some imidazolinium groups of
histidine are initially masked in the native myofibrils, and
become uncovered as actomyosin unfolds due to heating (Hamm,
1977).

57
The decrease in myofibrillar solubility between 30° and
60°C was attributed to the unfolding of the protein chain
followed by protein coagulation. Protein coagulation was not
attributed to the formation of SS bonds resulting from SH
group oxidation because coagulation occurred at temperatures
below the temperature at which the formation of SS begins.
The influence of pH on the water-holding capacity of raw meat
and meat heated to between 30° and 50°C revealed the presence
of unstable cross-linkages. These occurred between unfolded
protein chains that tightened as the isoelectric point of the
proteins was approached (Hamm, 1977).
Hamm (1977) in the same review also reported on the
changes that connective tissue proteins undergo when
subjected to heat. Collagen fibers shrink from a quarter to
a third of their initial length at 60°C while at higher
temperatures collagen is transformed into water-soluble
gelatin. Although meat contains several types of connective
tissue proteins, collagen is considered to be the most
important thermolabile protein of this type because of its
ability to influence the eating quality of the final product.
Paul (1963), Hamm (1966) and Draudt (1972) theorized
that heat-related changes which influence meat tenderness
result from two opposite effects. First, the changes that
connective tissue undergoes apparently has a tenderizing
effect and second, hardening of myofibrillar proteins imparts
a toughening effect. Dutson and co-workers (1976) utilized

58
two muscles that had been stretched to various sarcomere
lengths (1.35-2.60 um and 1.70-3.25 um) and differed in
collagen content (13.13 and 2.47 mg collagen/g of muscle).
Differences in tenderness of these muscles were related to
differences in connective tissue content at all sarcomere
lengths measured. This finding was thought to be due to a
shortening of both connective and muscle tissue fibers, which
resulted in decreased muscle tenderness, whereas in the low
connective tissue muscle, only the shortening of muscle
fibers influenced tenderness. Martens et al. (1982)
concluded that the resultant strength of connective tissue in
meat was dependent upon several factors: the amount of
collagen in the sample (as influenced by animal type and
muscle type), the case of collagen gelatinization during
heating (varied with the age of the animal) and the method of
cooking in terms of time and temperature. Lawrie (1985)
reported myofibrillar tenderness to be dependent on several
factors: the extensibility of fibrils
(stretching/shortening) as influenced by the state of rigor
mortis contraction, pH of post-rigor muscle and time and
temperature used to cook meat.
Deng et al. (1976) hypothesized that protein
denaturation produced an intramolecular swelling and
structural loosening of the protein as opposed to an
unfolding of the protein structure. The shrinkage of tissue
and the release of juice during heating of muscle tissue is

59
due to changes in myofibrillar proteins. Hamm and Deathrage
(1960) and Hamm (1960, 1966) studied WHC of muscle protein as
a function of temperature. The WHC started to decrease
slightly at 30°C, decreased significantly between 40° and
50°C, remained constant from 50° to 55°C, decreased again in
the range of 55° to 70°C, and was considered to be at its
lowest level at 80°C. However, later reports indicate that
weight loss from meat started to be significant at 60°C or
higher (Bengtsson et al., 1976; Nykvist and Decareau, 1976;
Godslave et al., 1977a,b). This implies a weak relationship
between weight loss and WHC.
Bengtsson et al. (1976) measured temperature and water
distribution in bovine semimembranosus muscle as functions of
cooking time. Muscles were oven roasted at 175° or 225°C
from initial temperatures of -20° and +5°C. Temperature
profiles as related to heating time were reported, as were
corresponding moisture and fat content profiles. Moisture
and temperature profiles were inversely related to each
other, with temperature minimum and moisture máximums
occurring near the sample center. Fat content had no
significant influence on any parameters measured. Heating
time was shorter and yield was lower at 225°C than at the
175°C cooking temperatures. Cooking time increased 50% when
cooking from the frozen state. Weight loss was reported to
occur almost entirely by evaporation from the product surface
up to 65°C. Above 65°C, weight loss became significant due

60
to liquid drip. Time/temperature profiles of weight loss for
thin slices of meat indicated that cooking temperature was
more important than the time required to produce the first
drip loss. The importance of this issue to meat tenderness
warrants additional detailed discussion.
Godslave et al. (1977a) studied water emission rates and
the mechanism of water loss (drip) from the surface of frozen
bovine semitendinosus muscle samples during oven roasting
(dry heating) temperatures between 121°C and 204°C and an air
flow rate of 13.7 m3/h. Muscle fiber direction was oriented
parallel to the direction of air flow within the cooking
environment. The moisture (drip) emission rate data
contained two constant rate periods followed by a falling
rate period. In general, moisture emission rate curves for
the samples exhibited peaks rather than plateaus, and in both
studies, temperature and time were found to be related to the
amount of weight lost (Godslave et al., 1977a). The
magnitude and duration of both the first and second constant
rate periods were reported to be dependent on the oven
temperature. Oven temperatures of 177°C or 204°C produced
greater water emission rates that were shorter in duration
when compared to oven temperatures of 121°C or 149°C. The
first constant rate period occurred when the surface
temperature of the product was 100°C. This was said to
produce moisture loss resulting from water vaporizing from a
boiling front that moved slowly inward. The second constant

61
rate period began when the protein at the interior of the
sample started to heat denature in the temperature range of
57°C to 67°C. The water released by denaturation flowed to
the surface of the sample. This action was said to wash out
the effect of the inwardly traveling boiling front and more
surface evaporation. The second constant rate period was
reported to end and the first period begin again when the
weight ratio of water to protein decreased to two. During
this time period water was still evaporating near or at the
product surface but the fraction of wetted surface was
continuously decreasing. The second falling rate period
started when the weight to water ratio was approximately one
(Godslave et al., 1977a). The rate at which the falling rate
period occurred was temperature dependent, with the higher
temperatures approaching zero more rapidly (Godslave et al.,
1977a).
A basis for understanding water emission behavior from
muscle tissue during cooking has been provided by Godslave et
al. (1977a). Muscle was viewed as a wet porous medium with
protein forming the porous matrix and water the wetting
fluid. Water emission from cooking muscle (as a heated
porous medium) occurs when protein transformation gives rise
to an increase in water mobility and matrix shrinkage. In
porous material, water flows by capillary action such that
inside a porous body there exists a complicated network of
interconnected pores and passages with some opening to the

62
surface of the solid. When the solid is wet, the pores are
filled with water. During drying, water evaporates from the
surface at the mouths of pores. This process produces a
meniscus at the product surface that draws water from the
internal network to the exterior of the solid by surface
tension forces. Hence, a smaller pore with a large meniscus
curvature will have a greater interfacial tension capable of
drawing water from the larger pores. Thus, during drying the
larger pores will drain first, provided they do not collapse
on themselves and the empty pores will fill with air.
Because the amount of moisture in a solid is finite, there
comes a point in time when the larger pores run out of water
and the water layer on the surface starts to recede into the
sample in the vicinity of the larger pores. Therefore as the
drying process procedes, air occupies more of the pore space
and eventually the water no longer covers the walls of the
pores with a continuous film. As a result, pool structures
occur within isolated areas of the pore network (Godslave et
al., 1977a). Knowledge of the processes that influence the
rate at which heat penetration occurs within a meat product
is important to minimize the energy required for thermal
processing and yield losses.
Hung (1980) using a modified version of the oven
previously utilized by Godslave et al. (1977a,b), studied the
relationship of water loss to muscle shortening and protein
denaturation during oven roasting of frozen bovine

63
sexnitendinosus muscle. Muscles were cut into cylindrically
shaped samples with fibers oriented parallel to the axis of
the cylinder. Two sample sizes were used, 100 g and 600 g.
The respective dimensions (length x diameter) of these
samples were 10.8 cm x 3.49 cm for the 100 g sample and 19.1
cm x 6.35 cm for the 600 g sample. In agreement with the
previous work of Godslave et al. (1977a,b), Hung (1980)
concluded that increasing the oven temperature increased the
amount and rate at which water was lost. However, the amount
of weight loss was not dependent on the orientation of the
sample fibers. Because of this finding, it was hypothesized
that the majority of weight loss was not due to the effect of
gravity. Hung (1980) also reported observing two distinct
drip periods which agreed with previous reports by Godslave
et al. (1977a,b). During the first drip period, the drip
amount for vertical or 45° oriented samples was greater than
for horizontal samples. It was suggested that, it is more
difficult for water to migrate across the fibers than along
the fibers and that gravity played a role in determining the
amount of drip in this period. When previously frozen
samples were allowed to partially thaw, only one drip period
occurred. The amount of drip was small, red in color and
appeared viscous and turbid. Hung (1980) concluded that the
first drip period occurred when the interfiber ice crystals
near the surface or cut ends thawed. Part of this liquid was
absorbed by the muscle fibers, and the rest migrated parallel

64
in the direction of the fibers or reached the bottom and/or
ends of the sample where it either formed a drip or
evaporated. If the rate of thawing is slow compared to the
rate of absorption, it is possible that absorption could be
sufficiently effective to pick up most of the thawed liquid.
According to Ramsbottom and Koonz (1939) and Wang et al.
(1954), if meat samples are rapidly frozen (e.g., -150°C),
both interfiber and intrafiber ice crystals occur. If the
meat samples are slowly frozen (e.g., -17°C), only interfiber
freezing takes place and the muscle fibers are partially
dehydrated. Slow freezing also results in larger ice crystal
formations, which can act as tiny knives to cut or rupture
myofiber cell membranes and contribute to muscle dehydration.
During the second drip period, the drip was clear and
evaporated explosively when contacting the pan. Thus it was
considered to be composed mostly of water. Meat surfaces
appeared dry, or at least partically dry corresponding to the
first peak of the drying curve. However, as the cooking
process continued, liquid drops appeared on the previously
dry surface and continued to grow until they dripped from the
sample. Hung (1980) implied that the liquid drops were
squeezed out of the meat samples due to shrinkage and
gravity. As muscle protein is heat denatured, the rate of
mass transfer increases greatly, possibly due to 1) cracking
across muscle fibers and 2) damage to muscle cell membranes
(Paul, 1963; Davey and Gilbert, 1976).

65
Changes in tenderness of meat that occur during cooking
are considered to be influenced by heat-induced changes in
the myofibrillar and stromal structural protein components of
muscle tissue. In mammalian skeletal tissue, the myofibrillar
proteins, i.e., actin and myosin, constitute 50 to 55% of the
total protein. Myosin is the predominant protein in prerigor
meat, whereas actomyosin is the predominant protein complex
in postrigor meat. The fibrous actin and myosin in
myofibrils can be histologically identified in raw and cooked
(time and temperature dependent) muscle samples. Hung (1980)
employed transmission electron microscopy (TEM) to evalulate
structural changes that occurred during cooking of bovine
semitendinosus muscle and found a normal distribution of
sarcomere lengths for raw samples (mean = 2.5 microns).
However, a two peak distribution for cooked samples appeared
at 2.05 microns and 1.55 microns. These peak values
suggested that two chemical reactions were involved in
sarcomere shortening. The first reaction caused a decrease
of sarcomere length from 2.5 urn to 2.05 um. The second
reaction caused a shortening from 2.05 um to 1.55 um and was
thought to be responsible for water loss during cooking.
Cooked muscle samples that contained long sarcomers had
fibrous looking I-bands (actin filaments), while short
sarcomeres contained nonfibrous looking I-bands. The two
sarcomere distribution peaks that were previously described

66
(2.05 and 1.55 microns) were reported to represent the two
types of I-band structures (fibrous and nonfibrous).
Disruption of myofibrils upon heating has been reported
(Giles, 1969; Jones et al., 1977; Hung, 1980; Leander et al.,
1980). Myofibrillar breaking points were reported either at
Z-I junctions (Giles, 1969; Hung, 1980; Leander et al., 1980)
or at A-I junctions (Giles, 1969; Jones et al., 1977).
Therefore, breaks in myofibrils occurring during heating are
thought to involve the I-band region of a sarcomere (perhaps
at the weak link point).
Draudt (1972) suggested that heat acted to solubilize
connective tissue providing a tenderizing effect, while
toughening myofibrillar proteins. These changes were
temperature dependent, such that myofibrillar protein
coagulation offsets the tenderization effect of any
additional collagen solubilization at temperatures above 60°C
and results in a decrease in tenderness of beef cooked beyond
the rare to medium-rare state.
Numerous researchers (Machlik and Draudt, 1963; Bouton
and Harris, 1972a,b; Davy and Gilbert, 1974; Hamm, 1977;
Bouton and Harris, 1981) have reported that meat tenderness
was greater at final internal temperature of 60°C than at
50°C. Draudt (1972), in a review, stated that the decrease
in shear force value that occurred as internal temperature
increased from 50°C to 60°C was due to the shrinkage of
collagen. However, Bouton and Harris (1972b) concluded that

67
the effect was dependent on the age of the animal and related
it to changes in connective tissue strength. Davey and
Neiderer (1977) suggested that heating muscle tissue to 65°C
increased proteolytic enzyme activity and improved meat
tenderness by reducing myofibrillar tensile strength.
Futhurmore, heating to temperatures above 65°C improved
tenderness through a reduction in the structural contribution
of the connective tissue. From this discussion, it is
obvious that some disagreement exists between the earlier
work of Machlik and Draudt (1963), Bouton and Harris (1972b)
and Davey and Gilbert (1974). It has also been reported by
Bouton and Harris (1981) that Warner-Bratzler (WB) shear
force values decreased for veal muscles as cooking
temperatures were increased from 50°C to 60°C. Increased
proteolytic enzyme activity at these temperatures, which may
produce an accelerated aging condition, did not appear to
explain the effect since there was a substantial decrease in
shear force when cooking temperatures were increased from
50°C to 60°C, even when the meat had been aged (7 wk at
5°-6°C) or when cooked for 24 hr. Bouton and Harris (1981)
concluded that even at these relatively low temperatures,
changes in connective tissue were involved since: 1) the
magnitude and direction of the changes in shear force with
increasing temperature was dependent on animal age and
cooking time, and 2) the effects of increasing cooking
temperature and/or time on the adhesion strength between the

68
meat fibers was significantly greater for samples from
younger animals.
The most dramatic changes that occur in meat as a result
of heating are the shrinkage and hardening of tissue, release
of juice and discoloration caused by changes in the muscle
proteins (Hamm, 1977).
Cheng and Parrish (1979) used SDS-polyacrylamide gel
electrophoresis to study the heat induced changes in the
solubility of myofibrillar proteins from bovine longissimus
muscle. Muscle samples were diced (particles size of 1 cm3),
placed into glass test tubes and heated in a water bath to
45°, 50°, 55°, 60°, 70°, and 80°C and held at the designated
temperature for 30 min. In addition, a control (raw) muscle
sample was also included for comparison. The heated and
control muscle tissues were homogenized and the myofibrillar
proteins extracted with 25 ml of 0.6M KC1, 0.1M K phosphate,
pH 7.4 for 1 hr and centrifuged at 15,000 x G for 15 min.
Because the control (raw) sample and samples heated to 45°,
50°, and 55°C contained residue of unheated protein, 1 mM
MgCl2 and 1 mM sodium pyrophosphate were added to aid in
suspension and separation of the protein supernatant. The
SDS-polyacrylamide gels indicated that the extractability of
actin, myosin and Z-disk myofibrillar proteins react
differently to heat. The heavy and light chains of myosin
were reported to be the first major proteins to become
insoluble at 55°C. This was in agreement with the earlier

