Chapter

13

PRINCIPLES OF MEAT
PROCESSING

The Science of
Poultry and Meat Processing
Shai Barbut PhD

University of Guelph

Chapters
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.

AUTOMATION
GLOBAL PERSPECTIVE
STRUCTURE* AND MUSCLE PHYSIOLOGY
LIVE BIRD HANDLING*
PRIMARY PROCESSING OF POULTRY*
HACCP IN PRIMARY PROCESSING*
INSPECTION AND GRADING*
STUNNING*
PORTIONING, DEBONING AND FRESH MEAT
COMPOSITION*
FURTHER PROCESSING EQUIPMENT
HEAT PROCESSING, COOLING AND PRESERVATION
METHODS
HACCP IN COOKED MEAT OPERATIONS
PRINCIPLES OF MEAT PROCESSING
BATTERING AND BREADING PRODUCTION UNDER
HACCP
MICROBIOLOGY AND SANITATION
EVALUATING TEXTURE AND SENSORY ATTRIBUTES
EVALUATING WATER/FAT BINDING AND COLOUR
WASTE TREATMENT AND BY-PRODUCTS

* Topics focussing on poultry. Rest of the chapters are related to both red meat and poultry.

Preface
The aim of The Science of Poultry and Meat Processing book is to provide students
and industry personnel with a comprehensive view of the modernized primary poultry
meat industry and further processing of both red meat and poultry. An emphasis is
placed on basic concepts as well as recent advancements such as automation (e.g.
increasing poultry line speed from 3,000 to 13,000 birds per hour over the last 40
years) and food safety (e.g. HACCP in primary and the further processing areas). The
book also includes chapters explaining basic muscle biology, protein gelation, heat
and mass transfer, microbiology, as well as meat colour and texture to help the reader
understand the underlying scientific concepts of meat processing. The Science of
Poultry and Meat Processing book is based on over two decades of university teaching
experiences, and is designed to be used as a course textbook by students, as well as a
resource for professionals working in the food industry. The book is available online,
at no cost, to any interested learner. Using this format has also allowed me to include
many colour pictures, illustrations and graphs to help the reader.
ii

The book is dedicated to my past and current students who have inspired me to
learn more and conduct challenging research projects. I see this as an opportunity to
give back to the field that I have received so much from as a student and as a faculty
member. Looking back, I have learned a great deal from my MSc and PhD advisor,
Dr. A. Maurer, who was the student of Dr. R. Baker - the father of poultry processing
in North America. I would also like to thank Dr. H. Swatland with whom I worked for
almost 20 years, for the many challenging scientific discussions.
Writing The Science of Poultry and Meat Processing book was a long process, which
also included having all chapters peer reviewed. I appreciate the help of my colleagues,
but I still take responsibility for any inaccuracy in the book. If you have comments or
suggestions, I would appreciate hearing from you ([email protected]), as I am
planning to revise and update a few chapters on a yearly basis.
I would like to thank the many people who have helped me during the writing process.
To Deb Drake who entered all of the material for the book, to Mary Anne Smith who
assisted in editing, and to ArtWorks Media for the design and desktop publishing
of the book. I greatly appreciate the help of my colleagues who reviewed chapters
and provided useful discussions. They include Mark B., Ori B., Sarge B., Gregoy
B., Joseph C., Mike D., Hans G., Theo H., Melvin H., Myra H., Walter K., Roland
K., Anneke L., Massimo M., Johan M., Erik P., Robert R., Uwe T., Rachel T., Jos
V., Keith W., and Richard Z. I would also like to thank my family for their love and
support during the entire process.

About the Author

Shai Barbut is a professor in the Department of Food Science at the University of
Guelph in Ontario, Canada. He received his MSc and PhD at the University of
Wisconsin in meat science and food science. He specializes in primary and further
processing of poultry and red meat. His research focuses on factors affecting the
quality of meat, as well as protein gelation with an emphasis on structure / function
relationships, rheological properties and food safety aspects. He has published over
two hundred peer reviewed research papers and is the author of the Poultry Products
Processing An Industry Guide textbook. He is a fellow of the Institute of Food
Technologists and has received awards from the Meat Science Association, Poultry
Science Association, and the Canadian Institute of Food Science and Technology. He
is involved in a number of government committees as well as academic and industrial
research projects.

iii

 2015 Shai Barbut

2015 Shai Barbut

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Issued in print and electronic formats.

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Includes bibliographical references and index.
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Issued in print and electronic formats.
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13
PRINCIPLES OF MEAT PROCESSING
13.1 Introduction
The continuous success of marketing meat depends on the innovation and
consistent production of high quality products. Consumers are looking for
convenient food products with new/exciting flavours, textures, etc. A simple,
inexpensive mix of dry powder containing all essential nutrients can meet
our nutritional needs; consumers, however, are looking for diversification
and excitement when eating food. As will be discussed in this chapter, the
food industry is making and preparing food in different ways and with many
ingredients. A simple example of this diversification is the use of white poultry
meat in roasts, deep fat fried nuggets, barbequed fillets/wings with honey garlic
sauce, or smoked sausages (recipes for all these products are provided at the end
of this chapter). Over the past few decades, the meat and poultry industries have
been very active in introducing new meat products. Initially, a lot of the products
were made from red meat (e.g., salami, pepperoni, ham). However, during
the past 30 years the poultry industry has taken the initiative to develop fresh,
marinated, as well as fully cooked products, and it has also adopted some red
meat recipes. Poultry frankfurters were unheard of 50 years ago; however, after
their introduction, they gained widespread popularity and currently represent
about a third of the North American market. These new developments have
helped to increase consumption and to move away from seasonal meat demands
(e.g., in the past, whole turkeys were primarily sold in North America prior to
Thanksgiving and Christmas). The industry has also realized that selling large
birds, such as whole turkeys, limits its ability to sell meat to all market segments.
Therefore, the industry started marketing smaller cuts and further processed
products in small packages. Another example that is unique to the poultry
industry is the development of the chicken nugget by the fast food industry in
the 1970s. This has given the industry a huge boost in sales and has dramatically
changed the marketing and processing of chicken meat. This innovation was
driven by the industrys need to develop line deboning of poultry as well as find
ways to sell the remaining chicken portions (i.e., before nuggets were introduced

13-2

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

the market was mainly set for selling whole birds and some bone-in cut up parts).
It also resulted in the introduction of mechanical deboning of the meat left on the
frames. All these developments created a market for various innovative further
processed meat products (Table 13.1.1; Fig. 13.1.1). Overall, this is an example
of the industry successfully responding to consumer demand for more convenient
food items including semi and fully prepared items. In this case, the increase in
poultry meat consumption (Chapter 2) has been the result of aggressive marketing,
the meats favorable nutrient profile, and its competitive price. As discussed in this
book, these developments have been coupled with the introduction of automation,
computer assisted programming (e.g., see discussion on Least Cost Formulation
below), and increasing line speed.
Table 13.1.1 Categories of the major meat/poultry further processed products on the international
market. Note: smoking procedures and cooking recipes for most products are
provided at the end of the chapter.
Category

Example

Comment

a. Whole Muscle

Oven roasted turkey breast

Smoked chicken/duck/goose fillet

Premium white meat product

b. Restructured

Poultry roll
Turkey luncheon roll
Cooked duck tenderloins
Turkey ham

Large/small meat chunks

c. Ground

Breakfast sausage
Pepperoni sticks
Salami
Chicken hamburger

Sold fresh/frozen to the consumer

Fully cooked/frozen ready to eat
Semi dried/dried ready to eat

d. Finely Comminuted

Chicken wiener
Turkey hot dog
Poultry Bologna

Very homogeneous appearance

e. Coated

Nuggets
Cordon Bleu
Chicken wings
BBQ bone in chicken wing/thigh
BBQ boneless poultry drum sticks

Battered, breaded and fried

Breaded with cheese insert
Battered, breaded, par-fried & cooked
Marinated and cooked
Marinated and cooked

Pieces of dark thigh meat

Overall, meat and meat products are mainly composed of protein, water, fat,
minerals (salts), and some carbohydrates. Proteins represent the major building
blocks of meat products and a major section in this chapter is devoted to protein
gelation. Mezzenga and Fischer (2013) indicated that protein aggregation has
fundamental relevance not only in the food industry (e.g., providing texture to meat
products, gelation of yogurt) but also in the medical field (blood coagulation by

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

fibrinogen) and others. However, aggregation of food proteins differs substantially

from the medical field, where the range of conditions is mostly limited to those
found
in the
human
bodyof(e.g.,
37C,
pH Showing
7.0, ionic
strength
aboutroast,
155mM).
Figure
13.1.1
Examples
different
products.
chicken
roast,ofturkey
turkey
pepperoni sticks, poultry wieners, turkey ham and turkey bacon. Photo by
Barbut and Jinde.

Figure 13.1.2 Schematic representation of the physical description of proteins in soft condensed
Figure 13.1.1 Examples of different products. Showing chicken roast, turkey roast, turkey
matter. (a) A hypothetical unfolded protein, interpreted as an ampholytic
pepperoni sticks,
poultry wieners,
hamand
and negative
turkey bacon.
polyelectrolyte,
containing
both turkey
positive
charges. (b) The
by obtained
Barbut and
intermediate case ofPhoto
gelatin,
by Jinde.
hydrolysis of the triple-helical collagen:
the -helical structure of gelatin strands can melt by increasing the temperature
and reversibly re-constitute upon cooling, with -helices interacting to induce
gelation of the solution. (c) A folded globular protein, such as -lactoglobulin,
viewed astemperature
a colloidal sphere
positive
and0negative
charges
its surfaces.
In the food industry,
canwith
range
from
300C,
pHonfrom
1 10,
From Mezzenga and Fisher (2013).

and ionic strength spans as many as seven orders of magnitude. Food systems
consist of complex mixtures of various proteins, fats, carbohydrates, and salts. In
general, food proteins can be divided into different classes based on the amino acid
sequence and thermal history. The protein structure may be referred to as either
globular or random coil (folded or unfolded, respectively, Fig. 13.1.2). They will
be discussed in more detail later in the chapter.
94

13-3

13-4

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

Figure 13.1.2 Schematic representation of the physical description of proteins in soft condensed
Figure 13.4.1
Effect of NaCl on the shrinking of cooked chicken muscle (700C) inmatter.
the presence
(a) A hypothetical unfolded protein, interpreted as an ampholytic polyelectrolyte, containing both
of
salt
and
different
polyphosphates
(0.5%).
HMP

hexa
meta
phosphate;
TPP
positive and negative charges. (b) The intermediate case of gelatin, obtained by hydrolysis of
tri
poly
phosphate;
KENA

commercial
phosphate
blend;
PP
pyro
phosphate
the triple-helical collagen: the -helical structure of gelatin strands can melt by increasing the
(sodium acid).
Redrawn
from upon
Shults
andwith
Wierbicki
(1973). to induce
temperature
and reversibly
re-constitute
cooling,
-helices interacting
0
gelation of the solution. (c) A folded globular protein, such as -lactoglobulin, viewed as
1
a colloidal sphere with positive and negative charges on its surfaces.
35
2
From Mezzenga and Fisher (2013).
3
30
HMP
NO PHOSPHATES 4
5
TPP
25
KENA
6
20 Processing Categories of Meat Products PP
13.2
7
8
15
There is a vast array of meat products available for customers in the supermarket 9
today.
10 Table 13.1.1 shows examples of the main processing categories/groups,10

but overall there are hundreds of products available on the market, which can be
5
challenging
for consumers to understand. To assist them, various systems have
been
suggested
for classifying meat products. For example, one system groups
0
products
on
and includes six
0 based
1
2 their
3 preparation
4
5 method
6
7(Aberle
8 et9al., 2012)
10
processing categories/groups: % NaCl IN MEAT
a. Fresh (uncooked) example: fresh breakfast sausage
b. Uncooked and smoked example: Italian sausage
c. Smoked and cooked examples: hot dogs, frankfurters, bologna,
95
mortadella
d. Cooked examples: liver sausage and pates

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

e. Dry/semidry or fermented examples: summer sausage, dry salami

f. Cooked meat specialties examples: luncheon meats, jellied products
and loaves
It should also be mentioned that new technologies have helped to diversify the
type of meat products we consume, especially the restructured meat products
(e.g., surimi), where small pieces of meat are made into a whole muscle/steaklike product. This can be done by high speed flaking of partially frozen pieces of
meat (usually from tougher cuts) that are later recombined under pressure with
the addition of hydrocolloid gums (e.g., alginate with a calcium supplement).
The surimi technology is based on using minced chicken/fish meat, which is first
washed (to remove pigments and enzymes) and later extruded to create a musclelike fibrous structure and texture.
Section 13.2.1 further discusses the categories of meat products mentioned in Table
13.1.1 and provides an introduction to the unique characteristics of each category.
This is followed by an explanation of meat and non-meat ingredients used by
the industry (Section 13.3 and 13.4, respectively), protein gel matrix formation
(Section 13.5), meat emulsions (Section 13.6), casings (Section 13.7), and recipes
for twenty popular, high volume meat products produced by the industry (Section
13.8).

13.2.1 Categories of Meat Products

a. Whole Muscle Products
Some of the largest whole muscle products produced by the industry are a whole
ham and a whole oven roasted turkey breast portion (with or without smoke). This
is considered a premium product because it is produced from one intact muscle
portion. A brine solution (i.e., water, salt, spices, and often gums) is injected into the
raw product prior to smoking and cooking. A formula and preparation procedure
for this product are provided at the end of the chapter. This specific formulation
calls for the addition of 30% brine, but some products on the market are produced
with a 50% brine injection, which still results in a high protein level of about 14%.
The brine in this case is injected directly into the large diameter product, but in
the case of small diameter meat pieces it can be added by tumbling (see Chapter
10). In the case of a whole turkey breast, the meat is massaged or tumbled after
brine injection to assist in moisture absorption and help distribute the non-meat
ingredients within the muscle. The latter is important in the processing of any meat
product as an uneven distribution of ingredients can cause serious flavour, colour
and texture problems. Starches and hydrocolloid gums (e.g., carrageenans, see

13-5

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

Section 13.4) are often added to assist in holding the injected brine. Non-meat
proteins such as soy concentrate/isolate and whey proteins can also be added
for the same purpose (see the recipe at the end of the chapter). The turkey breast
muscle can then be placed in a cooking bag or netting (with or without skin) and
smoked and cooked in a smokehouse until an internal temperature of at least 71C
is reached.
b. Restructured Products
Poultry rolls can be made from dark meat, white meat, or their combination.
The meat portions/trimmings can be obtained from the breast, leg, skin, and
mechanically deboned meat (e.g., from poultry, beef, pork). In this product, pieces
of muscle tissue ranging in size from 5 25 cm are glued together to form a
coherent product. This is done with the help of salt, which is used to extract the salt
soluble proteins such as actin and myosin (see previous chapters). During mixing,
these proteins form a tacky coating on the surfaces of the meat pieces. Later, during
cooking they coagulate and the glue is set (similar to the phenomenon seen in a
liquid scrambled egg mix turning into an elastic structure during heating). These
proteins also contribute to moisture and fat holding within the cooked product, as
will be explained later in the chapter. Fat, skin and trimmings are usually finely
chopped (the term emulsified is often used by the industry, even though no
true emulsion is formed) and used to fill the voids between the larger pieces of
meat. Moisture is added to compensate for cooking losses and to improve the
juiciness of the product. If added moisture exceeds a certain fraction of the raw
meat (regulations vary by country), then the product must be labeled accordingly.
The meat and non-meat ingredients are then mixed together until the meat batter
becomes sticky (an indicator of good protein extraction) and all the added moisture
is absorbed. Next, the mix is placed in molds or stuffed into casings and the
product is cooked either in water (moisture-proof casings) or an oven (moistureand smoke-permeable casings), depending on market preference and equipment
availability.
Another example of a restructured product is turkey ham, which is manufactured
from large pieces of turkey thigh meat. The product is usually lower in fat content
than the traditional pork ham and is preferred by some customers. The preparation
procedure (see recipe at the end of the chapter) is typical for a product made from
medium to large sized meat chunks. In the initial manufacturing step, a brine
solution (i.e., water, salt, phosphates, flavourings, and nitrite) is added either by
injection and/or by tumbling of the meat chunks. Tumbling is often used when
the brine is injected to achieve maximum moisture absorption, distribution of the
curing ingredients, and extraction of the salt soluble proteins. The raw meat is then

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

placed in molds (e.g., 4 4 ham molds) or stuffed into large diameter fibrous
casings that determine the shape and size of the final product (see Section 13.7).
Then the product is smoked and cooked to at least 71C. If moisture-proof casings
or metal molds are used, smoke flavourings can be added to the raw meat batter.
c. Ground Products
Fresh breakfast sausage, pepperoni sticks, cured chicken/turkey/duck sausages,
salami and Kolbassa are examples of ground meat products (particle size
commonly range from 0.5 to 2.5 cm) that have been stuffed into casings and
smoked, cooked, and/or dried. Formulations for five such products are provided
at the end of the chapter. These products are usually made from light and dark
poultry meat including trimmings, skin, fat, and a small amount of mechanically
deboned meat. The meat is first ground and then salt, water, and spices are added.
In some products, non-meat proteins (e.g., soy, egg, whey), gums, and/or starches
are added to help with water and fat binding. The products can be stuffed into
edible casings (e.g., collagen) or non-edible casings (e.g., cellulose or plastic) that
must be removed prior to consumption. Fresh sausages need to be cooked by the
consumer while products such as pepperoni and salami are fully cooked by the
meat processor.
Another unique example of a ground meat product is a poultry/red meat summer
sausage, which represents a group of fermented meat products to which a bacterial
starter culture has been added. The poultry product is usually made from dark
meat, skin, and fat. In the process, lactic acid bacteria are used to lower the pH
of the product from about 5.8 to 4.8. This helps to both preserve the product
and provide its typical tangy flavour. In the past, microorganisms from previous
batches were reintroduced into new batches (this practice is called back-slopping),
but today the industry mainly uses starter cultures with a known composition of
microorganisms. The industry can select from a variety of cultures that grow at
different temperatures and produce distinct flavour notes. During the past 30 years
there has been lot of progress in the area of genetic engineering, where desirable
characteristics from one bacterial strain are moved to another. Today, the use of a
starter culture is highly recommended because it ensures that lactic acid bacteria
dominate the fermentation, which both suppresses pathogens (e.g., E. coli O157)
and produces the desired flavours. The fermentation can be controlled by the
quantity of carbohydrate added (i.e., the energy source for the microorganisms) or
by continuous pH monitoring and starting a heating cycle when the desired pH is
reached. After fermentation, the product is smoked, cooked or dried. If the product
is to be sold as a dry product, Canadian government regulations usually require
that it be shelf stable with a low pH (around 4.5) and water activity below 0.90.

13-7

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

d. Finely Comminuted Products

Hot dogs, frankfurters, and bologna are examples of emulsified meat products,
where the product has been finely chopped and results in a very homogenous
appearance. Dark leg meat, trimmings, skin, and/or mechanically deboned meat
are commonly used as the starting materials. The meat is then chopped in a bowl
chopper or an emulsion mill (see Chapter 10), which efficiently minces the meat
particles and emulsifies the fat (i.e., significantly reduces their size and helps
coat the small fat globules with proteins; see further explanation below). Salt is
used to extract the meat proteins, which are essential in binding the small meat
particles and stabilizing the fat globules within the protein matrix (Youssef and
Barbut, 2011; Barbut and Findlay, 1989). Nitrite is added to prevent Clostridium
botulinum growth and provide the typical cured meat colour (Chapters 15 and
16). The meat batter used for small (hot dogs, frankfurters) and large (Bologna)
diameter products and is stuffed into cellulose casings, smoked, and cooked in
a smokehouse. A newer process is the fully automated co-extrusion casing
application, where semi-liquid casing material is extruded onto the meat product as
it comes out of the stuffing machine. In this case, an edible casing such as collagen
or alginate is applied (see Chapter 10), which does not need to be removed prior
to packaging like cellulose casings would. This also helps reduce the potential for
cross contamination (e.g., Listeria), as product handling by workers is minimized.
Since frankfurters are such a popular item, a number of large processors have
constructed dedicated lines to continuously make this product (24/7). As with
other meat products, low microbial contamination and refrigeration temperatures
are essential to the safety and shelf life of these products (some manufacturers
guarantee a shelf life of over sixty days).
e. Coated Products
This category includes bone in and boneless products such as poultry drumsticks
and wings. The products can be coated with batter and breading (e.g., chicken
nuggets) or with a marinade (e.g., honey garlic sauce, BBQ mesquite sauce; see
recipes at the end of the chapter) for a few hours prior to cooking to increase
juiciness and yield of the fresh meat. The addition of moisture, salt, and spices
helps to compensate for evaporation losses during cooking and enhances the
flavour and texture of the meat. Coating systems, which include battering and
breading, are described in Chapter 14. Chicken nuggets, first introduced in the
1970s, are one of the most successful poultry products. The product was originally
prepared from a single piece of slightly marinated breast meat that was battered
and breaded. Later, nuggets made from trimmings (including white meat, dark
meat, skin, mechanically deboned meat and their combinations) appeared on the

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

market. These nuggets are usually prepared by marinating and mixing the meat
pieces with a brine solution. The meat is then formed into the desired shape,
battered, breaded and deep fat fried. Frying preserves the product shape, cements
the batter and breading to the product, and provides the typical crunchy texture.