69
work of Locker (1956) who heated purified myosin and reported
that 82 to 92% of the protein became coagulated at 53°C.
However the thin filament proteins, including actin,
tropomysin and troponin T and I, became more extractable with
heating and were reported to be more heat resistant than
myosin. Troponin T and tropomyosin bands were more intensive
between 45° and 60°C than in unheated samples or samples
heated at 70° or 80°C, indicating their ability to resist
denaturation. The appearance of a 30,000 dalton component
within the gels was used as an indication that troponin T had
been degraded. The presence of this 30,000 dalton component
was reported to occur in samples heated at 55° and 60°C. The
observation that this 30,000 dalton component was more
prominent after heating led the authors to conclude that
calcium-activated factor (CAF) activity was stimulated during
heating. Actin was reported to become insoluble between 70°
and 80°C and tropomyosin and troponin became insoluble above
80°C. In response to these findings the authors theorized
the following possible explanations: a) the loss of
alpha-actinin solubility at 50°C results in weakening the
I-Z-I protein bonds and allows release of thin-filament
proteins; b) because actin was still soluble and myosin
insoluble at 55°C, a weakening or dissociation of the thin
filament proteins occurred allowing their release into
solution; and c) the action of CAF activity on Z-disks
permits an increase in the extractability of thin filament

70
proteins. It was concluded that the state of the Z-disk and
thin filament proteins were a major factor to be considered
when determining the level of tenderness in bovine
longissimus muscle. Knowledge of these changes and the study
of protein denaturation are important when trying to
understand the mechanisms by which heat and mass transfer
occur in meat during heating.
Microwave Heating
Copson (1975) and Decareau (1985) provides an excellent
source of basic references for heating with microwaves and
microwave power engineering. Together these two books
provide invaluable background information regarding microwave
heating properties as related to food.
Decareau (1985) described microwaves as a form of low
frequency non-ionizing electromagnetic energy, like radio and
television waves. In terms of frequency, microwaves lie
between television waves and infrared waves. The two ISM
(Industrial, Scientific and Medical) frequencies assigned by
the FCC (Federal Communications Commission) for microwave
heating in the U.S. are 915 and 2450 MHz. Microwaves are
capable of penetrating materials such as wood, water and
food. In addition, they are capable of passing through air,
vacuum, glass, paper and some plastics such as teflon.
However, they are reflected by metals or perforated metals
with holes much smaller than the wavelengths of the

71
microwaves. A 3.2 mm hole (1/8 inch) in metal is small
enough to reflect 2450 MHz microwaves.
Hung (1980) described the three basic components
contained within a microwave heating apparatus: the
generator, the waveguide assembly and the cavity. The
generator is considered to be the major part of the microwave
oven. Two types of microwave generating tubes are presently
used: the klystron and the magnetron. The klystron tube
possess higher or stronger power than a magnetron.
The waveguide is a rectangular piece of metal tubing
that transmits the power from one end to the other. A
waveguide assembly can be either a single component or a
combination of several components. Each component can be a
waveguide equipped with particular microwave hardware
capable of controlling or monitoring microwave transmission.
The design of the cavity is related to the uniformity of
the microwave field in it. The cavity is the chamber that
accepts the microwave energy and holds the product that is to
be heated. Another device associated with the cavity is
called a mode stirrer and functions to improve distribution
and uniformity of the microwave field. It consists of a
rotating metal fan that acts to reflect and distribute the
microwaves that contact it.
Electromagnetic waves produced by microwave ovens are
rapidly absorbed by water molecules present in food. This
form of energy is transformed into a random thermal motion of

72
water molecules. A water molecule will rotate in the
presence of the electric field of a microwave oven due to the
electric charge within the molecule. Walker (1987) offered
the following explanation on the physics of microwaves and
the water molecule. The electrons associated with hydrogen
atoms are shifted toward the eight protons in the oxygen
atom. The shift leaves the oxygen end of the molecule
negative and the hydrogen ends positive, resulting in a
charge distribution called an electric dipole. Normally the
dipole moments in water are randomly oriented. If an
electrical field is imposed, however, it creates a torque on
each molecule. The torque causes the molecule to rotate in
an effort to align its dipole moment with the imposed
electrical field. Therefore, a microwave oven operating at a
frequency of 2450 MHz attempts to rotate a water molecule at
2.45 X 109 rotations per second, and as a result the
temperature increases. Bakanowski and Zoller (1984)
described how this heating process occurs within foods. Some
molecules within food are electrically polarized and will
respond to the applied electromagnetic field by oscillating
in synchronization with it. These molecules are electrically
coupled to the rest of the food, and through this coupling,
the energy of oscillation is passed on as an increased
thermal motion. If the source of the electromagnetic field
is removed, the polar molecules stop oscillating in
synchronization with the field and no additional heating

73
occurs. However, a redistribution of the heat already
deposited will occur as a result of temperature gradients
established during the microwave heating. The redistribution
of heat results from thermal conduction and is not due to
microwaves "left behind" after the magnetron is turned off.
In a microwave oven when the magnetron is turned off, the
production of microwave energy ceases to exist in both the
oven and the food.
Microwave ovens have only been on the market for a
little more than two decades, yet they appear to have
revolutionized the way Americans prepare food. Microwave
ovens have opened up a new dimension in food preparation and
management both in the home and in food service processing.
In 1984, the largest annual shipment of any home appliance in
history was claimed for microwave ovens at 9.1 million units
(Markov, 1985a). In a survey of 2000 American households
nationwide, nearly 60% had microwave ovens, while about 50%
had dish washers (MRCA, 1987).
The greatest advantages of microwave cooking are its
time and energy savings. Meat can be cooked four or five
times faster and require approximately 75% less energy in
comparison with conventional methods (Moore et al., 1980;
Hoffman and Zabik, 1985). Markov (1985b), in an overview,
reported of the microwave oven market concluded that
excellent meals could be prepared with microwave technology.
However, the majority of consumers reported that they use

74
their ovens primarily for reheating and defrosting of foods.
The microwave has not been well accepted by homemakers and
food services for reheating or cooking of muscle tissue due
to uneven cooking, greater cooking losses, and less palatable
meat (Markov, 1985b). It is important to realize that the
microwave heating characteristics of a food product may vary
considerably with the processing frequency, temperature,
chemical composition, and physical state of the product
(Mudgett, 1982).
In developing products for microwave processing,
Schiffmann (1986) stressed that microwaves are a form of
energy, not a form of heat. The energy is only manifested as
heat upon interaction with a material as a result of one or
more energy transfer mechanisms. The heating of materials by
microwave energy is influenced by the oven equipment and the
material being heated (Schiffmann, 1986). Designing a
microwave cooking process involves understanding the thermal
properties of the food in question, and a number of
interrelated electrical properties. These properties vary
extensively with the processing frequency and product
time-temperature profiles which can affect transmission of
microwave energy at the products surface and energy
absorption by the product (Mudgett, 1986).
In a review, Schiffmann (1986) indicated the following
factors that must be considered when developing a
product/processing system: processing frequency, power

75
level, moisture content, product density, product geometery,
conductivity properties and specific heat of the product.
The depth to which microwave energy is capable of
penetrating into a food product is dependent upon the
frequency used to produce the electromagnetic microwave
energy. The primary difference between heating at 915 MHz
and 2450 MHz is in the differing penetration depths. The 915
MHz frequency has a longer wavelength which produces a
greater effective penetration depth of 33 cm compared to 12.2
cm for the shorter 2450 MHz frequency. Microwave energy at
915 MHz has an initial advantage in penetration depth but
loses penetration depth as the temperature of the product
increases. Nykvist and Decareau (1976) stated that 44 times
more energy reached the center of a 12 cm thick beef slab at
915 MHz compared to 2450 MHz. The frequency selected is
important, because it relates to the size of the object being
heated. In general, a large 220 kg block of frozen material
would be processed better at 915 MHz, while cooking an
individual sausage patty should be done at 2450 MHz.
The speed of microwave heating (power output) is usually
controlled by varying the power level setting. The speed or
rate at which microwaves heat is often the most attractive
feature of microwave heating. However, it is possible to
heat too rapidly, such that heat can be generated faster
than the product can keep up with it. When this occurs, the
outer regions of the product become over heated, which

76
results in excessive loss of product moisture and decreased
palatability. Another problem associated with excessive
heating rates is non uniform temperature distribution. This
occurs because the heating rate may be so fast as to prevent
effective thermal conductivity of the heat to the cooler
interior regions. The author suggested "heating fast; but as
slow as possible" (Schiffmann, 1986).
Nykvist and Decareau (1976) studied the effect of roast
diameter (6 to 14 cm) on the resulting temperature profiles
when appling 275 W of effective heating power generated at
915 MHz or 2450 MHz. These researches concluded that greater
energy dissipation occurred near the roast surface for the
2450 MHz frequency, resulting in higher surface temperatures,
in less power penetration and less energy being "focused"
and in relatively low center temperatures. However, for 915
MHz as the surface heated up the penetration depth decreased,
thus decreasing the amount of energy reaching the roast
center. From these results it would appear that to attain
optimum microwaving conditions for meat entrees the product
should initially be heated at 915 MHz to attain interior
heating followed by 2450 MHz for surface heating. The
authors stated that methods that promoted radial (uniform)
microwave penetration, such as a perfect cylindrical shape
roast would provide a more uniform temperature profile.
Schiffmann (1986) also agreed that the physical geometry
(size and shape) of a product influences the heating

77
properties of the product in several ways. He indicated that
the size of an individual product should be considered when
selecting a microwave frequency for heating. For example,
915 MHz would be more effective at thawing a 200 kg block of
meat because of greater penetrating characteristics than to
2450 MHz which produces greater surface heating. In
addition, sharp edges and corners should be avoided because
of their tendency to overheat. Schiffmann (1986) stated that
cylindrical shaped products tend to avoid this problem and
should therefore be considered when designing a microwavable
product.
The moisture content of a product is considered to be
one of the most important factors influencing how well the
product will absorb microwave energy. Usually, the more
water present in a product, the higher the dielectric loss
factor will be for the product. This should result in
superior heating of the product. At very low moisture
levels, the water is considered bound and not available to be
affected by the rapidly alternating microwave field. Product
density affects the dielectric constant properties and hence,
the heating of the product. As the density of the material
increases, so does its dielectric constant.
The transmission properties of electromagnetic energy
relate to the depth of penetration from the product surface
inward. Penetration depths are reported to increase as the
moisture content of the product and processing frequency are

78
decreased. Very porous materials, such as bread, because of
the air inclusions, are considered good insulators. As a
result heat transfer into these products is difficult and
slow.
The conductivity of a product describes the ability of a
material to conduct electric currents by displacing electrons
and ions. In a microwave system, dipolar rotation is the
most frequently discussed means of generating heat. The
presence of sodium chloride ions in the water matrix of a
product acts to increase the heating rate. When sodium
chloride dissociates in water, the positive and negative ends
of a water molecule are electrically attracted to the charged
ions. The electric field of a microwave drives the hydrated
ions through the water, pushing the sodium ions in the
direction of the field and the chloride ions in the opposite
direction. Whenever hydrated ions bump into water molecules,
energy is transferred, and the water is subjected to
additional heating.
The specific heating properties of a product can cause a
material which has a relatively low dielectric loss value
(low water content) to heat well in a microwave field. An
example of this effect is the ability of oils to heat faster
than water because of their lower specific heat.
The dielectric properties collectively reflect the
ability of a material to store and dissipate electrical
energy and, consequently, determine the product's ability to

79
act as an insulator. However, most foods are poor
insulators. As a result, they typically absorb a large
portion of the energy produced in a microwave field. Energy
absorption by the product is said to be instantaneous and
causes internal heating of the product. As a result the
dielectric properties and subsequent cooking properties of
food products in the liquid or semisolid state depend
primarily on their moisture, salt, and solid contents (Kent
and Jason, 1975,* Mudgett et al., 1980; Mudgett, 1982).
Microwave cookery has been shown to decrease cooking
time, labor and energy costs, but has not been well accepted
by food services or homemakers for cooking beef roasts due to
uneven cooking, greater cooking losses, and less palatable
meat when compared to conventional heating methods (Headley
and Jacobson, 1960; Marshall, 1960; Kylem et al., 1964; Law
et al., 1967; Ream et al., 1974; Drew et al., 1980; Moore et
al., 1980; Griffin et al., 1981). In further support of
this, Taki (1986) reported that homemakers still approach
meat cookery in a microwave oven by a trial and error
approach.
The scientific literature on microwave cooking of beef
or other muscle tissues has not been overly complimentary.
Comparisons between microwave and conventionally cooked meat
has indicated differences in sensory attributes, cooked
yields, microbial quality, and physical or chemical
characteristics of the final product, depending upon the

80
cooking method (Pollack and Foin, 1960; Marshall, 1960;
Korschgen et al., 1976; Drew et al., 1980; Moore et al.,
1980; Bodrero et al., 1980; Zimmermann, 1983; Sawyer et al.,
1984; Sawyer, 1985).
Marshall (1960) reported on the use of an "electronic
oven" in meat cookery. In her study, paired five pound
pieces of choice grade top round of beef were roasted in an
"electronic oven" or in a conventional oven. The author
indicated that in previous studies utilizing the "electronic
oven" the internal temperature of the product would rise
approximately 11°C after removal from the oven. Therefore,
roasts cooked in the "electronic ovens" were cooked fat side
down for one-half to two-thirds of the time and then turned
fat side up until an internal temperature of 80°C was reached
and then removed. The other half of the paired roasts were
cooked in a 148°C electric oven fat side up until an internal
temperature of 80°C was reached. The average cooking time
for roasts prepared in the "electronic oven" was 23.5 minutes
per kilogram compared to 100.0 minutes for the conventional
oven. The author also indicated that the shape of each roast
was such that one end was smaller than the other. As a
result of this uneven shape, the small end on roasts prepared
in the "electronic oven" became excessively brittle and
porous and it was deemed unpalatable. In addition, the fiber
hardening effect was reported to occur along all of the edges
and corners of the these roasts. Cooking losses included

81
losses due to drip, evaporation, and trimming of cooked
surface fat. "Electronic oven" prepared roasts averaged
60.6% cooking loss compared to 34.7% for conventional
cookery. Appearance and palatability of the roasts as judged
by a six-member taste panel indicated that roasts prepared in
the "electronic oven" were rated lower in appearance,
tenderness, juiciness, and flavor when compared to those
cooked conventionally. The author concluded that a method of
cooking whereby a more satisfactory product is obtained is
needed before the "electronic oven" will be practical for
roasting top round of beef to a well-done degree of doneness.
Korschgen and coworkers (1976) compared quality factors
in beef, pork, and lamb cooked by microwave and conventional
means. Regardless of meat species cooked, microwave cooked
roasts were prepared in less than half the time required to
prepare conventionally cooked roasts. The cooking loss
percentage for all three species indicated that the greatest
losses occurred via evaporation. Microwave cooked beef had
a smaller cooking loss compared to conventional cooking,
while there was no difference between pork and lamb roasts.
Shear force values indicated no difference due to cooking
method for beef and lamb, however, microwave cooked pork
roasts had lower shear force values than conventionally
prepared roasts. Sensory analysis indicated that no one
cooking method was superior for all three species. Beef and
lamb samples were significantly less tender when cooked by

82
microwaves compared to conventional cookery. No meaningful
trends were apparent in sensory scores for juiciness across
meat species. However, the interior portion of
conventionally cooked beef roasts was scored significantly
juicier than were those from microwave cookery. The authors
concluded that aside from the time-saving advantage for
microwave cooking, there were no major advantages for
microwave cooking over conventional cooking.
Drew and coworkers (1980) compared the effects of
cooking top round beef roasts from the frozen and thawed
states at different microwave power levels and conventional
methods on energy consumption, cooking times, cooking losses,
and palatability. The microwave oven used in this study
operated at 2450 MHz and on power levels of "high" (553
watts) or "simmer" (237 watts). Conventionally cooked roasts
were prepared using a still-air electric oven set at 163°C.
Roasts were cooked uncovered in the conventional oven and
were loosely covered with waxed paper when cooked in the
microwave oven. When compared to the conventional oven less
time was required to cook frozen or thawed roasts to the same
internal temperature when the roasts were cooked in the
microwave oven regardless of power level. Energy consumption
data indicated that about half as much electricity was
required to cook roasts in a microwave oven as compared to
conventional oven cookery. In addition, there was no
difference in the amount of electrical energy used between

83
"high" and "simmer" power levels. Cooking losses included
drip and volatile components and when added together yielded
a total cooking loss. Roasts cooked conventionally from the
frozen state had less drip (3%) and volatile losses (30.3%)
than microwave cooked roasts which had 5.6% and 36.4%,
respectively, for drip and volatile losses at high power and
8.4% and 29.2%, respectively, on low power. Roasts cooked
from the thawed state had less drip (8.3%) and volatile
losses (23.2%) than microwave cooked roasts which had 15.0%
and 26.4%, respectively, on high power. Total cooking losses
were significantly higher for roasts cooked at the "high"
microwave power level than for those cooked in a conventional
oven. However, when roasts were cooked at the "simmer"
microwave power level, the total loss was not significantly
different from those cooked in the conventional oven.
Sensory evaluation scores and shear force values for roasts
cooked from the thawed state did not differ for overall
acceptability, flavor, juiciness, and tenderness due to
microwave cooking method ("high" or "simmer") versus
conventional cooking. Roasts prepared from the frozen state,
regardless of cooking method had lower scores compared to
scores for thawed roasts. There was no difference between
conventional and microwaved "simmer" cooked roasts prepared
from the frozen state for sensory characteristics. However,
shear force values were lower for conventionally cooked
roasts than for roast cooked at either microwave power level.