13.3 Meat Ingredients and Least Cost Formulation

A variety of meats can be used for further processing. As has already been
mentioned, these meats can come from different cuts (e.g., breast, thigh, belly
meat) and states (e.g., fresh, frozen), with or without skin. Formulation of a meat
product requires some basic calculations. Most medium and large sized meat
companies use a computer program to formulate their products. Two of the main
reasons for this are the complexity and time needed to optimize the use of incoming
raw materials (i.e., costs are changing on a daily basis) and to formulate products
with tight specifications (e.g., protein level, fat content, colour, bind value). In the
past, processors commonly used simple formulations with only a few raw meat
ingredients. For such recipes the so-called sausage square calculation (simple
matrix calculation that includes 2-3 meat sources) was sufficient. However, the
diversity of raw materials and price fluctuations in the international markets
require calculating and optimizing formulations for several products concurrently.
In the late 1950s, development of linear programming for sausage manufacturing
began. The original term, least cost formulation (LCF), might mislead people who
are not familiar with the process into thinking that the goal is to formulate the least
expensive product. Instead, the programs are designed to select the lowest cost
meat ingredients after all the requirements (protein level, fat content, colour, bind
value) have been met. Pearson and Taubers (1984) description of the advantages
of such programs is still true today. The programs:
a. p rovide the most economical combination of ingredients for a specific
product within the limitations placed on each ingredient in the formula
b. permit complicated calculations that would not otherwise be possible
c. save time compared to the more laborious traditional calculation (pencil
or a calculator), which can then be devoted to other production problems
d. permit adjustment of formulas on the basis of analysis, using values
obtained from pre-blending or other sources
e. maximize the use of available ingredients
f. help reduce inventory
g. supply accurate procurement information
h. allow making real-time management decisions on production, pricing,
and labour utilization policies

13-9

13-10

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

Today there is a great emphasis on flexibility and traceability, where all data
can be kept on file electronically for a program such as HACCP (see Chapters
6 and 12). This is obviously another example of employing automation in the
meat industry to help streamline processes, reduce labour costs, and save money.
Overall, it should be recognized that computer programming of LCF requires
more basic information on ingredient composition (e.g., chemical composition,
bind value, water and fat holding capacity values), as well as skilled personnel to
operate computers and laboratory equipment. Meat technologists working in the
industry need to understand foundational scientific principles such as emulsion
stabilization and the functional properties of raw materials. This has become far
more important as the number of non-meat ingredients has increased (e.g., dozens
of different modified starches are now available on the market). It is important to
characterize the ingredients and establish constants that can be used to optimize
the quality of the finished product. Two important examples are the bind value and
the emulsification capacity value that had to be initially established for running the
LCF programs.
Dr. Robert Saffle is generally credited with introducing the concept of meat
constants in the early 1960s (LaBudde and Lanier, 1995). The constants were
developed based on the meat emulsion stability test and were needed to develop
sausage LCF programs. Linear programming requires numerical values that
describe each meats specific properties in order to develop the best combination
of raw materials from the few dozen meat cuts/trims available each day to a typical
processor. The programs goal is to calculate the best combination of ingredients
after satisfying requirements set by the operator. As mentioned previously, the
requirements can include protein, fat, and moisture content (Pearson and Tauber,
1984), as well as colour and meat bind values. It is important to note that when
Saffle developed his constant emulsification value, at least one major North
American company had already developed its own criteria for evaluating meat.
Saffles constant emulsification values were generally based on multiplying the
percent salt soluble proteins in a certain cut of meat by the emulsifying capacity
results. Today, various medium and large companies continue to use Saffles values
in one form or another, whereas some large meat companies have developed their
own proprietary criteria for rating meats and use these values in their in-house
developed LCF programs.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

13.4 Non-Meat Ingredients

The meat industry also uses various non-meat ingredients in order to:
a. help extract salt soluble proteins
b. provide flavour notes and enhance acceptability
c. help bind moisture through proteins (e.g., soy, dairy) and carbohydrates
(e.g., starch, carrageenan)
d. enhance juiciness
e. enhance freeze thaw stability through modified starches
f. improve/modify texture (e.g., gelling of soy proteins, alginate)
g. provide colour (e.g., paprika)
h. lower formulation cost
i. add bulk
j. improve sliceability (e.g., forming a carrageenan gel)
k. extend shelf life (e.g., lactic acid, spice extracts)
To simplify the discussion, non-meat ingredients can be divided into several major
groups including water, salts, spices, binders, and fillers.
Limits are imposed on the addition of several non-meat ingredients. The maximum
amounts permitted can be found in local regulations/meat inspection guides. An
example of a restricted ingredient is nitrite, which is added to prevent the growth
of deadly C. botulinum. At high levels, however, nitrite can present a health
hazard and therefore the level is tightly controlled (e.g., 120-200 ppm in USA and
Canada). Other functional ingredients, such as soy protein, are also commonly
regulated. For example, up to 3.5% soy can be added, alone or in combination with
other binders, to a variety of cooked sausages produced in the USA, However, if
this limit is exceeded, the product name must include the words soy added or
imitation to inform the consumer. In most countries, all the ingredients added
to a food/meat product must be listed on the label. Below is an example of an
ingredient list of a Canadian product showing the additives in a descending order
by weight:
Product name: Chicken Frankfurters. Ingredients: mechanically
deboned chicken, chicken, water, wheat flour, salt, modified corn
starch, spice, dextrose, sodium erythorbate, sodium nitrite, smoke.
The names and functions of most common non-meat additives used by the meat
industry are discussed below:

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

a. Water commonly used to compensate for evaporation losses during cooking,

increase juiciness, and reduced fat content in products. The latter reflects the trend
of combining water with ingredients such as hydrocolloid gums and starch. The
amount of added water is regulated in many countries. If the moisture added exceeds
a certain level in the finished product (i.e., after cooking and taking into account
evaporation loss), it should be mentioned in the products name (e.g., Chicken
Roll with Natural Juices/Added Water). Overall, water is the main component in
fresh and processed meats, ranging from 40-80%. Most of the moisture originates
from the lean meat portion (e.g., skinless poultry breast meat has 75% moisture,
see Chapter 3). Industry and consumers add moisture to products (see recipes
at the end of the chapter) because they would have a dry mouth feel if only the
original moisture was present. An example is a chicken fillet cooked at home or
in an industrial oven. Initially, the raw meat has about 22% protein but it ends up
with about 25% protein after cooking and taking into account evaporation loss.
This product will be fairly tough and unacceptable to the majority of consumers.
Added moisture increases product acceptability by compensating for moisture
lost during the heating process. Added moisture also serves as a carrier for spices
and other non-meat ingredients and ensures their adequate distribution. In finely
comminuted meat products (Table 13.1.1), ice is added during chopping to
maintain a sufficiently low temperature so that heat arising from the high friction
during cutting will not cause an emulsion breakdown. Additional discussion on
this topic is provided below in Section 13.6.
The microbiological and chemical quality of the water is an extremely important
issue. From a microbiological standpoint, water should meet the drinking quality
standards (e.g., municipal, national standards) at the very least and should be
checked on a regular basis (see Chapter 6). From a chemical standpoint, water
contaminated with compounds such as nitrate will cause undesirable pinking of
products such as oven roasted chicken breast. Nitrite contamination (1-5 ppm)
can be common in agricultural areas where the water source is located near fields
that are fertilized with nitrates. This is especially of concern after heavy rain (see
additional discussion in Chapter 16). Another consideration is the presence of high
salt levels. Water with calcium and magnesium salts, also referred to as hard water,
can destabilize emulsion-type meat products as well as cause problems within a
plants piping system.
b. Salt various salts can be added to meat products. The most common salt is table
salt (sodium chloride), which is used as a flavouring agent, protein solubilization
agent, and anti-microbial agent. Phosphates are another group of salts used to help
with meat protein extraction and solubilization (e.g., sodium tri-polyphosphate
is used to help extract myosin and actin). Other salts include sodium nitrite (for
preservation) and curing accelerators such as sodium erythorbate and sodium
ascorbate.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

b1. Sodium chloride (NaCl) is the most common ingredient added to meat
products because of its three major contributions:
1. S
 odium chloride provides a distinct salty flavour, which makes a
substantial contribution when added to processed food. The classic
salty taste is represented by NaCl and lithium chloride (LiCl), whereas
other salts usually have additional flavours associated with them that
can include a mixture of sweet, bitter, sour, and salty. Chemically, it
appears that cations cause salty tastes, whereas anions inhibit salty tastes
(Sebranek and Bacus, 2007).
Among the anions, Cl is the least inhibitory to the salty taste and does
not possess a taste of its own. Some anions can not only inhibit the taste
of their associated cations, but also contribute tastes of their own. An
example is the soapy taste associated with certain phosphates, which
results from the specific taste elicited by their anion.
In general, the most accepted model for describing the mechanism for
salty taste perception involves the interaction of hydrated cation-anion
complexes with the Shallenberger and Acree AH/B-type receptor site.
The individual structures of such complexes vary substantially. In the
presence of water, OH groups and salt anions/cations are associated with
specific receptor sites. Bitterness in salts involves a different receptor
mechanism that seems to be related to the sum of the ionic diameters of
the anion and cation components of the salt. Salts with ionic diameters
below 6.5 are salty in taste (LiCl = 4.98 , NaCl = 5.56 , KCl = 6.28
), although some individuals find KCl somewhat bitter. As the ionic
diameter increases (CsCl = 6.96 , CsI = 7.74 , MgCl2 = 8.50 ), salts
become increasingly bitter.
In any case, a processor should always try to use the highest quality
salt possible. High quality refers to low levels of impurities (e.g., heavy
metals such as copper, iron). These trace contaminants are known as prooxidants and can trigger fast lipid oxidation during storage, as will be
discussed later in the chapter when antioxidants are introduced.
2. S
 odium chloride is involved in the protein extraction of the salt soluble
fraction (mainly myosin and actin; see also Chapter 3), which is very
important in the production of processed meat products as these proteins
can bind meat pieces/chunks when heated. Overall, extracting the
proteins and bringing them to the surface provides sticky surfaces on the

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

raw muscle cuts. These proteins also help bind moisture (i.e., increasing
the water holding capacity, WHC), assist in emulsifying fat particles in
comminuted products (by coating the fat globules), and increasing the
raw meat batter viscosity. Later, these extracted proteins coagulate and
bind both the meat particles (important for holding the product together)
and moisture (important to minimize cooking losses) to form a coherent
matrix that is important for texture as well as fat retention during heat
processing.
Salt reduction (mainly sodium) in food/meat products was a hot topic
in the 1980s and is again today, as more individuals are suffering from
hypertension (high blood pressure). Besides the organoleptic effects,
an important consideration in replacing NaCl with other chloride salts
is the effect on the physical properties of the final product. Sodium
chloride reduction by itself will result in lower binding and lower WHC
of the proteins. Upon heating, this will result in a softer, drier product
with higher cooking losses. If cooking losses are too high the product
will be unacceptable to the consumer. The relationship between salt
concentration and WHC has been well established and depends on
factors such as the amount and type of protein present, pH, and previous
storage history. In post-rigor lean poultry meat, an increase in salt results
in a concomitant decrease in product shrinkage up to a maximum
at around 5% salt (Fig. 13.4.1). Further salt addition will result in a
decreased WHC, a phenomenon known as salting out. This is the
result of increasing charges on the protein molecules, which causes them
to precipitate.
3. S
 odium chloride suppresses microbial growth, as many microorganisms
are sensitive to high salt levels. High salt concentration can stop or
substantially slow the growth of microorganisms. In the past, high salt
levels (10 to 20%) were used as the main means of preservation because
these levels can provide shelf-stable meat products. This technique is
still used in places where refrigeration is a challenge and/or where the
traditional heavily salted products are preferred (i.e., the very high salt
content has to be washed out before consumption). However in many
markets today, substantially lower salt levels are used (e.g., 1.0 to 2.5%),
and it is only in conjunction with other additives (e.g., nitrite, lactic acid)
and appropriate refrigerated storage that product safety can be ensured
(Barbut and Findlay, 1989; Sebranek and Bacus, 2007).

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

b2. Sodium Nitrite (NaNO2) and Sodium Nitrate (NaNO3) also known as
curing salts, are added at very low levels (usually 120-200 ppm in the USA) and
have four main functions.
1. P
 revent Clostridium botulinum spore germination. The active compound
is nitric oxide (NO) and it inactivates C. botulinum spores. Only a very
small amount is needed and using the salt form provides an easy and
efficient way of introducing the active compound to the meat. It can also
be introduced in gas form in a lab setting.
2. C
 ontribute to the development of the typical pink cured meat colour.
Again, the active compound is NO. This pink colour is very different
from the brown colour of a cooked product such as chicken leg meat,
turkey thigh, pork chop, or pork loin. This can be described as the
difference between a home-cooked pork chop and a cured pork ham (see
additional discussion in Chapter 16). The chemical reaction involved is:
Myoglobin + NO Nitrosomyoglobin Heat Nitrosohemochrome
The nitrosohemochrome produces the typical pink pigment found in
cured meat products.
3. P
 rotect against lipid oxidation. Nitrite has antioxidant capabilities that
can help prolong the shelf life of meat products.
4. A
 dds some flavour. Nitrite addition results in the development of certain
unique flavour notes.
Overall, the chemical reaction of sodium nitrite (potassium nitrite is
also used sometimes by the industry) added to a meat system is shown
below. Sodium nitrite is broken down into its components:
NaNO2 HONO + Na + H2O
3HONO HNO3 + 2NO + H2O
The amount of nitrite permitted in meat products is heavily regulated
because at high levels it can be toxic. It is very important to note that
processed meat products are not necessarily a high source of nitrite in
our diet. In comparison, green vegetables such as celery have levels of
about 300 ppm nitrate. In addition, bacteria in human saliva and in the
gut are capable of producing even higher levels of nitrite. Nitrite added

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

to meat products is depleted over time, especially during cooking, and a

frankfurter with an initial 150 ppm NaNO2 level will end up with about
20-40 ppm or less at the point of purchase. Overall, it is estimated that
meat products contribute only 10-20% of the total nitrite in our diet
(Sindelar and Milkowski, 2012). There is also a concern in products
heated to high temperatures (e.g., bacon) that residual nitrite could react
with secondary amines to form nitrosamine compounds, which are
potential carcinogens. Therefore, in North America for example, the
use of an added curing accelerator (e.g., 500 ppm ascorbate) has been
mandated in such products to ensure a fast conversion of nitrite to nitric
oxide. This minimizes the chance of nitrosamine formation when the
product is exposed to high temperatures (frying at > 100C). The use of
nitrite in processed meat products and its safety has been reviewed by
Cassens (1990) and by Sindelar and Milkowski (2012).
b3. Phosphates salts of phosphoric acid can work together with sodium
chloride to enhance muscle protein extraction, which in turn improves the water
holding capacity and reduces shrinkage during cooking (Fig. 13.4.1). There are
different types of phosphates available on the market. Examples of common
polyphosphates and orthophosphates in meat products are shown in Figure 13.4.2.
Alkaline polyphosphates such as tripolyphosphate (TPP) are the most popular and
by some estimates account for about 80% of the phosphates used by the meat
industry. Phosphate use is limited to 0.5% in the finished product in countries such
as the USA. This limit is mainly imposed to restrict water addition but greater
levels can also result in off flavour problems such as metallic or soapy as reported
by consumers. In countries such as Germany, the use of phosphate is not permitted
in several products.
The effects of using 0.5% TPP, pyrophosphate, and a commercial blend called
KENA (which contains over 50% TPP) are shown in Figure 13.4.1. A synergistic
effect is clearly seen when TPP is used with 2-5% salt; i.e, the combined effect of
NaCl and TPP is much greater than the simple additive effect of NaCl and TPP.
The salting out effect, previously discussed, is clearly seen at a salt level above
5%. Pyrophosphate and NaCl show an even greater synergistic effect compared
to TPP (Fig. 13.4.1) but pyrophosphates are not commonly used due to their
effect on pH and other factors. Hexametaphosphate, for example, results in higher
shrinkage during cooking. This raises the point that processors should know
exactly what kind of phosphate(s) or blend they are using but this is information
that some ingredient companies are not eager to share. However, with the new
Material Safety Data Sheet (MSDS) requirements, this information is becoming
easier to access by the meat processor.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Fig 13.4.1

0
1
2
3
HMP
NO PHOSPHATES 4
TPP
5
KENA
6
PP
7
8
9
10

35
30

% SHRINK

25
20
15
10
5
0
0

% NaCl IN MEAT

10

Figure 13.4.1 Effect of NaCl on the shrinking of cooked chicken muscle (70C) in the presence
of salt and different polyphosphates (0.5%). HMP hexa meta phosphate; TPP tri poly
phosphate; KENA commercial phosphate blend; PP pyro phosphate (sodium acid).
Redrawn from Shults and Wierbicki (1973).

Most phosphates used by the meat industry help enhance the physical and sensory
properties of meat products by:
a. H
 elping extract the salt soluble proteins, hence increasing water holding
capacity and meat particle binding.
b. Shifting the pH away from the isoelectric point of the muscles proteins,
hence allowing more charges on the amino acid side chains. This can
result in increased repulsion between the proteins, which creates more
space for water molecules and more sites for water molecule binding.
c. Assisting in stabilizing meat emulsions due to the hydrophilic/
hydrophobic structure of the molecule
d. Slowing down oxidation due to the chelating effect of phosphate.
Certain phosphates can bind iron and other metals and prevent them from serving
as pro-oxidants. This helps extend the shelf life of the meat product in terms of
flavour but also protect it from meat pigment oxidation (colour problems).
In general, phosphates act in a food/meat system as polyanions that increase ionic
strength, control pH by buffering, and sequester meat ions. Some researchers claim
that the increase in water holding is due to an unspecific ionic-strength effect. As
indicated above, increasing the net negative charges will result in repulsion of the
protein groups, which creates more space for water molecules within the muscle.

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

However, the effect of a molecule such as pyrophosphate on WHC appears to be

greater than would be expected due to its ionic strength alone. Therefore, several
have
impliedstructure
a specific
pyrophosphate
effect, where
pyrophosphate
Figureresearchers
13.4.2 The
chemical
of sodium
tri polyphospate
(STPP)
commonly used in
was reported
to
dissociate
actomyosin
into
actin
and
myosin
(i.e.,
pyrophosphate
meat processing (solubility 14.5 g in 100 ml at 25 C; pH of
1% solution is 8.0).
Wikipedia.
More detailed
information from Material Safety Data Sheet
is capableFrom
of degrading
the actomyosin
complex).
can be found at: http://www.sciencelab.com/msds.php?msdsId=9927608.

FigureOxidation
13.4.2 The chemical
structure
of sodium
tri turkey
polyphospate
(STPP)Legends:
commonly used
in meat
Figure 13.4.3
byproduct
values
of raw
sausage.
a) no
additives ();
processing
14.5 ();
g in 100
at 25 C;only
pH of();
1% solution
is 8.0).+From
Wikipedia.
Moree) spice +
b) (solubility
1.7% salt
c)mlspice
d) spice
rosemary
();
detailed information
from Material
Safety Data
Sheet
can be found at:
BHA/BHT
(). Adapted
from Barbut
et al.
(1985).
http://www.sciencelab.com/msds.php?msdsId=9927608.

b4. Sodium Ascorbate and Sodium Erythorbate also known as curing

accelerators, they are added to increase the rate at which nitrite is reduced to nitric
oxide in an aqueous solution. In a meat system, some of the muscles enzymes
help reduce the nitrite. However, in order to speed up the conversion to nitric oxide,
curing accelerators that promote reducing conditions are added. Note that they
also accelerate the reduction of metmyoglobin to myoglobin. This is especially
important in continuous sausage production lines, where the processors objective
is to start cooking the product within an hour of blending and adding the nonmeat ingredients. In other cases, such as the manufacture of dry sausages, a slow
nitric oxide release is preferred and curing accelerators are not needed. In these
cases, processors are actually using sodium nitrate, which takes even longer to
breakdown to nitric oxide than sodium nitrite, so they get a prolonged release of
nitric oxide.
Sodium ascorbate and sodium erythorbate (or their corresponding acids ascorbic
acid and erythorbic acid) are used at low concentrations of about 550 ppm. For
products that will be exposed to high temperature cooking (e.g., turkey/pork
bacon), a number of countries require that a curing accelerator be added as high
temperatures can increase nitrosoamine96formation (see previous discussion on
nitrite).

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

c. Spices used to flavour and colour foods (e.g., paprika) as well as to add some
antimicrobial/antioxidant (e.g., rosemary) properties. In several cases they are
also used to enhance appearance (e.g., peppercorns on barbequed meat). Various
countries restrict the use of artificial food colouring in processed meat products,
hence the utility of spices for this purpose.
Examples of spices derived from different plant materials are listed below.
a.
b.
c.
d.
e.
f.
g.

seeds nutmeg (Myristica fragrans), mustard (Brassica nigra)

leaves sage (Salvia officinalis), thyme (Thymus vulgaris)
bulbs garlic (Allium sativum), onion (Allium capa)
fruit pepper (Piper nigrum), paprika (Capsicum annuum)
flowers clove (Eugenia caryophyllata)
bark cinnamon (Cinnamomum zeylanicum)
roots ginger (Zingiber officinale)

Spices can be added in different forms depending on the product, desired

appearance, expected shelf life, etc. In most commercial applications they are
added dried or after a heat treatment because they are then easier to handle (e.g.,
elongated shelf life, inactivated enzymes that can produce off flavours/colours in
the meat) and easier to standardize (e.g., strength/heat of pepper). Overall, spices
can be added before or after being dried (e.g., onion), whole or ground (e.g., black
pepper, mustard seeds), or as extracts (e.g., rosemary oleoresin). The decision as
to what form used is based on the meat product type and desired appearance. In
coarse ground products such as kielbasa (see recipe at the end of the chapter),
whole mustard seeds can be added so the cross section of the product has a nice
appearance. However, in a finely comminuted frankfurter whole mustard seeds
would not be as attractive.
Spices commonly carry a high number of microorganisms. Therefore, they should
be thoroughly cleaned and pasteurized or sterilized. Heat treatment is an option, but
is typically not the best approach because it releases many of the volatile flavour/
aroma compounds. Therefore, non-heat processes such as ionizing irradiation
and chemical pasteurization (e.g., ethylene oxide) are commonly used. Both are
considered cold processes that do not volatilize the flavour/aroma compounds.
Ionizing radiation is used quite extensively and usually irradiated spices do not
have to be identified as irradiated in the meat product ingredient statement, because
of the low level of addition. If the whole product is irradiated, however, certain
countries require that the international logo for irradiated food appear on the label
(see Chapter 11). Chemical sterilization possesses are also commonly used but
some consumer groups are concerned with the potential risk of residues.