84
In general, roasts cooked from the frozen state using "high"
microwave power had lower (less desirable) sensory scores
when compared to all other cooking methods.
Moore and coworkers (1980) studied differences among top
round steaks cooked by dry or moist heat in a conventional or
a microwave oven. The authors used a Gardner Color
Difference Meter to access the degree of doneness of each
steak and concluded that steaks were heated more evenly by
conventional dry heat than by conventional moist or by
microwave dry or moist heat. In addition, cooking time,
evaporative cooking losses, total moisture content, and
sensory juiciness and tenderness scores were less, and total
and drip cooking losses, and ether extract were greater for
steaks cooked by microwaves than for conventionally cooked
steaks.
Korschgen and Baldwin (1980) compared the quality of
beef rib roasts cooked by manually cycling a microwave oven
on and off so as to simulate the automatic cycling control
for microwave energy. Both microwave cooking methods were
compared to conventionally cooked beef rib roasts as a
control. Sensory panel scores indicated that regardless of
cooking method used, all roasts were deemed acceptable in
flavor and juiciness. Mean sensory scores for tenderness
indicated significantly lower (less desirable) scores for
roasts cooked by the manual pulsing procedure compared to
conventionally cooked roasts. There was no difference in

85
tenderness scores for automatically cycled microwave energy
compared to conventional cooking. Energy requirements were
lower and total cooking losses were higher for meat prepared
by microwave power regardless of cycling method (Korschgen
and Baldwin, 1980). The authors concluded that automatic
cycling permitted equilibration of heat developed within the
product. This transfer of heat within the product is due to
conduction from one region of the roast to another.
The issue of bacteria in food surviving in large numbers
after thermal processing by microwave radiation compared to
conventional hot air processing was studied by Sawyer and
coworkers (1984). The purpose of their study was to
determine the effect of plastic wrapping on the internal
end-point temperature and on the survival of bacteria in food
subjected to thermal processing in a microwave oven. Single
serving sized portions of chicken drumsticks, ham slices and
pork loin slices were cooked from the frozen state in a
microwave oven using 630 watts of power. Microbiological
counts of wrapped-vented and unwrapped foods were made before
and after microwave processing for Staphylococcus aureus
surface inoculated on to chicken drumsticks and ham slices.
Salmonella senftenbera surface inoculated on to ham and pork
slices indicated that wrapping did not have a statistically
significant effect on internal end-point temperature or on
counts of bacteria per gram of product tested. Wrapping
generally provided a slight improvement in microbial quality

86
when mean counts were considered. Schiffmann (1981) and
Ohlsson (1983) both indicated that the increased occurrence
of bacteria surviving in foods processed in microwave ovens
was due to a lack of a uniform microwave field. The lack of
field uniformity results in hot and cold spots occurring
within the microwave oven.
Zimmermann (1983) studied the effects of microwave
thermal processing on the survival of Trichinella spiralis.
the causative agent of trichinosis. In this study the author
indicated the difficulty in attaining 76.7°C throughout a
pork roast when subjected to microwave thermal processing.
Zimmermann (1983), in an attempt to cook pork roasts in a
microwave oven to 76.7°C, failed to do so 149 out of 189
attempts when following the oven manufactures and pork
industry recommendations. Zimmermann (1983) suggested that
low wattage cooking at 50% or less would give any trichina
present longer exposure to heat and, thus, provide an
approach to safe cooking methods. In this study some roasts
were still infective after cooking at 30% power for 46.2
t «
min/kg. This research futhur emphasizes the lack of
uniformity in heat distribution in microwave cooked products.
In a recent report, Welke et al. (1986) evaluated the
effect of microwave, convection and conventional cooking
methods on the texture of top round roasts when epimysial
tissue from one to eight year old animals was physically
inserted into the roasts (approximately 2000 g each).

87
Results of their study were that Warner-Bratzler shear values
for old epimysial tissue cooked in the microwave oven was
lower than shear values for old epimysial tissue cooked by
convection or conventional ovens (5.0, 7.7, and 8.4 kg,
respectively). Roasts cooked by the microwave method
required significantly shorter cooking times than did roasts
cooked by convection or conventional methods (97, 146, or 186
min, respectively). Microwave and convection cooked roasts
cooked to an internal temperature of 63°C experienced an 8°C
post-cooking temperature rise over a 30-min period, whereas
conventionally cooked roasts were heated to an end-point
temperature of 71°C. These authors suggested that lower
shear values from epimysial tissue from old animals for the
microwave method was due to an increase in collagen
hydrolysis when compared with convection and conventional
cooking methods. This supports the work of Law et al.
(1967), McCrae and Paul (1974) and Hutton et al. (1981), but
is in contrast to the theories of Van Zante (1973), Roberts
and Lawrie (1974) and Peckham and Freeland-Graves (1979) who
suggested that use of the microwave oven does not allow time
for collagen solubilization and tenderization. Factors to be
considered when producing a microwavable meat product are fat
percentage within the product and post-cooking temperature
rise. The effect of cooking method on fat percentage and
cooking yields for ground beef patties was reported by Berry
and Leddy (1984). Beef patties from ground round, ground

88
chuck and regular ground beef containing 14, 19, and 24% fat,
respectively, were cooked by six different methods and
analyzed for compositional differences. Percentage of
cooking yield, fat, and moisture of cooked patties were
significantly affected by the interaction of fat level and
cooking method. Except for patties cooked by broiling or
convection heating, patty yields decreased with increasing
fat levels. Microwave cooking always produced patties
containing the least fat and caloric content in comparison
with other methods since cooking losses were greater.
The duration and extent of post-cooking temperature
elevation in microwave cooking were reported by Ruyack and
Paul (1972), Sawyer (1985), and Welke et al. (1986). Ruyack
and Paul (1972) cooked choice beef semitendinosus muscles in
a 915 MHz, 1600 W microwave oven and reported a 2°C/min
post-cooking temperature elevation in roasts covered with a
polyester film and an 1.6°C/min increase in uncovered roasts.
Sawyer (1985) reported that experimental product processed in
a hot air oven did not exhibit post-cooking temperature
elevations. However, chicken frankfurters processed in a
microwave oven at 50% power had a 2.1°C greater post-cooking
temperature elevation than frankfurters processed at 100%
power. It was concluded that the extent of post-cooking
temperature rise may be related to power level used during
processing. Thus, post-cooking temperature elevation may be
more commonly associated with microwave heating than with

89
conventional heating when time of processing is kept constant
(Ruyack and Paul, 1972).
When beef is cooked in a microwave oven, water heats the
solid material. However, the surface temperature never
reaches a temperature greater than 100°C. This temperature
is not high enough to denature fully oxymyoglobin, thus the
surface never becomes dark brown. Also, the meat seldom
develops the flavor and aroma of meat cooked in a
conventional oven (Walker, 1987).
Even though microwave technology has made great strides
forward in the areas of increased speed, convenience and
futuristic computerized programmed appliances, this technical
sophistication has not been matched by the development of
beef entrees compatible with the microwave oven. A recent
survey indicated that one-third of the microwave oven owners
prepare more than three-quarters of their meals in their
microwave ovens and another one-fourth prepare more than half
of their meals that way (Taki, 1986). While consumers are
cooking more meals in their microwave ovens, research
indicates that the incidence of cooking meat entrees is
seldom (Taki, 1986).

CHAPTER 3
PREDICTING FINAL INTERNAL TEMPERATURE THROUGH THE USE
OF POST-COOKING TEMPERATURE RISE IN REFORMED BEEF ROASTS
COOKED WITH VARIABLE MICROWAVE POWER LEVELS
Introduction
As a result of changing life styles, consumers are
demanding convenience in meat entrees. One possibility is a
ready-to-cook roast beef product reformed from denuded chuck
muscle that can be cooked with microwave energy. Previous
work has indicated that microwave cooking of meat results in
greater cooking losses and less palatable meat than
conventional methods (Korschgen and Baldwin, 1976; Nykvist
and Decareau, 1976; Sawyer, 1985). Nykvist and Decareau
(1976) indicated that early research efforts on microwave
roasting of beef did not take into consideration the high
post-cooking temperature rise (PCTR) associated with
microwave roasting. As a result, roasts were often
overcooked when compared to controls, and therefore deemed
lower in palatability.
Moore et al. (1980) indicated that conventional oven
roasting of top round steaks with moist heat produced a 2°C
post-cooking temperature rise compared to a 10°C increase for
moist microwave cooking. Drew and coworkers (1980)
90

91
acknowledged that preliminary experiments had to be conducted
to establish the extent to which PCTR occurred in association
with microwave cookery (no values given) prior to conducting
their research. Sawyer (1985) identified the presence of an
extensive PCTR, which was highly variable in duration and
intensity, in food entrees subjected to microwave heating.
Experimental products were cooked in a microwave or a
conventional hot air oven and tested for PCTR. Some of the
products included chicken frankfurters, pork roast, turkey
roast, and cake cones. Experimental products processed in a
conventional hot air oven did not exhibit a PCTR. However,
microwave heating produced PCTR of 8.5°C + 6.5°C, 2.9°C ±
1.2°C, 6.1°C + 3.7°C, and 0, respectively. The time required
for each of these PCTR values to occur varied from as little
as 45 sec for chicken frankfurter to 16.2 min for turkey
roast. From these results it was suggested that PCTR was
more likely to occur in products processed with microwave
power, dependent on the type of product heated and possibly
the power level used. The author concluded that the duration
and intensity to which PCTR occurs should be given
consideration when commercial products are to be processed in
microwave ovens, or when developing mathematical models of
microwave cooking/heating procedures (Sawyer, 1985).
Nykvist and Decareau (1976) and Decareau (1985) allude
to the presence of a large temperature gradient existing
between the interior and the outer regions of a meat product

92
when subjected to microwave energy. The magnitude of
thistemperature gradient appears to be dependent upon several
factors, particularly, power level and duration of heating.
The presence of this large temperature gradient is thought to
be the driving force responsible for the large and varied
PCTR occurring in microwave heated meat entrees.
However, little work on characterizing this PCTR,
particularly in a reformed beef product, has been reported.
In order to cook a roast to an exact final internal
temperature, it appears necessary that this PCTR temperature
be considered.
The objective of this study was to develop a method for
predicting final internal temperature for a reformed beef
roast cooked in the microwave oven with consideration of
PCTR.
Materials and Methods
Preparation of Sample
Twelve beef forequarters from USDA Choice, yield grade 3
carcasses weighing a minimum of 318 kg were used. Latissimus
dorsi (LD) and Serratus ventralis (SV) muscles were removed
in their entirety, and trimmed of surface fat and connective
tissue removed using a hand-held Whizzard knife (Model No.
880). During removal of the respective muscles, starting
forequarter weight and denuded muscle weights were recorded

93
to determine the relative percentage for each muscle.
Denuded muscles were mechanically injected with a
water/salt/phosphate solution to achieve 10% added water,
0.75% NaCl, and 0.35% sodium tripolyphosphate levels in each
muscle using an Inject-O-Mat meat injector (Model No. PSM
10). Muscles were then vacuum tumbled using a Globus tumbler
(Model No. HS8-081). The tumbling cycle consisted of 20 min
of tumbling followed by 10 min of rest for a total time of
five hours. Following completion of the tumbling cycles, the
muscles were prepared for stuffing.
Two SV or LD muscles were positioned in a thick to thin
fashion to help attain uniform thickness and parallel fiber
arrangement. Muscles were stuffed by hand into 12.0 cm
fibrous casings (Viskase Corp., Chicago, IL), using a
modified stuffing horn (Jetnett Corp., Omaha, NE). Prior to
final clip sealing, each log was subjected to vacuumization
conditions to remove air pockets, using a Reiser
vacuum/sealer (Model No. VM-31). Following vacuumization,
each log was tightened to achieve a consistent diameter of
12.5 cm and clip sealed. Logs were placed on wire racks and
frozen overnight in a blast freezer (-30°C).
Individual roasts were prepared by cutting frozen logs
on a band saw. This produced a roast that was cylindrical in
size (12.5 cm dia), approximately 8 cm thick, and weighing
454 g to 570 g. Roasts were individually vacuum packaged and
kept frozen (-20°C) until needed. Roasts were thawed

94
overnight in a walk-in cooler at 4°C for cooking the
following day.
Microwave Cooking
Because microwave ovens are known to produce "hot-spots"
within the oven cavity, a study was conducted to determine
their location and intensity within the J C Penney (Model
No.963-5965-60) 2450 MHz microwave oven used throughout this
study. "Hot-spot" locations within this oven were determined
by measuring the heat absorbed by the change in temperature
of a fixed volume of water contained in a glass beaker and
placed in one of nine possible locations within the oven:
left rear (LR), center rear (CR), right rear (RR), left
middle (LM), center middle (CM), right middle (RM), left
front (LF), center front (CF), or right front (RF). The
microwave was operated on high, medium, and low power levels
for 60 sec for each possible oven location. Effective heat
absorbed at each power level was determined at the center
middle location by heating 1000 ml of deionized water at 20°C
in a 1-liter beaker and measuring the temperature rise. The
heat absorbed was then calculated using the equation q =
M*Cp* T (Copson, 1975) where q = the heat absorbed, M = the
mass (g) being heated, Cp = the specific heat of the product,
and T = the change in temperature.
Roasts, SV and LD, were placed on an Anchor Hocking
microwaveable meat roasting tray with the 12.5 cm roast

95
surface contacting the roasting tray. The roast and roasting
tray were placed in a glass dish to retain cooking drip.
LD and SV reformed roasts were used to study the duration and
intensity to which post-cooking temperature increases
occurred as a result of microwave cooking at power levels of
low, medium and high. This was accomplished by cooking the
respective roasts to a desired internal temperature and then
turning the microwave oven off (turn off temperature (TOT)).
The internal temperature of each roast was monitored
using a Luxtron Fluoropticâ„¢ thermometer and fiber optic
probe, (Model 1000A, Digital Readout Device and Model
GSA-4-10082 probe, Luxtron, Mountain View, CA) on loan from
the National Live Stock and Meat Board, Chicago, IL.
The roast was left in the oven with the oven door ajar.
The internal temperature of each roast was monitored until
it started declining. This procedure was performed
repeatedly at various internal TOT, for each roast type and
power level combination.
The transient nonuniform temperature distribution in a
solid food can be described mathematically by analytical or
numerical solutions to a complex second-order partial
differential eguation describing three dimensional heat
conduction if all thermal properties of the material are
known constants. During the microwave heating of meat
roasts, the thermal properties do not remain constant, but
vary widely with changes in moisture content, temperature,

96
and physical structure of the material. The mathematics
become further complicated in the case of microwave heating
because heat is being generated within the sample in response
to an ill-defined electromagnetic field.
Because of these complexities no attempt was made to use
such mathematical models. Instead, an empirical approach was
adopted based on observations of the transient temperature
profiles at the approximate center of the meat roasts and
statistically correlating the post-cooking temperature rise
with various control variables.
Proximate Analysis
Proximate analysis procedures were performed on
representative samples obtained from each log at the time of
processing individual roasts. The respective samples were
minced using a Krups household food processor (Model No.
700). Moisture, ether extract, and protein percentages were
determined using the methods outlined in AOAC (1980).
Statistical Analysis
A negative exponential function of the time after power
termination was fit to the post-cooking temperature rise.
This is consistent with the exponential temperature response
during transient conduction heat transfer. The equatorial
form was
T = TPT + A(l-exp(-kt))