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

Large volumes of spice extracts, which contain essential oils and oleoresins
extracted from plant material, are sold to the meat industry. The oils can be obtained
by pressing, distilling, or solvent extraction, and they are usually concentrated to
obtain a more potent solution. The oils will be free of microorganisms if a high
distillation temperature or a strong solvent is used. Overall, the advantages of using
oil extracts include reduced transportation costs, long shelf life, and they do not
change the appearance of the product. In finely comminuted products such as hot
dogs and bologna, which have a very homogeneous appearance, this latter point
is very important (e.g., adding visible ground black pepper particles would not be
acceptable to the consumer). The extracts are usually highly concentrated and are
commonly sprayed on to a carrier such as salt or sugar (dextrose) in order to assure
an even distribution within the product.
Standardizing the flavour strength is an important consideration when using natural
spices or extracts. Spice companies purchase materials from around the world and
factors such as growing conditions, climate, and plant variety can result in large
variations in taste. To overcome this, spice companies employ trained personnel
to standardize flavour profiles and obtain defined strengths (e.g., determine the
Scoville Heat Unit for red pepper). This is extremely important to meat processors
who want to create a consistent product. When standardizing the flavour of a spice,
a technician prepares serial dilutions of the extract and presents them to a trained
panel to identify the lowest concentration the panel can detect. This lower threshold
can be used to standardize the flavour. Additional sophisticated equipment such
as a gas chromatograph can also be used to determine the concentrations of key
flavour compounds that contribute to the overall flavour of a spice. In the case of
colour standardization of a spice such as paprika, the red colour intensity can be
described by the scale developed by the American Spice Trade Association (i.e.,
measuring absorbance of a sample diluted in acetone at 460nm).
d. Flavour Enhancers are compounds that act synergistically with meat
flavour compounds to enhance the meaty flavour. A few of the most commonly
used ones are 5-ribonucleotides, hydrolyzed yeast proteins, and monosodium
glutamate (MSG). When used at levels in excess of their independent detection
threshold these compounds contribute to what is called the delicious or umami
taste of foods. When used at levels below the independent detection threshold they
simply enhance flavours. It is important to recognize that a very small percentage
of the population is sensitive to ingredients such as MSG (i.e., they suffer from
headaches and nausea when eating MSG). Therefore, MSG should be clearly
marked on the package or at a restaurant buffet.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

e. Sweeteners and Browning Agents ingredients commonly used in low

amounts to add a sweet flavour, mask saltiness, enhance browning (i.e., the
Maillard reaction between proteins and carbohydrates), and provide a substrate for
fermentation (e.g., in salami where they are added as an energy source for lactic
acid bacteria).
Overall, natural and synthetic sugars vary in their sweetness. The standard for
the measurement is sucrose (a disaccharide composed of glucose and fructose
that comprises cane sugar), which is assigned a sweetness value of 100. On that
scale, dextrose (a monosaccharide of glucose) has a value of 74, fructose has a
value of 175, maltose (disaccharide of two glucose monomers) has a value of 40,
lactose (or milk sugar) has a value of 16, regular corn syrup solid has a value of
37 (therefore it can also be used as a partial bulking agent; see discussion below),
aspartame has a value of 180, and sucralose has a value of 600. There is a wide
selection of sugars to choose from and most commonly the meat industry uses
natural sugars at about 1 3 %. The reason for adding the sugar often determines
the type used. Reducing sugars contribute to the Maillard browning reaction when
they combine with secondary amines to form a brown pigment during heating.
Adding a reducing sugar such as dextrose, fructose, or maltose to a meat product
will enhance surface browning. This is important in smoked sausages where a
golden/brown colour is desirable (see recipe for smoked flavour turkey sausage at
the end of the chapter). Reducing sugars can be also added to fried products where
adequate golden/brown colour development during heating prevents overcooking/
burning the sausage.
f. Antioxidants important compounds used to suppress lipid oxidation. This is
a critical issue in meat and meat products as animal fat is prone to lipid oxidation
due to its fatty acid profile (including unsaturated fat; see also Chapter 7), there
is disruption of cells during processing (e.g., cutting, chopping of meat), and
enzymes are released during processing, heat treatments, and prolonged storage.
In living tissues there are various natural antioxidants (e.g., tocopherol/vitamin
E), however they are not always sufficient to protect the meat/meat products after
processing. The process of oxidation is driven by free radical formation and, once
started, it accelerates exponentially as one free radical forms two, two then form
four, etc. The food industry uses three types of antioxidants:
a. free radical terminators,
b. oxygen scavengers, and
c. chelating agents capable of tying up metal ions.

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13-22

Figure 13.4.2 The chemical structure of sodium tri polyphospate (STPP) commonly used in
meat processing (solubility 14.5 g in 100 ml at 25 C; pH of 1% solution is 8.0).
From Wikipedia. More detailed information from Material Safety Data Sheet
can be found at: http://www.sciencelab.com/msds.php?msdsId=9927608.

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

Because governments have certain restrictions on using synthetic antioxidants and

some are not permitted, natural antioxidants such as rosemary oleoresin are an
attractive option and are also label-friendly. In this case, they are only listed by the
spice name. Products such as a low-flavour rosemary oleoresin are also available,
where most of the flavour compounds have been removed so that the amount of
the oleoresin added to the product can be increased. Citric acid is another example
of a molecule that is an oxygen scavenger (i.e., can tie up free oxygen).
Figure 13.4.3 Oxidation byproduct values of raw turkey sausage. Legends: a) no additives ();
b) 1.7% salt (); c) spice only (); d) spice + rosemary (); e) spice +
BHA/BHT (). Adapted from Barbut et al. (1985).

Figure 13.4.3 Oxidation byproduct 96

values of raw turkey sausage. Legends:
a) no additives (); b) 1.7% salt (); c) spice only ();
d) spice + rosemary (); e) spice + BHA/BHT ().
Adapted from Barbut et al. (1985).

The industry also uses synthetic antioxidants such as butylated hydroxy toluene
(BHT), butylated hydroxy anisole (BHA), and propyl gallate (PG). These
compounds are free radical terminators, as they have a cyclic carbon ring structure
that is capable of accepting a free radical molecule. These three compounds are fat
soluble and their usage level (where permitted) is commonly limited to 200 ppm
of the fat content. Figure 13.4.3 shows the beneficial effects of using a BHA/BHT
mixture (200 ppm) and natural rosemary oleoresin on delaying lipid oxidation
in a turkey sausage produced with 25% mechanically deboned meat, which is
highly susceptible to oxidation (see Chapter 9). Both the mixture and the rosemary
oleoresin were very effective in suppressing oxidation in the stored product. The

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

spice mix used in isolation also resulted in some antioxidant activity as compared
to the meat control treatment. Figure 13.4.3 also illustrates the effect of salt, which
can accelerate lipid oxidation due to a small amount of heavy metal (e.g., iron)
contamination. The data is reported as the amount of malonaldehyde (i.e. an
oxidation byproducts from the breakdown product of oxidized fatty acids), which
is commonly used in the literature to follow lipid oxidation. The publication also
lists the amounts of other byproducts (e.g., hexanal, heptanal, penanol; measured
by gas chromatography) that contribute to off odours that can be detected by a
sensory panel.
g. Starter Culture bacteria capable of producing lactic acid are added to
fermented sausages, such as pepperoni and summer sausage. Lactobacillus
plantarum and Pediococcus acidilactici are used to ferment the added sugars and
produce lactic acid, which decreases the pH of the product. This helps to make the
product shelf-stable and provides unique flavours and textures. Processors should
add a simple sugar source (e.g., mono, disaccharide) to prevent bacterial utilizing
of fat and proteins which will result in the formation of oxidized compounds and
putrefied odours. In the past, processors relied on the naturally occurring lactic acid
bacteria or an innoculum from a previous batch of products for the fermentation.
Today, however, many use a standardized, controlled starter culture produced
by specialized companies. When using starter cultures the inoculation level is
107 bacteria per gram meat of the good lactic acid bacteria so it dominates the
fermentation. Concerns with E. coli O157:H7 have also driven the industry to use
starter cultures to assure fast and efficient fermentation.
h. Mold inhibitors are used to inhibit growth on the surface of dry and semi-dry
sausages that are not vacuum packed (molds are aerobic). This can be a problem as
these products have a water activity that supports mold (but not bacterial) growth.
Mold inhibitors are applied by dipping or spraying the outside casings. Common
chemical inhibitors include potassium sorbate and sorbic acid. These compounds
are permitted for use in some countries (e.g., USA), but not others (e.g, Canada).
In countries where these compounds are not permitted processors can use a cold
smoke treatment that contains natural antimicrobial compounds (see discussion
below) that help prevent mold growth.
i. Binders are ingredients used to help bind meat particles and increase water
holding capacity (see also Section 13.5). These ingredients usually consist of
proteins that can form a gel system or participate in meat protein gelation. It is
obviously advantageous if they act synergistically with the meat proteins (see Fig
13.5.1, Aguilera and Kessler, 1989). These ingredients can be expensive so when
processors consider using them they should look for added values such as:

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

a.
b.
c.
d.
e.

texture enhancement
water holding; i.e., reducing shrinkage during processing
improved products formulation
emulsification capabilities
reduction of formulation cost

The meat industry commonly uses dairy binders (e.g., milk powders and their
derivatives), vegetable proteins (soy, pea), and meat proteins (collagen, blood
plasma).
Examples of dairy binders:
a. W
 hey proteins a by-product of cheese manufacturing, and very
effective in meat products. After gentle drying (i.e., to prevent protein
denaturation) they are sold as a powder with about 70% protein
(marketed as whey protein concentrates) and with about 90% protein
(marketed as isolates).
b. Caseinate sold after drying as a highly functional ingredient that has
80-90% protein content. One of its main uses is in emulsified products.
c. Non-fat dry milk contains about 35% protein (80% is casein) and
about 50% lactose.
d. Calcium reduced non-fat dry milk used for finely chopped/emulsified
products where high levels of calcium can be detrimental to emulsion
stability.
Examples of vegetable protein binders:
Soy proteins commonly used as binders in products such as meat patties, meat
loaves, and sausages. In a number of countries their presence is limited to 2%
soy protein isolate or else the product name should include the word soy. Other
vegetable proteins such as pea are also used but to a lesser extent. The vegetable
proteins are also marketed under certain categories:
a.
b.
c.
d.

Soy/pea protein flour (fine particles with 40-60% protein)

Soy/pea grits coarse particles with 40-60% protein
Soy/pea protein concentrates with 70% protein and bland flavour
Soy/pea protein isolate with 90% protein, bland flavour, and high
water/fat binding capacity
e. Textured soy/vegetable protein cooked and extruded particles sized to
order, with or without flavour and/or colour added

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

It should be noted that vegetable protein flours and grits usually have a distinct
flavour (beany) if used at a high concentration. Much work has been done over the
past decade to minimize this problem and today the standards for low beany off
flavours are much higher.
j. Fillers are non-meat ingredients, usually made with complex sugars (e.g.,
starch) and low protein, that help bind water but not meat particles and are usually
considered to be good as bulking agents.
Fillers can be divided based on their cereal source (wheat, corn, starch) and are
added to the meat product either as flours or extruded/texturized particles. When
starch is heated past its gelatinization temperature in the presence of water it
opens up to bind water (e.g., can be 1:2 up to 1:10 ratio). At high temperatures the
solution becomes more viscous and when temperature is lowered (e.g., cooling
food/meat products after heating) the texture will become even more viscous. The
meat industry also uses pre-gelatinized starches where the starch manufacturer has
heated the product (in a solution) and then dried it. This creates a product that is
capable of binding water at lower temperatures, which is advantageous for the
meat industry because as meat proteins are heated (and denatured) they bind less
water. Please note that another popular application of flour and starches is in coated
products (see Chapter 14).
k. Hydrocolloid gums are unique compounds that are capable of forming a
high water gel matrix at low concentrations (e.g., at 1% carrageenan forms a very
firm gel after heating, which nicely binds the rest of the 99% water). Such gums
are added to meat products at relatively low concentrations to bind added brine/
water (see Turkey Pastrami recipe at the end of the chapter). In this case the firm
gel (upon cooling) also helps enhance the texture. Many gums are obtained from
seaweed, some are extracted from seeds, and others are the result of microbial
fermentation. Below are a few examples of common hydrocolloid gums:
a. A
 lginate is extracted from brown algae (Phaeophyta) that is usually
harvested off the coasts of Ireland (Davis et al., 2003). Alginate is
composed of manmuronic and guluronic acid monomers; the ratio
between them determines the brittleness of the gel, water holding, etc.
Since the algae are harvested at different places and during different
seasons, there are variations in the gelling performance. Therefore, it
is important that the meat processor uses a supplier who is reputable
and can control and standardize the gel performance. One of the
unique characteristics of alginate is its ability to gel at room/refrigerated
temperature instantly when a small amount of calcium ions is added.

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

The meat industry uses it for binding raw meat particles in products such
as restructured cutlets (Fig. 13.4.4) in order to provide binding of the
smaller meat trimmings and hold the product together prior to cooking.
It isMeat
alsotrimmings
used today
make
casingsgum
(Harper
2013) that
are coFigure 13.4.4
boundtowith
an alginate
to formeta al.,
restructured
product.
The
bindingdirectly
is done onto
at lowthe
temperature
withdiscussion
the help ofin
CaCl2
with10).
causes cold
extruded
product (see
Chapter
gelation of the alginate. Showing a raw chicken and beef products, as well as the
resulting cooked beef product. Photo by S. Barbut.

Figure 13.4.4 Meat trimmings bound with an alginate gum to form a restructured product. The binding is
Figure
Carrageenan
gels
(1%)
madewhich
by the
addition
of hot of
water
(85 C)Showing
followed
done at13.4.5
low temperature
with the
help
of CaCl
causes
cold gelation
the alginate.
rawby
2
cooling
(see text
for as
explanation).
The gel
the left
wasbymade
from nonchicken and
beef products,
as well
the resulting cooked
beefon
product.
Photo
S. Barbut.
refined carrageenan and the one on the right form refined carrageenan. The later
produced a clearer, harder, and more elastic gel, but with more syneresis. Photo
by S. Barbut.

b. C
 arrageenan gum that is extracted from Irish moss (Chondrus crispus
Stackh.) found along the Atlantic coast of the British Isles, Europe and
North America. It is composed of monomers of sulfated galactose
and anhydro-D-galactose. The gum is a complex mixture of about ten
different polymers. The main ones used by the meat industry are kappa
and iota (note: some lambda is also used to increase viscosity but it is a
non-gelling component). The type of gel formed depends on refining
the raw material (Fig. 13.4.5), the dominant polymer in the mixture and
the cation used to induce gelation during heating. Carrageenan forms a
reversible gel (i.e., can be remelted and reformed), is very effective at
binding water, and is added to products where water is used to replace
fat such as oven roasted turkey/chicken breast products and low fat
sausages.
97

Figure 13.4.5 Carrageenan gels (1%) made by the addition of hot water (85 C) followed by
cooling (see text for explanation). The gel on the left was made from nonrefined carrageenan and the one on the right form refined carrageenan. The later
produced a clearer, harder, and more elastic gel, but with more syneresis. Photo
THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT 13-27
by S. Barbut.

Figure 13.4.5 Carrageenan gels (1%) made by the addition of hot water (85 C) followed by
cooling (see text for explanation). The gel on the left was made from non-refined
carrageenan and the one on the right from refined carrageenan. The latter
produced a clearer, harder, and
97more elastic gel, but with more
syneresis. Photo by S. Barbut.

c. X
 anthan gum is produced by microbial biosynthesis and is an
extracellular polysaccharide. It is composed of cellulose chains with
attached oligosaccharide groups. Low xanthan concentrations produce
a highly viscous solution. Together with locust bean gum, xanthan can
produce a thermo-reversible gel.
l. Acids/Acidulants used to reduce pH, add flavour, extend the self-life and/or
produce a fermented-like meat product. A common example of an acid is vinegar
and an example of an acidulant is glucono delta lactone (GDL; introduced in the
1960s), which can yield a more rapid and improved colour development to cooked
comminuted meat products. An important advantage of using GDL is its slow
acid release that does not cause a problem with later protein binding (note: adding
a large amount of liquid acid to a meat product at the beginning of the process will
result in early protein denaturation, poor binding, and decreased WHC). Although
GDL was introduced to accelerate raw meat processing operations, it has been
later used in the production of fermented-like meat products (e.g., pepperoni for a
pizza topping and other industrial acidified products).
Encapsulated acids (e.g., lactic, citric) are another way to add acids to produce a
fermented-like products. The encapsulation material (wall component) is usually
made of hydrogenated vegetable oil with a melting point that has been adjusted
to be slightly higher than denaturation temperature for major meat proteins (e.g.,

13-28

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

60-65C). Other sensitive compounds can also be encapsulated (e.g., flavours)

to protect them until needed (e.g., coating material can be designed to be broken
by saliva, enzymes or mechanical shear). Overall, the market for encapsulated
flavour, sensitive oils, and vitamins has been growing at a tremendous rate over
the past three decades.
In the food ingredient business, the area of nanotechnology including
encapsulation, is becoming an important topic. Currently there is quite a lot of
use of encapsulation technology, but not so much at the nano scale. As mentioned
above, encapsulation is used to protect food additives such as flavour compounds,
vitamins, sensitive omega-3-fatty acids, and microorganisms (e.g., to protect some
probiotics from the stomachs low acidity and only release them later on in the
gut). This topic is beyond the scope of this book, but further information can be
found in Prakash et al. (2013) and Graffagnini (2010).
m. Natural and Liquid Smoke are mainly used to provide flavour, colour
(Maillard reaction), antimicrobial protection, and antioxidant compounds to the
surface of the product. Historically, smoking meat cuts over an open fire was
used to preserve different products. The exposure to mild/high temperature for an
extended period of time (e.g., several days; not currently used in the industry) also
resulted in significant drying. Today, smoking is commonly employed for a short
period of time (e.g., 10 - 90 min) and is mainly done to add flavour and colour and
to help increase the shelf life to the product.
There are several hundred different compounds in natural smoke. Maga (1989)
and Toledo (2007) reported over 300 in some of the commonly used hard woods
(maple, cherry). The compounds can be divided into four groups:
a. carbonyls contribute to flavour and colour development
b. organic acids help in preservation and coagulate surface proteins (i.e.,
assist in casings peeling)
c. phenols contribute to colour and flavour development, preservation,
and retard oxidation
d. polycyclic hydrocarbons are created when high burning temperatures
are employed; some of the compounds, such as benzopyrene, are
potentially carcinogenic.
Smoke can be applied by burning the sawdust or pieces of hard woods (e.g.
maple, cherry) or as a liquid smoke solution. The former is achieved with the help
of a special generator outside the smokehouse. As the moist sawdust is slowly
burned, the smoke is circulated into the smokehouse by a fan system usually for

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

10 30 min. During this process, the exhaust duct must be closed so smoke can
accumulate and is not wasted. The products surface must be dry (it could be wet
due to condensate) or else the smoke will drip off. Liquid smoke is a newer product
that is prepared in dedicated facilities where smoke compounds from burning
wood are captured by letting the smoke rise inside a tall chimney equipped with
a counter flow water shower. The smoke compounds can later be concentrated
and the preparation is applied to meat products as a dip, spray, or atomized mist.
An advantage of this process is the ability to separate some/most of the polycyclic
hydrocarbons by allowing then to settle out. In addition, some liquid smoke
products can be added directly to the raw product after the pH has been adjusted.
n. Enzymes several groups of enzymes can be added to meat products for
a variety of reasons. The two main groups are used for binding meat particles/
surfaces and for tenderizing tough meat cuts. Transglutaminase is an example of
commercially available enzyme used to bind meat pieces at low temperature (i.e.,
prior to cooking) in products such as those that have been restructured. This specific
enzyme has been used for hundreds of years in the production of fish surimi,
although the chemistry was not understood until recently. Transglutaminase is
able to catalyze acyl transfer reactions and introduce covalent cross links between
proteins. It is now commercially harvested from microbial fermentations.
The other major group of enzymes used is the one that can break down connective
tissue. Papain and ficin extracted from pineapples and figs respectively are able to
break down collagen and are sometimes used to tenderize meat. However, their
activity should be stopped at a certain point as extensive proteolysis can turn the
meat into mush.

13.5 Meat Protein Gelation and Binding

Note that sections 13.5 and 13.6 contain more detailed reviews of the protein
gelation, binding, and emulsification topics to help the reader understand the
relationships between the science and practical application of meat processing
principles.
Proteins are the main building blocks of meat products. Thus protein type (e.g.,
myofibrullar, sarcoplasmic, stromal proteins; see Chapter 3), configuration (Fig.
13.1.2), quantity, and quality (e.g., fresh vs. frozen) have major impact on the final
meat product characteristics. The product is also affected by processing parameters
such as the size of the meat pieces (small vs. large), addition of ingredients (e.g.,
salts, acidulants, gums), and cooking method (e.g., hot air vs frying). Overall, the

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

proteins interact with other components in the meat batter/product to form a gel
matrix. In any case, it should be recognized that proteins are the main functional
ingredient in meat products while the other two main components, water (3075%) and fat (5-30%), are important but do not directly contribute to structure
building. When discussing proteins contribution to structure it is useful to look at
its interactions with the other components in the meat product:
a. Protein-protein interactions: this is one of the main mechanisms that
contribute to the formation of an elastic gel upon heating of meat products. As
discussed in Chapter 3, there are over 50 different muscle proteins. The amount
and type of extracted salt soluble proteins (myofibrillar) and their later associations
during heat processing has a strong effect on the meat products characteristics. As
will be highlighted in the following comment, not all meat proteins can form a gel
and some proteins such as collagen actually melt when cooked (e.g., 65-72C) and
will only form a gel upon cooling (e.g., the basis of Jell-O manufacturing). This
example is mentioned here so the reader can understand that the production of
an acceptable meat product is complex. As much as possible, the meat processor
should understand the mechanisms involved and be aware of potential positive
and negative effects (e.g., using meat with too much connective tissue is less
expensive, but can destabilize the gel matrix). Processors should also be aware of
the compatibility (e.g. similar gelation temperature) of added non-meat proteins
(e.g., soy, whey) and how they will interact with meat proteins.
b. Protein-water interactions: water retention within a lean cut of meat or a
ground/finely comminuted meat product is extremely important in creating a
product that is acceptable to the consumer (e.g., juicy, not too tough) and profitable
to the producer (e.g., reasonable yield). A lean meat chicken fillet portion contains
75% water. In some products added water (e.g., 10-50%; see recipes at the end of
the chapter) should also be held within the product.
c. Protein-fat interactions: meat proteins associations with oils/fats present in
fat cells, membranes, or that have been added to the product are very important
in providing a mechanism to keep the fat within the product. This is extremely
important for sensory and economic reasons.
The binding of meat proteins during cooking involves extensive protein-protein
interactions as a result of heat denaturation. Overall, a meat gel matrix can be
described in terms of a composite structure. Figure 13.5.1.a shows various
possibilities for the production of simple, mixed, filled, and filled-mixed gels
with different results in terms of compatibility or incompatibility (i.e., possible
enhancement or disruption when two proteins are used). For a mixed gel system a

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

synergistic effect can result from the cooperation of two proteins/components. As

will be discussed in the following comments, another component in the gel matrix
can be fat particles/globules in a meat emulsion (e.g., frankfurter). When present as
small particles fat can significantly increase the gels hardness.
Figure 13.5.1.a Possibilities for engineered structures of simple, mixed, filled and filled
mixed gels. From Aguilera and Kessler (1989).

Figure 13.5.1.a Possibilities for engineered structures of simple, mixed, filled and filled mixed gels.
Figure 13.5.1.b Effect of filler
type, from
size, Aguilera
and volume
fraction
filler () on the Youngs modulus
Redrawn
and Kessler
(1989).
(Ec) of particle-filled comminuted meat protein gels. (a,c) Rice bran wax;
strongly bound filler (insets show greater separation in the y-axis). (b,d) Glass
beads; weakly bound filler. Experimental data in (a) and (b) were fit to the
exactproduct
solutionisofcomposed
the van derofPoel
modelsoluble
(Eq. 2)and
and non-soluble
the Kerner model
(Eq. 5),
In general, a meat
various
proteins,
respectively. Fitted parameters are presented in the actual paper. The data
fat, water, andpresented
carbohydrates.
theytransformation
can form composite
materials
that(b),
in (c) andTogether
(d) is a ln-ln
of that shown
in (a) and
Note: due
panels
c and d denote
volumephenomena.
fraction of theAgel
m in to
strengthen therespectively.
polymetric matrix
volumetric
and/orthesurface
matrix. Particle size ranges : 1.0-1.4 mm, : 0.50-0.60 mm, : 0.15-0.21
non-food example
is rubber, a polymer that can be described as a filled gel system.
mm, : 0.045-0.090 mm, : < 0.50 mm. From Gravelle et al. (2015).