97
where
T = current internal temperature of roast (°C), at
time t
TPT = internal temperature of roast at time
of power termination (°C)
A = asympotic post-cooking temperature rise (°C)
k = rate constant for heating (min-1)
t = time elapsed since power termination (min)
The parameters To, A and k were fit with the nonlinear
regression procedure (Proc NLIN) of SAS (1987), using
Marquardt's method.
Of several potential equational forms, the negative
exponential was selected for two primary reasons. First, it
contains an asymptotic maximum which is fit directly.
Maximum values of polynomial regressions must be obtained by
differentiating and solving the resultant equation. For a
data set of this size, this was deemed too time consuming.
Thus, a relatively direct measure of PCTR with an associated
variance estimate is obtained rather than an indirect measure
lacking a variation estimate.
The second motivation for the negative exponential is
theoretical. We assume that the rate of temperature increase
at the center probe is proportional to the difference between
the temperature at any given time and the ultimate end point
temperature. This seems a reasonable model of the post¬
cooking diffusion of heat from the exterior to the interior
of the roast. Simplifying assumptions include constant
density and composition of the roast, linear heat transfer,

98
and constant proportionality between heat energy and
temperature.
All possible subset regression was used to find the best
combination of variables to predict asymptotic PCTR (A)
generated by the nonlinear regression using PROC REG of SAS
with selection criteria being adjusted R2. Independent
variables were selected from oven power setting (watts),
internal temperature at power termination (To)(°C), the
natural logarithms of each of these variables and the squares
of each of these variables. Data from both types were pooled
for variable selection. However, after variables were
selected, data were fit separately for the two roast types.
This yielded two slightly different equations. The
prediction equation for A was used for inverse prediction of
TOT to arrive at a desired end point temperature. Goodness
of fit between predicted and actual endpoint temperature was
measured by correlation and t-test (Steel and Torrie, 1980),
using 54 individual roasts in a factorial arrangement of
treatments. Treatment levels were two roast types, three
power levels and three end-point temperatures, replicated
three times.
Results and Discussion
The means and ranges of the LD and SV muscles and their
relative percentage of the carcass weight and forequarter
weight are presented in Table 3.1. The data indicate that

99
Table 3.1. Means and extremes, and standard deviations of
muscle yield characteristics.
Traita
Mean
Minimum
Maximum
S.D.b
HCW (kg)
330.6
342.0
318.0
2.86
FQW (kg)
83.9
80.5
90.5
0.81
FQW % of HCW
(%)
25.3
24.6
26.6
0.18
SVW (kg)
3.35
2.91
3.73
0.075
SV % of HCW
(%)
1.01
0.91
1.09
0.017
SV % of FQW
(%)
3.99
3.49
4.43
0.074
LDW (kg)
1.40
1.09
1.86
0.062
LD % Of HCW
(%)
0.40
0.31
0.55
0.021
LD % of FQW
(%)
1.56
1.51
1.86
0.064
aHCW = hot carcass weight; FQW = forequarter weight;
SVW = Serratus ventralis weight; SV % of HCW (%) = percent
of hot carcass weight due to Serratus ventralis; SV % of FQW
(%) = percent of forequarter weight due to Serratus
ventralis; LDW = Latissimum dorsi weight; LD % of HCW (%) =
percent hot carcass weight due to Latissimus dorsi; LD % of
FQW (%) = percent of forequarter weight due to Latissimus
dorsi.
bS.D. = standard deviation of the mean.
n
12

100
the mean percentage contributions made by the LD and SV to
the forequarter were 1.15% and 3.49%, respectively. In
contrast to these values, Johnson et al. (1988) reported the
percentage contribution of the LD and SV muscles to the lean
portion of the forequarter to be 4.4% and 8.9%, respectively.
When these mean values are expressed as a percentage of the
mean whole forequarter weight, the LD and SV represent 3.36%
and 6.8%. A hand held and operated mechanical Whizzard knife
was used to denude each muscle. This process permitted a
human fatigue factor to enter this aspect of the study which
may contribute an additional source of variation.
Proximate analysis values for uncooked LD and SV roasts
are presented in Table 3.2. Roasts made from LD muscles were
initially designed to be leaner (<10% fat) than roasts
prepared from SV muscles (>10% fat). The data indicate that
the LD roasts contained 6.34% fat and the SV roasts contained
11.22% fat. These fat content values are in agreement with
those presented by Johnson et al. (1988). They reported
denuded LD muscle to contain 6.0% fat and SV muscle to
contain 11.3% fat.
The results of determining heating intensity and
location of potential hot-spots within the the microwave oven
are presented in Figure 3.1. The data indicate the presence
of "hot-spots" occurring at different locations and power
levels within this oven. The variations in heating intensity
and location appear to be more extensive within the high and

101
Table 3.2. Chemical composition of uncooked Latissimus dorsi
and Serratus ventralis roasts.
Muscle
Latissimus dorsi Serratus ventralis
(n = 13) (n = 20)
Mean
S.D.
Mean
S.D.
Moisture
(%)
73.11
1.131
69.99
1.306
Protein
(%)
18.52
.963
16.86
1.007
Fat (%)
6.34
1.224
11.22
2.406
Asha (%)
2.03
. 036
1.93
.041
determined
by difference.
Table 3.
3.
Means and extremes, and standard deviations
(S.D.) of post-cooking temperature rise by roast
type and microwave power level.
Temperature
(°C)
Musclea
n
Power
level
Mean
Minimum
Maximum
S.D.
LD
3
Low
9.71
5.28
18.37
4.32
LD
6
Medium
14.92
7.15
24.14
3.94
LD
4
High
21.57
12.98
32.12
3.94
SV
4
Low
13.88
7.09
20.46
3.17
SV
5
Medium
20.97
12.32
28.38
2.75
SV
11
High
25.85
7.42
36.57
2.36
aLD = Latissimus dorsi; SV = Serratus ventralis.

Figure 3.1. Effect of power level and position within
the microwave oven on the apparent energy
absorbed by 1000 ml of deionized water
subjected to microwave energy for 60 sec.
Locations were LB = left back, CB = center
back, RB = right back, LM = left middle, CM
= center middle, RM = right middle, LF =
left front, CF = center front, RF = right
front.

o
o
0
if)
h:
0
Z5
O
0
Cl
0
10.0T
8.0-
6.0-
4.0-
2.0 - „
0.0
1 ....J Low power (174 W)
V/Á Medium power (342 W)
â– â– High power (523 W)
LB CB
Location within oven
103

104
medium power levels. These differences indicate a
non-uniform distribution of the microwave energy field
occurring within the oven. Based on the location and
intensity (by power level) of the various potential
"hot-spot" locations, it was decided that all roasts prepared
in this study would be placed in the center middle location
of the oven for cooking. Therefore, power wattage output was
measured at the center middle location for the microwave oven
used in this study. It was was determined that the oven
generated 523 watts on high power, 342 watts on medium power
and 174 watts on low power in water placed at the center.
Preliminary research in our lab indicated the presence
of a varied and potentially large PCTR. Means and extremes
of PCTR by roast type and microwave power level are presented
in Table 3.3. The data indicate that the presence and
intensity of the PCTR appears to be influenced by roast type
and microwave power level. The wide range occurring between
minimum and maximum values is thought to be due to the
temperature at power termination (TPT) selected for a
particular roast by power level combination. The data
collected during this phase of the study were used to develop
a mathematical equation to predict the intensity of the PCTR
as influenced by roast type, power level, final end-point
temperature desired, and temperature at power termination.
Results from fitting the PCTR to a negative exponential
curve are shown in Table 3.4. The nonlinear regression

105
Table 3.4. Parameter values obtained by non-linear
regression for post-cooking temperature rise in
Serratus ventralis and Latissimus dorsi roasts.
""Power3 Probe temperature
level at power
(watts) termination A k To
Serratus ventralis
174
21.1
174
37.8
174
48.9
174
71.1
342
21.1
342
33.9
342
35.0
342
44.4
342
60.0
523
26.7
523
32.2
523
35.9
523
43.3
523
48.9
523
50.6
523
54.4
523
71.1
523
76.7
523
37.8
523
64.4
174
20.9
174
49.0
174
71.1
342
20.9
342
37.8
342
47.8
342
60.0
342
60.0
342
71.1
523
35.0
523
49.0
523
20.9
523
76.7
19.6
24.9
9.5
8.3
40.4
31.8
22.8
35.8
15.2
30.7
34.7
43.1
33.7
33.3
34.8
27.3
26.6
37.0
36.5
6.8
Latissimus dorsi
23.6
25.0
6.4
30.5
17.4
26.7
13.6
13.6
5.7
39.2
25.3
42.8
6.3
0.0829
21.1
0.1106
36.3
0.1826
67.9
0.2509
70.9
0.0664
21.1
0.1079
31.9
0.2020
31.9
0.1106
33.2
0.3008
51.8
0.0692
23.2
0.1702
27.5
0.1287
32.8
0.1567
40.9
0.1750
44.9
0.1905
49.7
0.2313
53.0
0.2056
69.1
0.2669
77.5
0.1564
33.9
0.6831
65.3
0.0744
19.5
0.1374
45.6
0.3882
70.6
0.0565
22.4
0.1271
36.0
0.1776
45.5
0.6137
54.4
0.6137
54.4
0.3755
72.8
0.1437
31.8
0.2394
46.2
0.1023
19.7
0.3352
76.7
aA = asymptotic post-cooking temperature rise; k = rate
constant for heating; To = estimated internal temperature at
power termination.

106
algorithm converged rapidly to stable parameter values in all
cases except one, which was then deleted from further
analysis. Final standing endpoint temperature may be
obtained from adding To and A. In all cases, (TPT) closely
approximated the probe temperature at power termination, and
is included as a scaling factor to adjust for temperature
before power termination. Since the primary interest was in
the magnitude of PCTR, further analysis was directed toward
A, the asymptotic PCTR, rather than k, which relates the rate
of PCTR rather than the extent. Asympotic correlation
between A and k within any given roast ranged from .42 to
.86, indicating that the two parameters could be reflecting
different aspects of the same phenomenon. This justified an
emphasis on A, the asymptotic estimate of PCTR.
The variables which best predicted asympotic PCTR were
power level (in watts) and three variables derived from the
temperature at the time of power termination (Table 3.5).
Thus, the predicted value of A from linear regression (Á) can
be expressed as Á = f(power level, temperature,
In(temperature), (temperature)2), A = f(watts, TPT, ln(TPT),
TPT2). While the three temperature variables are collinear
to a moderate degree, they also provide a wider range of
values and account for some nonlinearity of response to
temperature at power termination. Regression coefficients
obtained by variable selection methods such as adjusted R2
are not unbiased (SAS 1987), but are a guide for use on other

107
Table 3.5. Results of variable selection for prediction of
asymptotic post-cooking temperature rise (A).a
Adjusted R2
R2
Variables13
.513
.572
TPT LTPT TPTSQ WATTS
.512
.571
TPT LTPT TPTSQ WATTSSQ
.506
.536
TPTSQ WATTS
.506
.536
TPTSQ WATTSSQ
.506
. 550
TPT LTPT WATTSSQ
an = 34.
^Variables: TPT = meat temperature at power termination (°C)
LTPT = natural logarithm of TPT
TPTSQ = TPT * TPT
WATTS = power setting of oven (W)
LWATTS = natural logarithm of WATTS
WATTSSQ = WATTS * WATTS
Table 3.6. Regression coefficients, standard errors, R2, and
significance of regression for prediction of
asymptotic post-cooking temperature rise (A) in
Serratus ventralis and Latissimus dorsi roasts.
Inter-
Roast cept TPT LTPT TPTSQ WATTS R2 P
SV -328.5 -8.686 165.9
(249.33)a (5.5596) (114.75)
.04780
(.031080)
.04308 .580 .0080
(.013324)
LD -160.0 -3.200
(237.74) (5.4644)
80.27 .009595 .01290 .801 .0032
(111.442)(.0302194)(.011970)
aValues in parentheses are standard errors of the estimates.

108
data. Thus, the four predictor variables were used in
separate regressions by roast (Table 3.6). Although standard
errors of coefficients were large, the overall fit and
significance of the prediction equations were judged
adequate.
To obtain a desired end-point temperature (EPT) it was
necessary to estimate a temperature for power termination
(TPT). Since EPT = A + To, desired EPT and selected power
level can be entered into the equation. Rearrangement leads
to a convergent iterative formula for temperature at power
termination. An iterative form was used since the
transcendental equation in temperature, log(temperature) and
(temperature)2 does not admit a closed analytic solution.
Reasonable initial values for temperature converged to stable
valués within six iterations. The power termination
temperature values obtained in this manner for additional
roasts are in Table 3.7, presented by roast, power level, and
EPT desired.
The prediction equations that were developed as a result
of this work estimate the internal temperature (by roast,
power level used, and final internal temperature desired)
that should be attained prior to terminating the microwave
(Table 3.7). The data indicate a lower temperature at power
termination for high power heating compared to medium or low
power levels. As end-point temperature increased the span
between temperature at power termination and desired

109
Table 3.7. Estimated internal temperature before power
termination needed to attain a desired end-point
temperature for a given power level and roast.
Muscle
desired
EPTa °C
Power level (watts)
Low (174)
Medium (342)
High (523)
Turn off temperature
(°C)
Serratus
60
48
28
22
ventralis
70
63
52
38
75
67
60
52
Latissimus
60
31
31
29
dorsi
70
63
57
53
75
72
68
66
aEPT = desired end-point temperature (internally).