When the so called carbon-black particles are added, there is a great increase in the
mechanical moduli. In such a case both the size of the carbon black particles and
their strong surface adsorption properties
contribute to the gel strength. Aguilera
98
and Kessler (1989) have also shown this strengthening phenomenon in a mixed
dairy gel containing small fat globules with modified membranes.
Gravelle et al. (2015) have reported on the physical and mechanical properties of
particle-filled composite gels prepared from chicken breast meat proteins. They

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

examined the effects of solid filler with varying size (1.0-1.4, 0.50-0.60, 0.15-0.21,
0.045-0.090, and < 0.50 mm) and surface properties (hydrophobic rice bran wax
particles and hydrophilic glass beads). All composites were found to be stable up to
0.5 volume fraction () filler, based on post-gelation liquid loss, light microscopy
and cryo-SEM analyses. Both filler type and size were found to influence the
Youngs modulus and stress at 50% strain (Fig. 13.5.1.b). The recoverable
energy and post-compression height recovery were found to be predominantly
influenced by the filler volume fraction, and were less influenced by particle/gel
interactions. Interestingly, filler type and size range were observed to have no
effect on the cohesiveness of the composites, as this parameter was found to be
solely dependent on the volume fraction of the elastic filler present. The behavior
of the Youngs modulus was compared to that predicted by particle-reinforcement
theories proposed by van der Poel and Kerner, each with subsequent extensions
(Fig. 13.5.1 b).

Figure 13.5.2 Typical thermal curve of muscle with three major transition zones. Top figure

shows 13.5.1.b
a summary
of of
denaturation
peaks:
myosin
subunits;
(B)onsarcoplasmic
proteins and
Figure
Effect
filler type, size,
and (A)
volume
fraction
filler ()
the Youngs modulus
(Ec)
collagen
(C) actin.
As muscle
type
and environment
change
the shape
ofbound
the curve
of particle-filled
comminuted
meat
protein
gels. (a,c) Rice
bran wax;
strongly
filler changes
(insets
accordingly. Based on data from Barbut and Findlay (1989) and Wright et al. (1977).
show greater separation in the y-axis). (b,d) Glass beads; weakly bound filler. Experimental
data in (a) and (b) were fit to the exact solution of the van der Poel model and the Kerner
model, respectively. Fitted parameters are presented in the actual paper. The data presented in (c) and (d) is a ln-ln transformation of that shown in (a) and (b), respectively.
Note: m in panels c and d denote the volume fraction of the gel matrix. Particle size
ranges : 1.0-1.4 mm, : 0.50-0.60 mm, : 0.15-0.21 mm, :
0.045-0.090 mm, : < 0.50 mm. From Gravelle et al. (2015).

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Protein gelation can be defined as an aggregation of denatured protein molecules

with a certain degree of order, which results in the formation of a continuous
network. This can be described as a two-step process: denaturation and aggregation
(see review by Totosaus et al., 2002). Gelation can be induced by physical means
(e.g., heat, high pressure) as well as chemical means (e.g., salt ions, acid, urea, and
enzymes such as transglutaminase). Phillips et al. (1994) and later Totosaus et al.
(2002) classified the factors that affect gelation as extrinsic or intrinsic factors.
Extrinsic factors are the environmental conditions surrounding the proteins and
include:
a. p H affects the net charge of a protein. At its isoelectric point the
proteins charge is equal to zero but the further the environment is from
the isoelectric point, the more charged the protein becomes.
b. Protein concentration in general, the cross-linking of macromolecules
of an arbitrary initial size distribution is required for gelation and is
proportional to the protein concentration. There must also be a minimal
concentration of the protein itself, below which a continuous threedimensional structure cannot be formed. Gel strength and deformability
is highly dependent upon protein concentration.
c. Ionic strength affects water absorption, swelling, and solubility of
proteins as competitive linkages are created. Ionic strength has an effect
on the microstructure of the gel matrix; at low ionic strengths (<0.1 M)
of monovalent cations a fine-stranded matrix is formed, whereas at high
ionic strengths (>0.1 M) the matrix becomes mixed (Foegeding et al.,
1995).
d. Type of salt chloride monovalent ions (e.g., Li +, K +) form a fine
stranded matrix at ionic strengths less than 0.1 M. The salt concentration
required to affect gel microstructure depends on the salts position in the
Hofmeister series. Matrix formation also occurs when low concentrations
(1020 mM ) of divalent cations (e.g., Ca 2+, Mg 2+) of chloride salts are
present (Foegeding et al., 1995).
e. Temperature one of the most important factors because it is a driving
force behind protein unfolding. When the gelling temperature coefficient
is high, the first gelation step (denaturation) is completed faster than the
second (aggregation).
f. Pressure can affect the solgel transition of protein solutions. High
pressures (e.g., 200-500 MPa) modify the native volume of proteins,
which is composed of the volume of constituent atoms (compositional
volume), the volume of internal cavities, and a contribution due to
solvation (e.g., presence of water). The native structure governs the

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

biological activity of proteins and is a delicate balance between the

stabilizing and destabilizing interactions within the polypeptide chain
and the solvent.
Intrinsic factors are related to the protein itself and include:
a. A
 mino acid composition proteins that contain less than 31.5% mol
of hydrophobic residues (i.e., proline, leucine and tryptophan) form a
coagulum-type gel, whereas proteins with more than 31.5% hydrophobic
residues form a translucent gel. Some suggest that a more appropriate
parameter might be the ratio of the net charge to hydrophobicity rather
than hydrophobicity alone (Totosaus et al., 2002).
b. Electrostatic interactions are related to the net charge of the protein
molecule as influenced by attractive and repulsive forces. They affect
proteinprotein and proteinsolvent interactions (Phillips et al., 1994).
These electrostatic interactions are promoted by changes in ionic strength
and/or pH (extrinsic factors).
c. Hydrophobicity when non-polar amino acids are grouped together,
they form a hydrophobic nucleus surrounded by a polar residue layer
that remains in contact with the solvent (e.g., water). This plays an
important role in protein organization and should be taken into account
in any protein-folding consideration. Effective hydrophobicity refers
to the value representing the interactions between the proteins and
surrounding medium.
d. Molecular weight differences in the average molecular weight and the
hydrodynamic size of polypeptide species could be related to variations
in the formation of self-supporting gel network and gel strength. The
polypeptide critical molecular weight for gel formation is about 23 000
Da.
e. Disulphide bonds and thiol-disulphide interchanges increase the
apparent chain length of the polypeptide rather than acting as an initial
network stabilizer among polypeptide chains involved in protein
gelation. Disulphide bonds are not essential for gelation of proteins,
but their role in gelation is related to their ability to increase the average
molecular weight and hence the chain length.
Meat proteins denature at different temperatures (Fig. 13.5.2) and can then form
a gel structure. The figure shows that myosin and its subunits denature first (5458C), followed by sarcoplasmic proteins and collagen (65-67C), and then actin
as actomyosin and as fragments of F and G monomers denature last (71-83C;
Wright et al., 1977).

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

13-35

Figure 13.5.2 Typical thermal curve of muscle with three major transition zones. Figure
shows a summary of denaturation peaks: (A) myosin subunits; (B) sarcoplasmic
igure 13.5.3 Heat-induced
gel
of actomyosins
reconstitution
proteins
andstrength
collagen (C) actin.
As muscle type and environment
change the of different myosin-t
shape of the(5
curve
changes accordingly.
Based on data from
ctin ratios. The protein samples
mg/ml)
were dissolved
in aBarbut
0.6 and
M KCl solution containi
Findlay (1989) and Wright et al. (1977).

0 mM phosphate buffer, pH 6, and incubated for 20 min at temperatures varying from 20 to

00C. Gel strength was measured at each temperature. M - myosin alone; A - actin alone; A
ctomyosin. TheStudying
figuresthe
in textural
parenthesis
the mole
for myosin-to-ac
changesindicate
in a raw meat
systemration
during (corrected)
the cooking process
tio in respectiveand
systems.
Yasui
et al. (1980).
correlatingFrom
that data
with molecular
changes is useful in understanding protein
gelation. As well, following the rheological changes (i.e., small deformation testing)
that take place during gel formation has been useful to studying the sequence of
molecular interactions within a food/meat system. The latter studies have become
more feasible within the last few years as the market has seen the development of
high precision programmable rheometers. Prior to the development of scanning
rigidity monitors, samples had to be changed for each temperature point, which
resulted in time being a continuous independent variable. An example of
information from an early thermal scanning rigidity monitor is shown in Figure
13.5.3. Yasui et al. (1980) studied the effect of using pure myosin, pure actin and
their combinations at different ratios on forming a gel matrix. The researchers
chose these two proteins because they are the main proteins responsible for meat
binding (i.e., myofibrillar salt-soluble proteins). Overall, binding characteristics
of meat products prepared from isolated myofibrillar proteins provide a basic
understanding of the gelation process. Figure 13.5.3 shows that myosin by itself
will start forming a gel at 45C. The authors indicated that this gel structure
determines the binding quality in meat products and that binding strength bears a

re 13.5.3 Heat-induced gel strength of actomyosins reconstitution of different myosin-toratios. The protein samples (5 mg/ml) were dissolved in a 0.6 M KCl solution containing
13-36 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
mM phosphate buffer, pH 6, and incubated for 20 min at temperatures varying from 20 to
C. Gel strength was measured at each temperature. M - myosin alone; A - actin alone; AM
relationship
to the amount
of myosin
liberated
the (corrected)
myofibrils. Thefor
datamyosin-to-actin
myosin. Theclose
figures
in parenthesis
indicate
the
mole from
ration
also
show
that
actin
by
itself
does
not
form
a
gel
under
these
conditions.
in respective systems. From Yasui et al. (1980).

Figure 13.5.3 Heat-induced gel strength of actomyosins reconstitution of different

myosin-to-actin ratios. The protein samples (5 mg/ml) were dissolved in a 0.6 M
100 buffer, pH 6, and incubated for 20
KCl solution containing 20 mM phosphate
min at temperatures varying from 20 to 70C. Gel strength was measured at
each temperature. M - myosin alone; A - actin alone; AM - actomyosin.
The figures in parenthesis indicate the mole ration (corrected) for
myosin-to-actin ratio in respective systems.
From Yasui et al. (1980).