110
end-point temperature decreased. The lower temperatures at
power termination for SV roasts suggests the presence of a
greater PCTR occurring within these roast, which might be
attributed to the roasts' higher fat content.
When tested (n=54), the correlation between predicted
end-point temperature and attained end-point temperature was
r=.996 ± .001 (P<0.0001). Accuracy, as determined by paired
t-test, showed that the predicted and attained values did not
differ (p=.0009) (Table 3.8). The prediction equation
developed as a result of this study accounts for the
post-cooking temperature rise occurring within the product as
influenced by internal temperature of roast at time of power
termination and power level (watts) to achieve a desired
end-point temperature. Attempts to utilize time variables in
developing the prediction equations were non-relevant.
Nykvist and Decareau (1976) indicated that earlier
research failed to consider or account for the much higher
PCTR associated with microwave cooking of roast beef. As a
result roasts were often over-cooked when compared to
controls. The possibility of over cooking with microwave
power in earlier work was probably due to the method by which
temperatures were monitored, usually involving copper or
iron-constantan thermocouples. Nykvist and Decareau (1976)
reported that metallic probes utilized by many researchers in
earlier reports were capable of concentrating the microwave
field, which resulted in over-cooking and charring at the

Ill
Table 3.8. Means and extremes of time lapse during post-cooking temperature rise,
and actual versus desired final temperature, by roast, microwave power
level, and end-point temperature desired.
Roasta
Power
level*5
(watts)
EpijCd
(°C)
Mean
Minimum
Maximum
S
.D.
Time
(m)
Temper¬
ature
(°C)
Time
(m)
Temper¬
ature
(°C)
Time
(m)
Temper¬
ature
(°C)
Time
(m)
Temper¬
ature
(°C)
LD
L(174)
60
17.5
59.1
9.0
58.3
25.0
60.2
8.1
0.9
SV
10.0
58.9
8.0
58.3
14.0
59.4
3.5
0.6
LD
70
3.4
69.6
3.0
69.3
4.0
69.9
0.6
0.3
SV
9.6
69.7
6.0
69.3
17.0
70.4
6.4
0.6
LD
75
3.0
75.4
2.0
74.8
5.0
75.9
1.7
0.6
SV
4.7
75.1
3.0
74.8
7.0
75.4
2.1
0.3
LD
M(342)
60
22.5
59.1
12.0
58.7
34.5
59.4
11.3
0.4
SV
14.3
59.2
14.0
58.3
15.0
60.0
0.6
0.9
LD
70
4.3
69.9
3.0
69.3
6.0
70.4
1.5
0.6
SV
7.6
69.1
4.0
67.7
12.0
69.9
4.0
1.3
LD
75
3.0
74.8
2.0
74.8
4.0
74.8
1.0
0.0
SV
5.0
75.8
4.0
74.8
7.0
76.4
1.7
0.9
LD
H(523)
60
13.0
59.0
9.0
58.9
18.0
59.4
4.6
0.3
SV
11.7
58.6
4.0
58.3
17.0
59.4
6.8
0.6
LD
70
3.7
69.9
2.0
69.3
6.0
70.4
2.1
0.6
SV
19.7
69.2
10.0
68.9
30.0
69.3
10.0
0.3
LD
75
3.0
75.7
2.0
75.4
4.0
75.9
1.0
0.3
SV
4.0
75.2
3.0
74.8
5.0
75.9
1.0
0.6
aRoast, LD = Latissimus dorsi, SV = Serratus ventralis.
kpower level, L = low, M = medium, H = high; n = 3 for each combination

112
probes entrance to the meat, and produced erratic readings at
times.
The data contained in Table 3.7 indicate that to cook a
SV roast on high power to a final internal end-point
temperature of 60°C (rare), the oven power should be turned
off when the internal temperature of the roast reaches 22°C
and the roast allowed to stand. The standing period allows
heat contained in the outer regions of the roast to be
transfered inward by conduction to attain the desired final
end-point temperature. However, when the same high power
level is used to cook an LD roast to the same internal
temperature, the data indicate that the oven should be turned
off when the internal temperature of the roast is 29°C.
Anomalous heating effects are known to occur in
heterogeneous food products that have different phase
properties (Mudgett, 1986). The use of microwave energy to
thaw frozen meat products produces "runaway" heating if a
thermal equilibration period is not permitted. Anomalous
heating in this case resulted due to significant differences
in the phase properties of frozen solids and aqueous ions
(Mudgett, 1986). Still, other mechanisms of interaction
could occur between organic food solids or nonpolar fluids
and high-frequency electric fields which could cause
anomalous heating effects (Mudgett, 1986). The differences
in fat content between LD and SV roasts could be capable of

113
producing different phase properties that might produce
anomalous heating effects.
In support of the statement that fat content of the
roast was the primary factor responsible for different TPT
values occurring between the two roasts, Mudgett (1986)
identified basic types of food products that would likely
produce anomalous heating rates when subjected to microwave
energy, e.g., pizza, jelly filled doughnuts, and liquids with
large solid inclusions,e.g., meat and vegtable soup. In
soup, the conductivity of the continuous liquid phase is
greater than that of the suspended-solids phase. In meat,the
conductivity of the lean muscle tissue is greater than the
that of fat inclusions contained within the product. Mudgett
(1986) classified products of this type to be low-loss
suspensions. Jelly filled doughnuts and frozen foods were
classified as being high-loss suspensions. In the jelly
doughnut, the jelly phase has a high dissolved sugar content
that absorbs microwave energy very effectively, compared to
the flour dough. While pizza products were classified as
layered products, the microwave energy transmitted through
the sauce to the phase boundry between the sauce and the
dough is significantly reduced in strength, with little
energy being transmitted through the dough (Mudgett, 1986).
These classifications of loss factors associated with
microwave heating characteristics of various food products
are thought to result in anomalous heating effects, and

114
relate to the transmission properties of microwave energy.
The absorption of energy from a microwave field is known to
be influenced by the food products' dielectric properties,
size, and geometry, and by the operating characteristics of
the processing equipment (Mudgett, 1982).
The SV and LD roast products developed in this study
would be classified as "low-loss" suspensions according of
Mudgett (1986). The SV roast in particular contained larger
and more frequently occurring fat inclusions throughout the
roast compared to LD roasts. Therefore the fat inclusions
may be the primary factor contributing to the differences in
TPT values for the respective roasts. In contrast to this
theory, Mudgett and coworkers (1974) stated that moisture
content was the most clear-cut correlation that could be
drawn from the effects of composition on the dielectric
properties of meats, and that lipids were considered
essentially to be inert dielectrically based on the earlier
work of Pace and coworkers (1968). Pace and coworkers (1968)
reported on the dielectric properties of commercial cooking
oils. From their work it was concluded that there was little
difference between unsaturated vegetable oils and animal fats
such as tallow and lard in terms of power absorption. In
addition, as the temperature of a sample increased, there was
a tendency for the loss factor (power absorption) to increase
slightly. However, this increase was considered to be too
small for any practical importance, when compared to water.

115
Contrary to earlier statements, Mudgett (1986) reported
that the energy-transfer efficiency (% maximum microwave
power coupled) by 1000 ml of olive oil to be 98% compared to
water at 100%. The author stated that the mechanism for
energy coupling by olive oil was not clear, and that some
mechanism of interaction of the oil with the electric field
other than the rotation of water dipoles or the conductive
migration of dissolved ions must be involved.
Fuoss (1943), as quoted by Pace and coworkers (1968),
studied the electrical properties of various polymers
subjected to microwave energy. At low temperatures, the
polymers possessed high internal viscosities that resulted in
little or no microwave power absorption by the polymer.
However, as temperatures increased, polymer viscosity
decreased and power absorption increased.
Based on these previous reports it could be theorized
that fat inclusions contained within the SV roasts are
capable of influencing the heating attributes of the roast.
First, initial roast temperatures of 4°C yields cold and firm
fat inclusion that possesses poor dielectric properties,
making the product slower to heat. Second, once the fat
inclusions are liquified, they would be capable of absorbing
microwave energy and possibly generating heat due to dipole
rotation, and thus retain greater quantities of heat compared
to water. Finally, the increased heat retained within the
fat inclusions would then be capable of sustaining conductive

116
heat transfer to cooler inner regions for a longer period of
time compared to water. Thus, when SV roasts are cooked the
oven could be turned off at a lower temperature and the roast
contain sufficient heat in its outer regions and liquefied
fat inclusions to finish cooking the product.
Summary
Individual model reformed beef roasts were subjected to
cooking in a 2450 MHz microwave oven operated at high,
medium, or low power levels (523, 342, or 175 watts),
respectively. Microwave cooking, established the presence of
a large and variable post-cooking temperature rise, that was
affected by roast type, power level, and oven turn-off
temperature. To obtain a desired end-point temperature, it
was necessary to estimate an internal roast temperature for
oven turn-off temperature. The following prediction equation
was determined to estimate the final internal temperature
that should be attained prior to temperature at power
termination: Á = b0 + b2LTPT + b3TPTSQ + b4W, where TPT =
the internal temperature of the roast at the time of power
termination, LTPT = the natural log of TPT, TPTSQ = TPT
squares, and W = the apparent wattage at a particular power
level. When tested on 54 roasts, the correlation between
predicted end-point temperature and attained end-point
temperature was r=.996 + .001 (PcO.OOOl). Accuracy, as
determined by paired t-test, significantly indicated that the

117
predicted and attained values did not differ (p=.0009). The
prediction equation developed as a result of this study
accounts for the post-cooking temperature rise occurring
within the product as influenced by internal temperature of
the roast at time of oven power terminated and power level
(watts) to achieve a desired end-point temperature.
The data presented in this report indicate the presence
of a large and variable post-cooking temperature rise
associated with microwave cooking of reformed roast beef
products. The ability to predict and ultimately control the
extent to which post-cooking temperature rises occur in a
meat entree prepared in a microwave oven is critical to
obtaining a palatable product. The data indicated that the
power level utilized (high, medium, or low), temperature at
power termination, and the composition of the roast influence
the amount of post-cooking temperature rise that occurs.

CHAPTER 4
COMPARISON OF MICROWAVE AND CONVENTIONAL COOKERY
AND END-POINT TEMPERATURE ON CHEMICAL, PHYSICAL AND
SENSORY PROPERTIES OF REFORMED BEEF ROASTS PRODUCED
FROM CHUCK MUSCLES
Introduction
The greatest advantages associated with microwave
cooking are the time and energy saving factors. Meat can be
cooked four or five times faster and require approximately
75% less energy in comparison with conventional methods
(Moore et al., 1980; Hoffman and Zabik, 1985). However,
while consumers are cooking more meals in their microwave
ovens, homemakers still consider meat cookery in a microwave
oven a trial and error experience (Taki, 1986).
The skepticism surrounding the use of the microwave oven
for preparation of beef entrees is due in part to uneven
cooking, greater cooking losses, and less palatable meat
(Headley and Jacobson, 1960; Kylem et al., 1964; Law et al.,
1967; Ream et al., 1974; Drew et al., 1980; Moore et al.,
1980; Griffin et al., 1981). Some studies have suggested
that part of the problem may be associated with over cooking
when the post cooking temperature rise (PCTR) is not
considered (Nykvist and Decareau, 1976; Moore et al., 1980;
Drew et al., 1980; Sawyer, 1985). In a recent study, Yates
118

119
(1988) indicated that PCTR ranged from 20°C to 40°C in
reformed beef roasts and was considered to be dependent on
the power level used to cook the roasts. However, major
questions still remain unanswered regarding microwave oven
cookery of beef entrees and the perceived relationship with
toughness and lack of product juiciness.
Microwaves are electromagnetic waves. Walker (1987)
discussed the rapid cooking action associated with microwave
ovens. Heat produced by this form of energy is a result of
the water present in food absorbing the energy waves. A
water molecule, because of its dipole moment, can be made to
rotate by the electric field of a microwave. The dipole
moment is represented by a vector that points from the oxygen
end along the line of symmetry between the hydrogen ends
(Walker, 1987). Ordinarily the dipole moment of water is
randomly oriented. However, when microwaves are imposed, the
dipole vector of water tries to align itself with the
changing microwave field causing the molecule to rotate. The
electrical field of a microwave oven operating at 2450 MHz
(typical household microwave oven) is changing its electrical
field 2.45 billion times per second. As a result, the dipole
moment of water tries to rotate at the accelerated rate. At
the molecular level, microwave heating is caused by the
disruption of weak hydrogen bonds resulting from dipole
rotation of free water molecules and by migration of
dissolved ions (i.e., free salts) (Mudgett, 1982).

120
The most dramatic changes that occur in meat as a result
of heating are the shrinkage and hardening of tissue, release
of juice and discoloration caused by changes in the muscle
proteins (Hamm, 1977). When proteins are heated, they
progress from their native state through an unfolding
denaturation and into a three-dimentional protein matrix of
myosin and actomyosin forming a gelation state. Heat induced
protein denaturation does not occur as an "all or none"
process, but rather as a continuous process with various
regions of the protein molecule changing at different rates
depending on the rate and duration of heating (Paul and
Palmer, 1972). The input of thermal energy into a protein
system is considered to be the single most important factor
influencing the transition from native state to denatured
state (Acton and Dick, 1984). The denaturation reaction
process occurs along a particular path of bond breaking and
bond reformation into new structures at a particular rate.
Ziegler and Acton (1984a) indicated that the perceived
characteristic texture of various processed meat products may
be a function of the protein denaturation process, and its
specific interactions with the continuous aqueous phase and
dispersed fat. Research continues to indicate that gelation
of muscle proteins is largely responsible for the physical
and chemical stabilization of fat and water in comminuted
meat products and for binding between meat pieces in
sectioned and formed products (Hand, 1986). Thus, the

121
palatability problems associated with microwave cooking could
be related to either the rapid rate of heat generation and
its effect on protein denaturation, gel formation and water
retention, or to the heating method itself.
The research presented herein briefly describes
production of two reformed whole muscle roast products
produced from the beef forequarter. The roasts were designed
with microwave cooking considerations as described by Nykvist
and Decareau (1976) and Schiffman (1986) in mind. Roasts
were uniform in size and shape factors deemed necessary for
uniform heating.
The objectives of this studies were to quantify the
changes in meat components related to sensory properties
(characteristic) and meat binding that occur during thermal
processing with conventional and microwave at different
cooking rates (low, medium and high power levels) cooking
methods when final end-point temperature is comparable
between the two methods and to study the changes in
extracellular space of reformed beef roasts thermally
processed in the conventional or microwave oven at similar
rates of heating.
Materials and Methods
Two independent studies were conducted using a prototype
reformed beef roast product as the model for comparison of

122
cooking methods. This model allowed composition control in a
product similar to whole muscle roasts.
Raw Material
Forty-eight forequarters from carcasses weighing a
minimum of 318 kg and possessing a USDA quality grade of
Choice, and yield grade 3 were purchased from a local packing
company.
In study I, 36 beef forequarters were used. Latissimus
dorsi (LD) and Serratus ventralis (SV) muscles were removed
in their entirety. Surface fat and connective tissue were
removed using a hand-held Whizzard knife (Model No: 880).
During removal of the respective muscles, starting
forequarter weights and denuded muscle weights were recorded
to determine the relative percentage for each muscle.
Denuded muscles were mechanically injected with a
water/salt/phosphate solution to achieve 10% added water,
0.75% sodium chloride (NaCl), and 0.35% sodium
tripolyphosphate (NaTPP) using an Inject-O-Mat meat injector
(Model No. PSM 10). Pumped muscles were then vacuum tumbled
in a Globus tumbler (Model No: HS8-081) using a tumbling
cycle consisting of 20 min of tumbling followed by 10 min of
rest for a total of 5 h. Following completion of the
tumbling cycles, two SV or LD muscles were positioned with
respect to fiber orientation in a thick to thin fashion to
attain uniform thickness and parallel fiber arrangement.

123
Muscles were stuffed by hand into 12.0 cm fibrous casings
(Viskase Corp., Chicago, IL), using a modified stuffing horn
(Jetnett Corp., Omaha, NE). Prior to final clip sealing of
the casing, each stuffed casing was placed into a Reiser
vacuum/sealer (Model No: VM-31) to help remove internal air
pockets. Following this step, each casing was tightened and
cliped sealed to achieve a log shape and a consistent
diameter of 12.5 cm. Logs were placed on wire racks and
frozen overnight in a blast freezer (-30°C).
Individual roasts were prepared by cutting frozen logs
on a band saw. This produced a roast that was uniform in
size (12.5 cm dia), shape (cylindrical) approximately 9 cm
thick, and weighing 454 g to 570 g. Roasts were individually
vacuum packaged and held frozen (-20°C) until needed. Roasts
were thawed overnight in a walk-in cooler at 4°C for cooking
the next day.
Study II utilized 12 beef forequarters having the same
specifications and manufacturing steps as previously stated
for study I, except that only LD muscles were used. The
percentage of added water was changed to achieve levels of
5%, 10%, and 15% but at the same salt and phosphate
percentages stated for study I.
Cooking Methods
Conventional (control) roasts were cooked in one of
three Kenmore gas ovens (Model No. 9113248231). Prior to

124
experimental use, each oven was calibrated to maintain a
temperature of 161°C with the smallest possible interval
between cool down and reheat cycles within and between ovens.
Control roasts cooked in studies I and II were cooked as
described by Korschgen and Baldwin (1980). The procedure was
to roast (161°C) the meat on a rack in an open pan until the
desired internal temperature of 60°C/ 70°C, or 75°C was
achieved. Type T copper-constantan thermocouples connected
to a Leeds and Northrup Speedomax recorder (Model No.
CEGJO-OOO) potentiometer were used to monitor both the oven
temperature and internal temperature of the roast.
Microwave cooking was performed in a J C Penney (Model
No.963596560) 2450 MHz variable power microwave oven.
Wattage output for power level of: high, medium, and low was
determined by heating 1000 ml of deionized water at 20°C in a
1-liter beaker, according to the method of Copson (1975).
The oven was determined to produce 523 watts on high, 342
watts on medium, and 175 watts on low, when measured at the
center-middle position of the oven.
Roasts cooked in the microwave oven were placed on an
Anchor Hocking microwavable meat roasting tray in an open
glass dish. The internal temperature of each roast was
monitored using a Luxtron Fluoropticâ„¢ thermometer and fiber
optic probe, (Model 1000A, Digital Readout Device and Model
GSA410082 probe, Luxtron, Mountain View, CA) on loan from the
National Live Stock and Meat Board, Chicago, IL. The

125
equation developed by Yates (1988) was used to predict the
temperature at which microwave power should be terminated in
order for the PCTR to give the desired final endpoint
temperature. Roasts were cooked using high, medium, or low
microwave power levels to achieved a final internal
temperature of 60°C, 70°C, or 75°C.
Cooking losses were determined by weight differences
measured before and after cooking (when roast were cooled to
room 20°C). After weighing, each roast was sliced on a
Hobart slicer to produce 0.5 cm thick slices. A minimum of
2 slices were assigned to each of the following analyses:
proximate analysis, sarcomere length, Kramer shear force, and
textural assessment (Instron Universal Testing Machine).
Samples for proximate analysis were processed the same day
the roast was cooked. All remaining slices were kept frozen
in a blast freezer (minimum 2 weeks) until other analyses
could be performed.
In Study II, experimental procedures were replicated 2
times. Treatment combinations for LD roasts were: two
cooking methods (conventional and modified-low power level);
three added water levels (5%, 10%, or 15%) ; and a single
internal end-point temperature of 70°C. The modified-low
power level in the microwave was approximate to that achieved
by the conventional cooking rate of LD roasts. The
modified-low power level was accomplished by placing four
1-liter beakers and two 400 ml beakers inside the oven

126
cavity. Beakers contained 500 ml or 200 ml of a 40% sucrose
solution and was covered with a plastic wrap material.
Preliminary work revealed that a 40% sucrose solution was
capable of absorbing more microwave energy than water alone.
The sucrose solution functioned to absorb microwave energy
which reduced the total amount of electromagnetic energy
available for product heating. This provided the opportunity
to study the effect of heating method (conventional vs
microwave) when heating rates were approximately the same in
conventional and microwave cookery.
Proximate Analysis and Sarcomere Length
At the time each uncooked roast was cut in the frozen
form, a slice was removed from the face of each roast to
represent the product in the raw form. Representative raw
and cooked samples from each roast were prepared for
sarcomere length determination and proximate analysis.
Sarcomere length was determined using the laser method
described by Cross et al. (1985). Samples for proximate
analysis were minced using a Krups household food processor
(Model No. 700). Moisture, ether extract, and protein were
determined using the methods outlined in AOAC (1980). Ash
content was determined by difference.

127
Shear Force
Cooked and frozen roast slices were allowed to
equilibrate to room temperature (22°C). Samples were cut
into 2.5 x 4.0 cm portions. Each sample was weighed and
placed into the Kramer shear cell. Maximum force per gram
required to shear through the sample was determined using a
Texture Test System (FTC, Model No. TP-1, Rockville, MD)
equipped with a transducer (Model No. FT-300) and pressure
gauge of 54.55 kg max. Results were reported as peak shear
force per gram of sample (kg of force/g of sample). Work
(Joules) was determined by calculating the area under the
force deformation curve.
Bind Strength
The Universal Testing Machine (Model 1125, Instron
Engineering Corporation, Canton, MA) equipped with a tension
load cell (scale, 50 kg) was used to determine the tensile
strength of the roast at the bind juncture. Strips (0.5 x
2.5 x 8.0 cm) were allowed to equilibrate to room temperature
(22°C) prior to testing. A pair of clamps (2.5 cm apart)
were used to hold the strip of roast for the tensile strength
measurement. The sample was held securely in place while a
force was applied until the slice separated at the binding
junction. Only samples that ruptured at the binding junction
were used. The Instron was operated at full scale load of

128
500 g, crosshead speed of 10 mm/min and recorder chart speed
set at 20 mm/min (1:2). The force (kg) required to pull the
slice apart was recorded. Two samples per roast treatment
combination were evaluated. The measurement for modulus of
elasticity was taken from the forward slope of the curve
(N/cm2). Force of rupture (tensile strength) was taken at
the peak height of the curve at the point of rupture (N/cm2).
Work (Joules) was measured as the area under the force
deformation curve from the point of contact to the point of
rupture.
Sensory analysis
Juiciness, connective tissue, and tenderness of 0.5 x
2.5 x 2.5 cm slices were evaluated by a 10-member panel
experienced as members of sensory panel analysis for
evaluation of beef. Panel scores were based on an
eight-point descriptive scale (juiciness, 1 = extremely dry;
8 = extremely juicy; connective tissue, 1 = abundant 8 = none
detected; tenderness 1 = extremely tough, 8 = extremely
tender).
Panelists were given four roast samples per session.
One of the four samples was prepared conventionally, the
remaining samples were prepared in the microwave oven using
low, medium or high power levels. All samples were cooked to
achieve the same final end-point temperature. All samples

129
were served warm in preheated glass jars, held in a thermal
jacket protector.
In Study II, the effect of heating method (C vs MW) and
brine level (5, 10 or 15%) on water distribution within LD
roasts was studied by measuring the change in extracellular
space (ECS). Extra cellular space measurements were
determined using the methods described by Vaccari and Maura
(1978) and Currie and Wolfe (1983). This procedure uses
inulin [14C] carboxylic acid as the ECS marker obtained from
Amersham. The ECS results were expressed as ml/g dry weight
(ECS¿W). The formula used to calculate the ESC was that
given by Currie and Wolfe (1983):
ECSdvj- T°tal dom/o muscle idrv weight)
dpm/ml incubating solution
A measure of the size of the ECS swelling is given with this
method of calculation (Currie and Wolfe, 1983).
Statistical analysis
In Study I, experimental factors were replicated three
times. Main effects were 2 roast types (SV and LD); 4
cooking methods (conventional and microwave low power, medium
power and high power level); and 3 internal end-point
temperatures (60°C, 70°C, and 75°C). All treatment effects
and interactions were determined by analysis of variance for
a factorial arrangements of treatments. The Statistical

130
Analysis System (SAS) for personal computers at the
University of Florida was used to calculate least square
means, standard error and interactions. Thaw weight of each
roast was used as a covariate for analysis of cooking time
and cooking loss data. Means separation was performed using
Duncan-Waller procedures within SAS (Barr et al., 1979).
All treatment effects in Study II were determined by
analysis of variance procedures for a factorial (2
replications by 2 cooking methods by 3 water levels)
arrangement of treatments. The Statistical Analysis System
(SAS) for personal computers at the University of Florida was
used. F-tests were used to determine the effects of cooking
method and added water level on the parameters investigated.
Means separation was performed using Duncan-Waller procedures
within SAS (Barr et al., 1979).
Results and Discussion
Study I
The means and extremes of the forequarter
characteristics and percentage contribution of the SV and LD
muscles (N=48) used in studies I and II are presented in
Table 4.1. The average forequarter utilized in these studies
weighed 84.1 kg, had a ribeye area of 75.4 cm2, and a USDA
quality grade of low choice. The SV weighed approximately
3.1 kg and represented 3.7% of the forequarter weight. The

131
Table 4.1. Means and extremes, and standard deviations of
carcass and muscle characteristics (N = 48).
Trait
Mean
Minimum
Maximum
SDa
HCW, kgb
337.1
314.5
378.6
2.53
FQW, kgc
84.1
75.9
93.6
0.60
FQ % Of HCW
24.9
23.6
26.6
0.09
Ribeye area, cmd
75.4
59.5
98.0
1.16
Marbling scoree
5.3
4.1
6.9
0.15
Fat thickness, cmd
1.39
0.64
2.29
0.06
Serratus ventralis
wt, kgf
3.1
2.5
3.9
0.05
Serratus ventralis
of FWQf
%
3.7
2.9
4.4
0.05
Serratus ventralis
of HCWf
%
0.92
0.71
1.12
0.01
Latissimus dorsi wt, kgr
1.4
1.0
1.9
0.03
Latissimus dorsi %
of FQWr
1.61
1.20
2.13
0.03
Latissimus dorsi %
Of HCWf
0.40
0.31
0.54
0.01
aStandard deviation of the mean.
bHCW = hot carcass weight.
CFQW = forequarter weight.
^Measured on the 12th rib face.
eScore of 9 = abundant (prime), 6 = modest (choice),
3 = slight (select).
fDenuded muscle.

132
LD weighted approximately 1.4 kg and represented 1.6% of the
forequarter weight.
Johnson and coworkers (1988) characterized thirty-four
muscles/muscle groups located within the beef forequarter.
They reported that the SV, Infraspinatus, and Triceps brachii
complex were the larger muscles/muscle groups within the beef
forequarter. It was concluded that maximum utilization of
the beef forequarter may best be achieved when individual
muscles are fabricated and marketed according to their size,
tenderness potential and composition.
Cooking times
Results of the analysis of variance and subsequent
F-tests for cooking parameters are summarized in Table 4.2.
Results of the analysis of variance using thaw weight of each
roast as a covariate and subsequent F-tests for cooking time
is presented in Table 4.1. Total cooking time including
equilibration time (PCTR) were considered. Means for cooking
time by main effects of roast type, cooking method and
end-point temperature are presented in Table 4.3. There was
no difference (P>0.05) in cooking times between LD and SV
roasts (Table 4.3). However, an interaction (P<0.05) of
cooking method by end-point temperature was found for this
characteristic. As illustrated in Fig 4.1, cooking time
increased as end-point temperature increased from 60°C to
75°C for conventional and low power cooking methods, but did

Table 4.2. Analysis of variance for cooking parameters.a
Item
Roast
(R)
Cooking
method
(CM)
End¬
point
temper¬
ature
(EPT)
R*CM
R*EPT
CM*EDT
R*CM*EPT
Cooking time
NS
*
*
NS
NS
*
NS
Cooking loss
NS
*
*
NS
NS
NS
NS
Water loss (%)
NS
*
*
NS
NS
NS
NS
Fat loss (%)
Raw sarcomere
*
NS
NS
NS
NS
NS
NS
length
Cooked sarco-
*
NS
NS
NS
NS
NS
NS
mere length *
Percentage length
NS
NS
NS
NS
NS
NS
change
NS
NS
*
NS
NS
NS
NS
Juiciness
Connective
*
*
*
*
NS
*
*
tissue
*
NS
NS
*
NS
NS
NS
Tenderness
*
*
*
NS
NS
NS
*
Kramer force
*
NS
NS
NS
NS
NS
NS
Kramer work
Tensile
NS
NS
NS
NS
NS
NS
NS
strength
NS
NS
NS
NS
NS
NS
NS
Instron work
NS
NS
*
NS
NS
NS
NS
Strain
*
NS
NS
NS
NS
NS
NS
Rigidity
NS
NS
NS
NS
NS
NS
NS
a*
P<0.05; NS = nonsignificant (P>0.05)
133

Table 4.3. Least-square means for cooking time, cooking loss, and sarcomere length
by roast type, cooking method, and end-point temperature main effects,
n=72.
Main effects
Cooking methods
Roast
Microwave
. End-point temperature (°C)
Latlssimus Serratus
Item
dorsl
ventralis
SEa
Conventional
Low
Medium
High
SEa
60
70
75
SEa
Cooking
Time (m)
52.4
51.4
1.51
100.3°
46.3d
32.7d
27.8e
2.18
46.2°
54.0d
55.5e
1.87
Loss (1)
24.0
25.6
.76
21.0°
20.2°
25.5d
32.5e
1.12
19.6°
26.4d
28.4d
.96
ll2Ob (l)
88.6
75.6
.84
¡ 78.7°
8 1.6°
8 4.0d
82.4e
1.93
78.3°
83.7d
82.3d
1.03
Fatb (1)
11.4°
24.4d
.86
21.3
18.4
16.0
17.6
1.24
21.7
16.3
17.7
1.06
Sarcomere length (un)
Raw 2.50c
2.10d
.051
2.25
2.35
2.32
2.27
.072
2.24
2.32
2.34
.062
Cooked
2.01c
1.73d
.037
1.93
1.88
1.86
1.82
.052
1.92
1.90
1.80
.045
Change (%)
18.79
16.41
1.75
13.73
19.23
18.56
18.89
2.48
13.63°
16.61°
22.57d
2.15
aSE = standard error.
bWater and fat are expressed as a % age of total loss.
cdeMeans within a main effect group on the same line bearing different superscripts
are different (Pco.05).
134

Figure 4.1. Effect of cooking method and end-point
temperature on total cooking time required
for Latissimus dorsi and Serratus ventralis
roasts.

0
E
120
100
a a Conventional^ 63 °C oven)
• — «Low microwave(179W)
o o Medium microwave(342 )
â–¡ â–¡ High microwave(523W)
T
A
X
55
65 70
End-point temperature
(°C)
60
75
80
136

137
not increase for medium or high power microwave cooking.
Cooking times for medium and high power cooking methods
actually decreased as desired end-point temperatures
increased.
The process of heat transfer involves moving energy (in
the form of heat) from one region to another by means of a
temperature gradient. During conventional (still hot air)
heating, heat was transferred slowly from the heated air
surrounding the roast to the interior regions of a roast by
means of conduction. Since microwave energy is considered to
generate heat almost instantaneously from within the meat
product (Nykvist and Decareau 1976), it did not come as a
surprise that cooking time was less (P<0.05) for all
microwave power levels and end-point temperatures studied
when compared to conventional cooking. The speed at which
heat is generated within a food product is considered to be
one of the most attractive features of microwave heating
(Decareau, 1985).
The time-saving advantage of microwave cooking over
conventional methods has been documented by many researchers
(Marshall, 1960; Kylem et at., 1964; Nykvist and Decareau,
1976; and Drew et al., 1980). However, the time saved has
been reported to be highly dependent on the condition of the
meat, fresh versus frozen and the level of microwave power
used. In this study regardless of cooking method, all roasts
were cooked from the thawed state.

138
Cooking losses
Results of the analysis of variance and subsequent
F-tests for cooking loss parameters are summarized in Table
4.2. Means for total cooking loss main effects are
summarized in Table 4.3. There was no difference in total
cooking losses between LD and SV roasts. However, total
cooking loss was influenced by cooking method and end-point
temperature (EPT) main effects. Total cooking loss was
greatest for high power, while medium power was intermediate
compared to conventional and low power cooking which did not
differ. Increasing the end-point from 60°C to 75°C produced
a greater total cooking loss, while 70°C was intermediate but
not different from 75°C.
The water and fat values presented in Table 4.3 are
expressed as a percentage of the total loss. The actual
percentage of water loss during cooking for LD and SV roasts
was not different, 24.2% and 23.3% (+ 0.84) respectively.
However, the actual percentage of fat lost was influenced by
roast type, with SV roasts loosing more fat 7.5% (+ 0.86)
compared to 3.2% (+ 0.86) for LD roasts (P<0.05). The actual
percentage of fat lost was not influenced by cooking method
or end-point temperature. Cooking method and EPT did
influence the actual percentage of water lost from a roast.
Conventional and low power cooking methods were not different
and had lower water losses compared to medium and high power
cooking methods, with high power producing the greatest water

139
loss. End-point temperature also influenced the percentage
of water lost from a roast. The actual percentage of water
lost was lowest at 18.0% (+1.03) at 60 °C compared to 26.2%
and 26.9% (+1.03) for 70°C and 75°C, respectively. These
values are as expected considering the initial composition of
the respective roasts and the methodology of heat generation
associated with microwave heating. These results agree with
numerous other reports concerning total cooking loss and
compositional losses as influenced by cooking method and
endpoint temperature (Marshall, 1960; Ream et al., 1974;
Nykvist and Decareau 1976; Korschgen and Baldwin, 1980; Drew
et al., 1980; Berry and Laddy, 1984).
The increased water losses associated with medium and
high power heating when compared to conventional and low
power cooking are thought to be related to the increased rate
in which heat was produced within the respective roasts.
This theory is supported by the shorter cooking times
required for medium and high power cooking compared to
conventional or low power cooking Table 4.3. The scientific
literature consistently reports greater water losses from
meat products prepared in the microwave oven on high power
levels compared to conventional or low power levels. The
single most incriminating reason for these results appears to
be related to the heating rate. The application of heat to a
native protein structure causes amino acid chain unfolding,
which exposes the interior of the protein chain. It was

140
theorized that some imidazolium groups of histidine are
initially masked in the native myofibrils, and become
uncovered as actomyosin unfolds due to heating (Hamm, 1977).
This results in changing the protein molecules affinity to
other molecules (Martens et al., 1982). Hamm (1977) reported
that when muscle tissue was heated to temperatures between
40°C and 60°C the pH of the system increases. Associated
with the shift in pH is a simultaneous increase in the
water-holding capacity of the myofibrillar proteins. The
increase in pH and water-holding capacity was reportedly due
to an increase in available basic protein groups. Therefore,
during medium and high power microwave heating the thermal
denaturation process of the myofibrillar proteins is thought
to occur at such an accelerated rate compared to conventional
or low power heating that the protein structures tend to
collapse (coagulate) on themselves instead of forming the
more intricate protein-protein gel matrix. This coagulated
structure does not possess the properties thought necessary
to bind or entrap water. As a result, water is forced out of
the product and lost in the form of evaporation or drip.
Sarcomere length
Sarcomere length measurements are typically used to
study the extent to which muscle contraction has occurred.
However, in this project it was used as a method to study
structural changes associated with fluid loss and protein

141
denaturation as influenced by cooking method and end-point
temperature.
Means for sarcomere length measurements are presented in
Table 4.3. The data indicate that roasts made from LD
muscles had longer sarcomere lengths in the raw state
compared to roasts made from SV muscles. One possible reason
for this increased length could be due to the greater degree
of stretching thought to be imposed upon the LD muscle as the
carcass hangs and enters rigor mortis. Neither cooking
method nor end-point temperature affect the cooked sarcomere
length (P>0.05), and cooked sarcomere lengths remained longer
for LD roasts compared to SV roasts (P<0.05). However, the
percentage change in sarcomere length from raw to cooked was
influenced by end-point temperature. At an end-point
temperature of 75°C the percentage change in sarcomere length
was greater compared to 60°C or 70°C. The greater relative
decrease in sarcomere length occurring at 75°C is thought to
reflect the increases in protein denaturation, structural
matrix collapse, and increased cooking loss associated with
increased temperatures (Hamm, 1977).
Chambers et al. (1982) studied the histological
characteristics of beef and pork cooked by dry or moist heat
in a conventional or microwave oven. They indicated that
sarcomere length from porcine muscle tissue was the only
histological characteristic significantly affected by type of
heat or oven. Beef muscle characteristics did not differ

142
between steak positions (inside, outside) or between sample
positions within a steak (center, edge). In their study,
fiber width of both bovine and porcine decreased less with
moist heat than it did with dry, and sarcomere length in
porcine muscle decreased less with dry heat than with moist
heat. This was thought to be related to the higher end-point
temperature (75°C vs 65°C) for porcine tissue. In this
study, two frozen slices from each cooked roast were prepared
for sarcomere length measurement with without consideration
as to the site of sampling.
Proximate analysis
Means and range values for proximate analysis of LD and
SV roasts utilized in Study I are presented in Table 4.4.
Roasts made from LD muscles were initially designed to be
leaner (<10% fat) than roasts prepared from SV muscles (> 10%
fat). The data indicate that the LD roasts contained an
average of 7.6% fat and the SV roasts contained 13.4% fat.
The large standard deviations associated with these values
are thought to result from the method of sampling, the amount
available to sample, and the variations within the muscles.
During preparation of the roast product a thin frozen slice
was removed from the face of each roast for raw product
analysis and the location within the muscle was not
controlled.

143
Table 4.4. Means and extremes, and standard deviations of
chemical composition of raw Latissimus dorsi and
Serratis ventralis roasts.
Item
Mean
Minimum
Maximum
SDa
Moisture
LD*3
(%)
73.54
56.29
77.27
2.17
SVb
68.96
59.82
75.91
4.07
Fat (%)
LD
7.55
3.00
26.43
5.15
SV
13.40
6.39
32.94
6.70
Protein
LD
(%)
16.71
11.95
20.84
1.41
SV
15.66
11.95
20.84
1.91
aSD = standard deviation.
bLD = Latissimus dorsi roast, SV = Serratis ventralis roast.
n=72

144
Texture measurements
Kramer peak shear force (PSF) values are an indication
of product tenderness, and the lower the number, the higher
the tenderness. Results of the analysis of variance and
subsequent F-tests for shear force and work required to shear
the sample are summarized in Table 4.2. Means for Kramer
shear force (kg/g), and its derived work are presented in
Table 4.5. The data indicate that neither Kramer shear force
(kg/g) nor work (J) measurements were influenced (P>0.05) by
cooking method or end-point temperature. Kramer shear force
was, however, influenced by roast type although its
associated work parameter was not (P>0.05). Maximum peak
force (kg/g) was lower (P<0.05) for SV roasts (5.4) than for
LD roasts (5.9). It should be noted that peak shear force
(PSF) values reported for LD and SV roasts are low and that
both roasts would be considered tender. The higher PSF
values for LD roasts may be attributed to its lower fat since
a lower fat content may allow greater aggregation of proteins
within the roast and possibly yield a more dense product. In
this study regardless of the cooking method or final
end-point temperature used, there was no difference in
tenderness as measured by Kramer PSF or work.

145
Binding strength
Means for the Instron Universal Testing Machine
(Instron) measurements of tensile strength (N/cm2), work (J),
and the modulus of rigidity (N/cm2) are presented in Table
4.5. Appendix Fig. A1 illistrates a typical force
deformation curve produced during Instron testing.
Tensile strength expressed as break force in newtons per
cm2 of cross sectional area. Tensile strength was not
influenced (P>0.05) by roast type, cooking method, or
endpoint temperature. The fact that there was no difference
between roasts is thought to have been influenced by
processing methods used to produce the roasts. During the
processing sequence, both muscles LD and SV were vacuum
tumbled together. Therefore both muscles should contain
similar amounts of extracted salt soluble proteins on their
surfaces. Schnell et al. (1970) studied the effects of
chemical or physical action treatments on the mechanism of
binding meat chunks. He concluded that substances which
reduced the amount of cookout function to increase the
binding between meat pieces, irrespective of their chemical
or physical action. Tensile strength and cooking loss
results in Table 4.3 tend to support the finding of Schnell
et al. (1970).
Neither tensile strength, work, nor the modulus of
rigidity were influenced by cooking method (P>0.05). This
would suggest that the rapid heating rate associated with

Table 4.5
Least-square means for Kramer shear force and work and Instron binding
strength measurements by roast type, cooking method, and end-point
temperature main effects.9
Main effects
Roast
Cooking methods
Microwave
Latlsslmus Serratus
Item dorsl ventralls SEb
Conventional Low Medium High SEb
End-point temperature (°C)
60 70 75
SE
b
Kramer cell
Shear force
(kg/g)
5.9b
5.4C
.46
5.7
5.8
5.8
6.2
. 65
5.5
6.1
6.0
.56
viork (J)
n = 72
1.2
1.0
. 18
2.2
2.7
2.4
2.4
.25
2.1
2.4
2.7
. 22
Instron
Tensile
strength
(ll/cm2)
. 38
.33
. 059
. 36
.37
.31
. 37
.042
.31
.34
•U
.072
Work (J)
Modulus of
19.7
22.5
2.83
19.8
21.2
18.5
24.8
4.16
to
O
o
o
a
15.5°
27.8d
3.54
rigidity
(ll/cm2)
12.4
7.5
1.84
12.4
9.2
8.6
9.5
2.70
7.7
10.2
11.9
2.30
n = 40
an=48.
bSE = standard error.
cdMeans within a main effect group on the same line bearing different superscripts
are different (P<0.05).
146

147
microwave cookery did not adversely affect the functionality
of the binding proteins.
The work parameter was found to be the only factor
influenced by end-point temperature and strain influenced by
roast type (Table 4.5). The work required to cause rupture
in the material was measured from the force deformation
curves up to the point of maximum force. There was no
difference (P>0.05) between roasts or cooking method for the
Instron measurement of work. It would appear that the major
factor influencing the parameter work would be the number of
heat induced protein-protein bonds occurring between muscles,
within the extracted protein matrix. A possible reason for
the greater work requirement at 70°C could also be related to
a stronger protein-protein interaction associated with
prolonged heating.
The modulus of rigidity is an indication of the rigidity
of a material or stiffness. Neither roast type, cooking
method, nor end-point temperature influenced the modulus of
rigidity. The values for the modulus of rigidity tend to
indicate that the binding junction of LD roasts were stiffer
than SV roasts. This suggests that the level of fat present
within the final product (after cooking) functions in a
positive way to enhance the textural and sensory assessment
of the product. Although least-square means for the modulus
of rigidity were not significantly influenced by cooking
method, microwave cookery tended to reduce the modulus of

148
rigidity 23% to 30% commpared to conventional cookery. This
suggests that a stiffer- binding matrix may be produced with
conventional cooking compared to microwave cooking methods.
Instron textural assessment for binding strength of the
reformed roasts indicate that cooking method did not
influence the binding strength parameters measured.
Furthermore, the accelerated heating rates associated with
microwave cooking do not produce adverse effects on bind
formation on the reformed roasts.
Sensory evaluation
Results of the analysis of variance and subsequent
F-tests for sensory panel assessment are summarized in Table
4.2. Main effects means for juiciness, connective tissue,
and overall tenderness for reformed roasts are presented in
Table 4.6. Sensory panelists consistently rated the SV roast
higher in juiciness, connective tissue content and overall
tenderness (P<0.05) than the LD roasts. As a result of
compositional difference, it was not an unexpected result
when SV roasts consistently generated higher sensory scores
compared to the LD roasts. The influence of fat on various
sensory attributes has been well documented throughout the
scientific literature (Carpenter et al., 1966; Cross et al.,
1980; Valvano, 1983; Hand et al., 1987). The presence of fat
within a food product is thought to provide a sensation of
wetness and mouth lubrication to the taster. Both cooking

Table 4.6. Least square means for sensory panel assessment of juiciness, connective
tissue, and tenderness by roast type, cooking method, and end-point
temperature main effects, n=515.
Main effects
Cooking methods
Roast
Microwave
End-point temperature (°C)
Item
Latissimus
dorsi
Serratus
ventralis
SEa
Conventional
Low
Medium
High
SE
60
70
75
SE
Juiciness
5.2b
6. lc
.05
5.9b
6.0b
5.6C
5.id
.08
6.3b
5.5C
5.2d
.07
Connective
tissue
5.4b
5.9C
.06
5.8
5.7
5.7
5.5
.09
5.6
5.7
5.7
.08
Tenderness
5.7b
6.5C
.06
6.4b
6.3b
6.0C
5.8°
.08
6.4b
5.9C
6.0°
.07
aSE = standard error.
bcdMeans within a main effect group on the same line bearing different superscripts
are different (P<0.05).
149

150
method and end-point temperature were found to affect
(P<0.05) juiciness scores. However, a significant roast type
by cooking method by end-point temperature interaction for
sensory panel juiciness score was detected indicating that
juiciness scores were not consistent across main effects.
As expected, juiciness scores generally decreased as
end-point temperature increased, but the decreases were not
consistent for cooking methods or roast types. For the LD
roasts (Fig 4.2), conventional or low power microwave cookery
resulted in a decrease from 60°C to 70°C but increased from
70°C to 75°C. Medium and high power microwave cookery
resulted in a slight decrease or little change for medium and
high power, respectively. However, further heating by
these methods to 75°C caused drastic reductions in juiciness
scores. In fact, at 75°C, both medium and high power
microwave cookery resulted in scores in the unacceptable
category (<5). Juiciness scores for the SV roasts (Fig. 4.3)
showed similar cooking method by end-point temperature
changes except that the differences at 70°C apparent in the
values for the LD roasts for high and medium power cooking
were significantly lower.
These juiciness scores are thought to be related to the
cooking loss differences detected for cooking methods. The
high loss of water and fat for medium and high power
microwave cookery methods should have effects on juiciness of
the product. The magnitude of the values suggests that these

Figure 4.2.
Effect of cooking method and end-point
temperature on taste panel assessment of
juiciness for Latissimus dorsi roasts; 8
extremely juicy, 6 = moderately juicy, 4
slightly juicy, 2 = very dry (n=515).

Juiciness Score
152

Figure 4.3. Effect of cooking method and end-point
temperature on taste panel assessment of
juiciness for Serratus ventralis roasts;
extremely juicy, 6 = moderately juicy, 4
slightly juicy, 2 = very dry (n=515).

Juiciness Score
154

155
products should be acceptable in juiciness except when the LD
roast is cooked at high or medium power to a well-done degree
of doneness.
A significant roast by cooking method interaction for
sensory panel assessment of connective tissue was detected
and is presented in Table 4.7. Connective tissue content as
assessed by a sensory panel for SV roasts was determined to
be lower compared to LD roasts regardless of cooking method
used. However, sensory panel connective tissue scores for LD
roasts cooked with microwave energy were improved compared to
LD roasts cooked conventionally. This is in contrast to SV
roasts, where connective tissue scores decreased as a result
of microwave cooking methods. These data tend to indicate
that several underlying factors are influencing these
results. The higher fat content associated with the SV
roasts is thought to be the single most important factor
responsible for the differences between roasts. Second, the
influence of the faster heating rate and the subsequent
results on stromal and myofibrial protein denaturation are
thought to influence connective tissue scores within a roast.
A significant roast by cooking method by end-point
interaction for sensory panel tenderness score was detected.
Figures 4.4 and 4.5 illustrate the influence of cooking
method by end-point temperature for LD and SV roasts
respectively. Tenderness scores tended to be higher (more
tender) for SV roasts regardless of cooking method and

156
Table 4.7. Roast by cooking method interaction for sensory
panel assessment of connective tissue, n = 515.
Cooking method
Microwave
Item
Roast
Conventional
Low
Medium
High
SEa
Connec-
Latissimus
tive
tissue*3
dorsi
5.3
in
•
in
5.6
5.4
. 13
Serratus
ventralis
6.3
5.8
5.9
5.6
. 13
aSE = standard error.
^Connective tissue, 8 = none detected, 6 = trace amount,
4 = modest amount, 2 = moderately abundant.
n=515

Figure 4.4.
Effect of cooking method and end-point
temperature on taste panel assessment of
tenderness for Latissimus dorsi roasts; 8
extremely tender, 6 = moderately tender,
slightly tough, 2 = very tough (n=515).

Tenderness Score
158

Figure 4.5. Effect of cooking method and end-point
temperature on taste panel assessment of
tenderness for Serratus ventralis roasts; 8
= extremely tender, 6 = moderately tender, 4
= slightly tender, 2 = very tough (n=515).

Tenderness Score
160

161
end-point temperature compared to LD roasts. As expected,
tenderness scores decreased as end-point temperature
increased. However, the changes in tenderness scores were
not consistent within cooking methods and end-point
temperatures. In SV roasts, high power decreased tenderness
scores from 60°C to 70°C but increased from 70 °C to 75°C.
In LD roasts, the use of low power microwave energy resulted
in decreased tenderness scores from 60°C to 70°C, but
increased from 70°C to 75°C. Tenderness scores for LD roasts
cooked with high power microwave energy showed little change
as end-point temperature increased. These results are
thought to reflect the differences in fat and moisture
content and cooking losses associated with the different
roast types as influenced by the different treatment main
effects.
Results of Study I suggest that reformed LD and SV
roasts can be produced from the beef forequarter with design
consideration for microwave cooking. The roasts were uniform
in size, shape and composition, factors deemed necessary for
uniform heating. The ability to accurately predict the
intensity and duration of the PCTR associated with microwave
cooking was a necessity for conducting this study.
The results of this study indicate that the adverse
changes in chemical, physical and sensory measures of
tenderness and palatability associated with microwave cooking
of beef entrees can be rectified when PCTR is accurately

162
controlled. Microwave cooking times were less than
conventional cooking for all power levels or end-point
temperatures tested. Changes in chemical composition were
measured as changes in proximate analysis from the raw to
cooked form. Results indicate that LD and SV roasts did not
differ in total cooking loss. However, SV roasts lost a
greater percentage of fat during cooking than did the LD
roasts. There was no difference in cooking loss between
conventional and low power microwave cooking. Cooking losses
were greater for high power microwave cooking compared to all
other methods, while medium power cooking was intermediate
compared to other methods. Cooking method did not affect the
percentage change in sarcomere length from raw to cooked
samples. However, as end-point temperature increased,
sarcomere length decreased. Results indicated that SV roasts
had superior textural qualities compared to LD roasts.
Cooking method did not influence tensile strength, work,
strain, or the modulus of rigidity of the binding juncture
between muscles. Sensory panel assessment for palatability
attributes indicated that SV roasts tended to be juicier,
have less connective tissue, and were more tender when
compared to LD roasts. Sensory panel juiciness scores for LD
and SV roasts generally decreased as end-point temperature
increased. Medium and high power microwave cooking methods
produced greater cooking losses at 75°C compared to
conventional and low power methods for both roasts. However,

163
medium and high power microwave cooking of LD roasts to 70°C
produced higher juiciness scores compared to conventional and
low power cooking methods. Medium and high power cooking of
SV roasts to 70°C and 75°C produced lower juiciness scores
compared to conventional and low power methods.
Study II
The primary objective for developing the modified-low
power microwave level was to provide a slower cooking rate
within the microwave oven that approximated the rate of
cooking that occurred within the conventional oven (161°C).
By doing this, it provided an avenue by which to study the
effect of heating method (non-ionizing electromagnetic
energy-microwave versus indirect still air
conduction-conventional). The purpose of this study
therefore was to investigate the adverse effects of decreased
product palatability associated with microwave cooking due to
the method (microwave vs conventional) in which heat was
generated.
Means for cooking rate (g/min) as influenced by cooking
method and added brine level main effects are presented in
Table 4.8. Cooking rate was not influenced by cooking method
(P>0.05) as expected since the rate in the microwave had been
adjusted. However, cooking rate was influenced by the
percentage of added brine in that the addition of 10% or 15%
added brine resulted in a faster (P<0.05) cooking rate

Table 4.8. Least-square means for cooking rate, cooking loss, and assessment of
extracellular space (ECS) by tissue condition, added brine percent,
and sampling site main effects.
Tissue condition
Cooking
method
Added brine
(t)a
Sampling site
Item Raw
Conven¬
tional
Mod 1-
f led
SEb
5 10
15
SE
Interior Exterior SE
Cooking0
rate
(min/g)
(n=12)
0.1981
0.1976
.00009
0.2034° 0.1959d
0.1942d
.00115
—
loss (»)
(n=12)
20.3
19.8
1.04‘
17.8 21.0
21.3
1.27
—
Fpc
(ml/g) 3.13'
d 1.72e
1.82®
. 122
1.97d 2.15d
2.54®
.125
2.364d 2.087® .0001
aWhen added to
a roast
at these
levels,
the roast would contain 0.
75» llaCl
and 0.35»
sodium tripolyphosphate.
bSE = standard error.
cTime required to cook a given amount of product mass to 70°C.
deHeans within a main effect group on the same line bearing different superscripts
are different (P<0.05).
164

165
compared to the cooking rate at 5% added brine (Table 4.8).
Cooking loss percentage was not influenced by main effects.
These data indicate that the conventional cooking method and
the modified-low power microwave energy allowed the reformed
LD roasts to heat at the same rate. The ability to slow down
the rate of heat conduction occurring as a result of
microwave heating within an LD roast so that it approximated
the rate of heat conduction occurring within an LD roast
cooked conventionally was a critical part of this study.
This was done to study the influence of heating method
(conventional versus microwave) on changes in the
extracellular space of the roast beef product, when the
heating rate was held constant.
Heffron and Hegarty (1974) used inulin as the ECS marker
to study the changes in cell volume during rigor development
in mice. Currie and Wolfe (1980) also used that procedure to
measure water translocation between the intracellular and
extracellular spaces in beef muscle undergoing rigor. Currie
and Wolfe (1983) concluded that the reagent grade inulin used
in there previous work (Currie and Wolfe, 1980) was not pure
enough to give reasonable values for the ECS. However,
Currie and Wolfe (1983) determined that inulin [14C]
carboxylic acid from Amersham to be highly purified and free
of any compounds capable of permeating the functional
membrane.

166
The inulin [14C] carboxylic acid space was used as a
measure of the size of the ECS after swelling. It is
expressed as ml/g on a dry weight (dw) basis (ECS¿W) using
the formula presented by Currie and Wolfe (1983). Means for
ECS¿W assessment values by main effects of raw tissue,
cooking method, added brine level, and sampling site are
presented in Table 4.8. The mean ECS¿W value of 3.13 ml/g
for the raw product far exceeds the typical ECS¿W of 1.4 ml/g
for semitendinosus (immediately postmortem) reported by
Currie and Wolfe (1983). However, they did reported a
maximum ECS^ of 2.7 ml/g occurring within 12 to 28 hours
postmortem. They concluded that this extraordinarily high
ECS¿W value was due to inulin uptake in the intracellular
region due to membrane breakdown. The high ECS¿W values
reported in this study are also thought to be due to cell
membranes rupturing, as a result of the numerous processing
conditions imposed on the muscle tissue prior to assessment
(especially freezing and the addition of brine). Damaged
membranes would allow inulin to migrate into the
intracellular space. However, because the membrane is
damaged, its intracellular content becomes extracellular and
the total is therefore able to be measured as ECS.
The influence of cooking method on assessment of ECS¿W
is presented in Table 4.8. The data indicate that cooking
method did not influence ECS¿W. Since microwave cooking
generates heat within a food product by producing rotation of

167
water molecules it may be that this action would be
responsible for the lower palatability characteristics
associated with meat products and microwave cooking. This is
because of the established fact that the moisture content of
a food product has a tremendous influence on the product
texture and palatability attributes. In this particular
study, it has been hypothesized that if microwave energy was
detrimental to these attributes then changes in ECS¿W should
have been detected. Because ECS^w values were not different
as a result of cooking method the data from Study I would
suggest that heating rate was responsible for differences in
chemical and sensory attributes. The increased cooking
losses reported in Study I as a result of increased heating
rates are thought to reflect a collapse in the ECS structure.
In Study I, Table 4.3 (total cooking loss %) and Table 4.6
(sensory assessment) and Figures 4.2, 4.3, 4.4, 4.5.
indicate that microwave cooking of roasts on high power had
greater cooking losses, numerically lower sensory scores and
decreased product juiciness and tenderness respectively.
This is thought to occur as a result of heat being generated
rapidly within the roast. Rapid heating results in excessive
protein denaturation/coagulation without forming the desired
water holding gel-matrix. The collapse of ECS structures
could act to squeeze water out of the product in the form of
cooking drip. However, the possibility also exists that
greater water losses associated with medium and high power

168
microwave levels could be reflecting the greater rotational
activity of the water molecules as water is lost in the form
of steam.
Schiffmann (1986) indicated that the speed or rate at
which microwaves heat was usually their most attractive
feature. However, it is possible to heat too rapidly, such
that heat can be generated faster than the product can
adequately distribute it. When this occurs, the outer
regions of the product becomes over heated, which results in
excessive loss of product moisture and decreased
palatability. Another problem associated with excessive
heating rates is non uniform temperature distribution. This
occurs because the heating rate may be so fast as to prevent
effective thermal conductivity of the heat to the cooler
interior regions. The author suggested a general rule to be
followed in microwave processing is "fast—but as slow as
possible" (Schiffmann 1986. p.95).
The influence of sampling site (interior or exterior)
within a roast on ECS¿W values is presented in Table 4.9.
The data indicate the presence of greater (P<0.05) ECS¿W
occurring at the interior of the roast compared to the
exterior region. This was an expected occurrence since
moisture content is typically greater in the interior region
of a roast due to surface dehydration and the interior would
be effected less by cooking than the exterior.

169
Means for ECS¿iw values by added brine levels are
presented in Table 4.8. Addition of 5% or 10% added brine to
LD roasts did not influence the ECS¿W. However, adding 15%
brine to the roasts resulted in a significant increase in the
ECS(jw compared to additions of 5% or 10% added brine.
Cooking losses were not influenced (P>0.05) by added brine
levels. However, the increase in ECS¿W detected for the 15%
added brine suggests that these roasts bound more of the
added brine compared to 5% and 10% levels simply because
there was more brine initially available to bind. This can
be compared to producing a "water added" meat product.
Knowing that cooking loss incurred during thermal processing,
brine would be added to the product (prior to cooking) at a
level to compensate for the cooking loss incurred plus have
an amount of added water retained within the product. In
this study, the 15% added brine level is thought to represent
a level where compensation for cooking losses were
demonstrated.
Cooking rates were faster for roasts with added brine
levels of 10% and 15% compared to the 5% level (Table 4.8).
Numerous reports have indicated that the thermal conductivity
of beef is dependent on the moisture content of the product
(Bengtsson et al., 1976; Godslave et al., 1977ab; Perez and
Cálvelo, 1984; Singh et al., 1984). Although not significant
(P>0.05), cooking losses tended to be lower for the 5% added
brine level compared to 10% and 15% levels. This could be

170
reflect the slower heating rate of the 5% added brine level
roasts.
Overall Summary
Latissimus dorsi (LD) and Serratis ventralis (SV)
muscles were removed from 48 USDA Choice, yield grade 3 beef
forequarters. Muscles were denuded and further processed to
produce roasts designed for microwave cooking. The roasts
were uniform in size and shape, factors deemed necessary to
achieve uniform microwave heating. The ability to accurately
predict the extent to which post-cooking temperature rise
(PCTR) occurred in the roasts was necessary for conducting
this study. This research was conducted to study the effect
of heating rate (slow vs fast) and the method of heat
production (conventional vs microwave) on palatability
attributes.
Two separate studies were conducted as completely
randomized designs. Study I used a factorial arrangement:
three replications by two roast types (LD and SV) by four
cooking methods (conventional, low, medium and high microwave
power levels) by three end-point temperatures (60°C, 70°C and
75°C). Study II used LD roasts in a factorial arrangement
involving two replications by three cooking methods
(conventional and modified-low power microwave) by three
levels of added brine (5%, 10% and 15%), and two locations
within the roasts (exterior and interior).

171
The results of Study I indicated that microwave cooking
required less time than conventional cooking for all
treatment combinations tested. Total cooking loss was
greater for roasts cooked with high microwave power and lower
(P<0.05) for conventional and low power microwave cooking,
while medium microwave power was intermediate. End-point
temperature of 60°C produced lower cooking losses than either
70 or 75°C which were not different (P<0.05). Changes in the
chemical composition of roasts due to cooking method
indicated greater water losses for medium and high power
microwave cooking (P<0.05) than for the other cooking
methods. Cooking method did not affect the percentage change
in sarcomere length from raw to cooked samples. However, as
end-point temperature increased, sarcomere length decreased.
Product tenderness was measured using the Texture Test System
equipped with a Kramer cell. Textural assessment of the
binding junction was performed using an Instron Universal
Testing Machine. There was no difference in peak force
(kg/g), work (J), tensile strength (N/cm2), strain (mm/mm) or
modulus of rigidity (N/cm2) due to cooking method (P>0.05).
These results were supported by sensory panel assessment for
palatability attributes.
Study II was designed to provide a slow cooking rate
within the microwave oven (modified-low power) that
approximated the rate of heating occurring within the
conventional oven (161°C). This permitted studying the

172
effect of heating method, and its effect on extracellular
space (ECS) assessment using inulin [14C] carboxylic acid.
The data indicate ECS was not affected by cooking method
(P<0.05).
The changes in extracellular tissue fluid distribution
occurring within a reformed beef roast (LD) as influenced by
the method of thermal processing (microwave vs conventional)
were studied. The data suggest that the extracellular water
space is subject to change due to thermal processing and that
this relative change is capable of being detected. The data
indicated a decrease in ECS from the raw product to the
cooked product, cooked conventionally or with modified-low
power microwave heating.

APPENDIX
INSTRON FORCE DEFORMATION CURVE

Figure Al. Stress strain diagram for a material
without a bioyield point. Point C
represents the maximum tensile stress
that a material is capable of sustaining.
Area encompassed by points A, B, and C
represents the work required to cause
rupture, also referred to as an estimate
of product roughness. Modulus of
rigidity (Em) is take as the slope of the
line connecting the origin and point C,
(or secant Modulas between points A and C).

STRESS
175

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BIOGRAPHICAL SKETCH
Joseph A. Yates was born June 14, 1955, in Miami, FL.
In the spring of 1964, his family moved to Daytona Beach, FL.
While growing up in Daytona Beach, he becme active in Cub
Scouting and Boy Scouting. On July 9, 1969, at the age of
14, he became one of the youngest individuals in Florida to
earn the rank of Eagle Scout. In August 1969, his family
moved to Perrine, FL, a suburb of Miami. Upon graduation
from Miami Palmetto Senior High in June 1973, he entered
Miami-Dade Community College. In August 1975, he graduated
from Miami-Dade Community College with an Associate of Arts
degree. He entered Auburn University in September 1975. In
June 1976, he married his high school sweetheart, Diana
Lorayne Mosel. In June 1978, Auburn University presented him
with a degree of Bachelor of Science in agriculture, with a
major in animal science. Following graduation, he returned
to Florida gaining experience as a swine farm manager, feed
store manager, and finally as a high school vocational
agriculture teacher.
In August 1981, the author entered the University of
Florida as a post-baccalaureate student. In August 1982, he
entered the graduate program in animal science to pursue the
194

195
degree of Master of Science under the guidance of Dr. Terry
Coffey, while working as graduate research assistant. In
August 1984, he received a Master of Science degree with a
major in swine nutrition from the University of Florida. Mr.
Yates continued his gradute studies at the University of
Florida in meat science and food processing, as research
assistant under the co-direction of Dr. Roger L. West and Dr.
Rachel Shireman. During his Ph.D. studies, his wife gave
birth to their son, Brandon Joseph Yates, on April 32, 2986.
Following completion of requirements forthe degree of
Doctor of Philosophy, Mr. Yates will become the Research and
Product Development Coordinator for Crofton and Sons, Inc.,
in Tampa, FL.

I certify that I have read this study and that in my
opinion it conforms to acceptable standards of scholarly
presentation and is fully adequate, in scope and quality, as
a dissertation for the degree of Doctor of Philosophy.
A . uJdS[
R.L. West, Chair
Professor of Animal Science
I certify that I have read this study and that in my
opinion it conforms to acceptable standards of scholarly
presentation and is fully adequate, in scope and quality, as
a dissertation for the degree of Doctor of Philosophy.
R.B. Shireman, Cochair
Associate Professor of Food Science
and Human Nutrition
I certify that I have read this study and that in my
opinion it conforms to acceptable standards of scholarly
presentation and is fully adequate, in scope and quality, as
a dissertation for the degree of Doctor of Philosophy.
D.D. Jranson
Assistant Professor of Animal
Science
I certify that I have read this study and that in my
opinion it conforms to acceptable standards of scholarly
presentation and is fully adequate, in scope and quality, as
a dissertation for the degree of Doctor of Philosophy.
C.
S.C. Denham
Assistant Professor of Animal
Science

I certify that I have read this study and that in my
opinion it conforms to acceptable standards of scholarly
presentation and is fully adequate, in scope and quality, as
a dissertation for the degree of Doctor of Philosophy.
M. Harshail
Associate Professor of Food Science
and Human Nutrition
I certify that I have read this study and that in my
opinion it conforms to acceptable standards of scholarly
presentation and is fully adequate, in scope and quality, as
a dissertation for the degree of Doctor of Philosophy.
A. Teixeira
Associate Professor of Agricultural
Engineering
This dissertation was submitted to the Graduate Faculty
of the College of Agriculture and to the Graduate School and
was accepted as partial fulfillment of the requirements for
the degree of Doctor of Philosophy.
December 1988
De
Dean, Graduate School

UNIVERSITY OF FLORIDA
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