However, in the presence of myosin, a synergistic effect between actin and myosin
is observed. This is because actin, in the presence of other cross-linking proteins,
can enhance gel structure. The effect of the relationship between myosin and actin
concentration on rigidity is demonstrated in Figure 13.5.3. This can be used to also
illustrate the effect of a two protein system that produces a synergistic mixed gel
(see also Figure 13.5.1; second row on the right side). Maximum gel rigidity was
obtained when the myosin to actin mole ratio was 2.7, (a weight ratio of myosin
to actin of about 15:1). Increasing the portion of myosin beyond this point caused

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

a decrease in gel strength. Yasui et al. (1980) suggested that the synergistic effect
is either ionic strength dependent or is determined by the state of myosin per se
at different ionic conditions. At <40C it can also be observed that actin exhibits
some resistance to gel, probably due to its thixotropic nature. However, upon
heating, the gel collapsed into a compact string or bead-like structure (scanning
electron microscopy pictures are not provided here). Isolated myosin fragments
were shown to affect gel characteristics differently. Intact myosin monomers
produced the strongest gels, followed by myosin rods and the S-1 fragment (see
Chapter 3 for myosin structure). The S-1 fragments produced gels with low
water-retaining ability. As mentioned above, the differences were also evaluated
by electron microscopy. Myosin rods produced an extended three-dimensional
network system, while the S-1 fragment formed a bead-like aggregate structure
upon heating. Combining the myosin rods and S-1 fragments did not produce high
gel strength as was observed for the intact myosin molecules. This indicates that,
once cleaved, the fragmented myosin did not have the same capabilities to form
a gel matrix.
Table 13.5.1 Effect of sodium chloride (NaCl), tripolyphosphate (TPP) and heating temperature on gel
strength and amount of extractable protein. Adapted from Barbut et al. (1996).

Penetration Force (N)

Extractable Proteins (mg/mL)

Treatment Temp. 2.5% NaCl 1.5% NaCl + 0.4 TPP 2.5% NaCl 1.5% NaCla + 0.4 TPP
a

20 C

30.8f

25.3f

1.62ab

1.72a

40 C

43.3ef

40.1ef

1.58b

1.60b

50 C

60.0

60.5

1.38

1.50b

55 C

189.0d

194.1d

1.18de

1.21d

60 C

356.6b

287.5c

1.07e

1.08e

70 C

475.8

373.3

0.37

0.40f

Both the 2.5% NaCl and 1.5% Nacl + TPP were formulated with the same ionic strength
(IS=0.42).
Means followed by the same letter, within each test category, are not significantly different at
95% level.
a

Structure development during heating of a commercial type meat batter can show
the direct relationship between the meat protein system (i.e., containing many
different proteins) and structure formation. Table 13.5.1 shows gel strength values
(measured via penetration force) for a chicken meat batter heated from 20-70C
and the available protein extracted at each temperature. As temperature increased,
more protein-protein interactions occurred and penetration force values increased

13-37

13-38

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

from 30 to 475N. At the same time the amount of available proteins decreased
because progressively more were bound together to form the gel structure. The
microstructure of the gels at the different heating temperatures is shown in Figure
13.5.4. As other researchers have shown, the basic gel structure is formed when
the meat batter is prepared (at low temperature) and is solidified during heating
through the creation of covalent and disulfide bonds.
In the study, Barbut et al. (1996) followed the gelation of finely comminuted
turkey meat (mechanically deboned) prepared with 13% fat and 2.5% NaCl and
in reduced sodium (1.5% NaCl plus 0.41% tripolyphosphate) products. From
20-70C, the process was studied by evaluating gel strength, extracting available
proteins, and microscopy. Gel strength, as measured by the penetration test,
tripled as temperature increased from 50 to 55C and then doubled again when
temperature was raised to 60C (Table 13.5.1). The amount of extractable proteins
continuously decreased as heating temperature was raised. The decrease in the
amount of soluble protein indicates that they were taken up into the gel structure
(Asghar et al., 1985). Cryo-scanning electron micrographs (Fig. 13.5.4) revealed
that adding phosphate to the low sodium meat batter resulted in a protein matrix
with larger pores than the 2.5% NaCl treatment (both treatments were formulated
with equal ionic strength). The overall differences in microstructure of the two
treatments remained the same during cooking (micrographs taken every 10C).
Development of a rigid gel structure during cooking was characterized by some
contraction of protein strands within the matrix. Closer examination of the data
revealed that the first major increase in rigidity was observed when the temperature
was increased from 20 to 40C. This corresponded to an initial small reduction
in the amount of soluble protein (Table 13.5.1). A further increase was observed
from 40 to 50C and then a major increase was observed when temperature was
increased from 50 to 55C. The latter actually resulted in tripling gel strength values,
which could be related to myosin denaturation and its transformation into a rigid
structure. A major decrease in the amount of soluble protein at this range has been
previously reported by Yasui et al. (1980). They showed that, at this temperature,
interactions between actin and myosin were responsible for the rigid structure
development (i.e., actin by itself will not gel, but with myosin a synergistic effect
can be observed; Fig. 13.5.3). The values for gel strength were further increased
when the temperature was increased from 55 to 60C. Temperature increases in
this range have been shown to be critical in the thermal gelation of meat systems.
The amount of extractable protein significantly decreased above 50C in both the
2.5% salt and reduced salt treatments. This corresponded to the large increase
in gel strength. Contrast analysis showed that the overall means for extractable
protein were significantly different between the 2.5% NaCl and 1.5% NaCl + TPP
treatments across all temperatures.

igure 13.5.4 Cryo scanning electron micrographs of meat batters containing 2.5% NaCl (
strength = 0.42), heated to (A,B) 20 C; (C,D) 40 C; (E,F) 55 C; and (G,H
C. Micrographs on the left are at low magnification (bar = 15 m), on the
at higher magnification (bar = 3 m). Part G shows a fat globule entra
SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT 13-39
within the proteinTHE
matrix.
From Barbut et al. (1996). With permission.

Figure 13.5.4 Cryo scanning electron micrographs of meat batters containing

2.5% NaCl (ionic strength = 0.42), heated to (A,B) 20C; (C,D) 40C; (E,F)
55C; and (G,H) 70C. Micrographs on the left are at low magnification
(bar = 15 m), on the right at higher magnification (bar = 3 m).
Part G shows a fat globule entrapped within the protein matrix.
From Barbut et al. (1996). With permission.

101

13-40

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

Micrographs taken during different stages of cooking (Figure 13.5.4) showed a

progressive change in the batters microstructures. The first micrograph shows an
organized gel structure prior to heating. This kind of structure has been previously
observed by other groups. On heating to 40C, the protein strands became
thicker while the pore size stayed the same. A further increase to 55C resulted
in an increased number of connections among protein strands. The junction
zones between strands also became thicker. In addition, thin protein strands were
visible among the thick strands. This also increased the density of the protein
matrix. These changes corresponded to the large increases in gel strength at this
temperature (Table 13.5.1). Further heating to 70C resulted in a denser protein
matrix, which resulted from the formation of additional protein strands concurrent
with a reduction in pore sizes. With the help of a scanning electron microscope,
Wang and Smith (1992) reported that a salt-soluble protein solution (30 mg/mL,
at pH 6.5) heated to 55C produced aggregates composed of globular structures
connected by strands. When the temperature was increased to 65C the strands
became thicker (125 vs. 300 nm). Additional heating to 80C caused a reduction in
strand size, but the structure remained ordered. Since they only started monitoring
the structure at 55C, comparison with a structure at a pre-denaturation temperature
(20C) is not possible.
A meat products gel formation is strongly affected by use of additives such as
salts and pH modifiers. As already shown, salt concentration plays an important
role in the amount of proteins extracted and later in binding. This is observed in the
reduction of salt from 2.5 to 1.5% in commercial-type poultry meat batters (14%
protein and 18% fat), which resulted in a substantially lower final rigidity value
(12.2 vs. 4.9 kPa, respectively; Figure 13.5.5) as observed by small deformation
testing (using a programmable rheometer). Differences were also observed in the
development of the modulus of rigidity (G) after the initial protein coagulation
started at around 55C. In both batters, a small but linear increase was observed up
to 55C, indicating that the protein matrix was continuously developing. When the
temperature reached the myosin denaturation zone at around 55C, a rapid increase
in G was observed. However, when the temperature reached the collagen and
sarcoplasmic protein coagulation zone at around 63C, there was a sharp decline in
the 1.5% NaCl treatments curve, whereas there was a steady G value in the 2.5%
NaCl treatment. The sharp rigidity decline might indicate a structural breakdown
in the reduced salt meat batter. The general gelation pattern for the 2.5% NaCl,
seen in the figure, is similar to the one reported by Montejano et al. (1984) for hand
deboned turkey meat containing 2.5% NaCl. Overall, the rapid steady increase in
G from 56 to 70C (Fig. 13.5.5) indicates the formation of a stable, elastic, and
self-supporting matrix structure typical of heat-induced protein gels. With further
increase in temperature, there was no increase in G value, up to 80C. When

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

polyphosphates were added to the reduced salt (1.5% NaCl) meat batters, structure
weakening around 63C was eliminated; however, gelation patterns were different
depending on the phosphate. Adding 0.5% sodium acid pyrophosphate (SAPP)
resulted in the closest match to the rigidity modulus development pattern seen in
the 2.5% NaCl treatment. It is interesting to note that, in another study, a taste
panel also rated reduced-salt poultry frankfurters containing SAPP as having the
most closely matched texture to frankfurters containing 2.5% NaCl. The curve
of the TPP treatment shows that structure formation followed the pattern of the
1.5% NaCl treatment up to 64C, but unlike the 1.5% NaCl, it did not weaken
and stayed at a constant value (G=8.9) up to 80C. Addition of SAPP resulted in
further increases of the G values as temperature was raised above 64C. Evidently,
the change from a viscous to an elastic structure in a meat batter happens almost
instantaneously; additional heating further increases the rigidity modulus, but only
up to a certain point. It is important to note that salt and phosphate addition already
affect raw meat batter viscosity during preparation. This can be seen in Figure
13.5.5 as the differences in G at 20C. The authors also investigated the effects
of applying higher shear rates to the raw meat batters (Figure 13.5.6) in order to
determine viscosity and yield stress values. Both are important when selecting
pumps
to move large volumes of meat in a processing plant.
Figure 13.5.5 Shear-rigidity modulus profile of reduced salt meat batters containing various
phosphates during heating. (1 = 2.5% NaCl; 2 = 1.5% NaCl; 3 = 1.5% NaCl +
0.5% TPP; 4=1.5% NaCl + HMP; 5 = 1.5% NaCl + 0.5% SAPP). From Barbut
and Mittal (1989). With permission.

Figure 13.5.5 Shear-rigidity modulus profile of regular and reduced salt meat batters containing various
phosphates during heating. (1 = 2.5% NaCl; 2 = 1.5% NaCl; 3 = 1.5% NaCl + 0.5% TPP; 4=1.5%
NaCl + HMP; 5 = 1.5% NaCl + 0.5% SAPP). From Barbut and Mittal (1989). With permission.

13-41

Figure 13.5.6 Relationships between shear stress and shear rate for reduced salt raw meat
batters with two phosphates (1 = 2.5% NaCl; 2 = 1.5% NaCl; 3 = 1.5% NaCl +
0.5%
4=1.5%
HMP; 5 = 1.5% NaCl + 0.5% SAPP). From Barbut
13-42 CHAPTER
13:TPP;
PRINCIPLES
OF NaCl
MEAT +
PROCESSING
and Mittal (1989). With permission.

13.5.6ofRelationships
stress and shear
for regular
reduced salt raw meat
Figure 13.6.1Figure
Effect
choppingbetween
time shear
on cooking
lossrate(ml)
fromandcomminuted
beef meat batter.
batters with three phosphates (1 = 2.5% NaCl; 2 = 1.5% NaCl; 3 = 1.5% NaCl + 0.5% TPP;
Temperature
values
(C)
at
each
time
are
listed
above
bars.
From
4=1.5% NaCl + HMP; 5 = 1.5% NaCl + 0.5% SAPP). From Barbut and Mittal (1989). Barbut (1998).
With permission.

The following short discussion is not directly related to meat protein gelation, but
is included here to explain flow behavior of raw meat batters and to help the reader
understand the forces involved. Figure 13.5.6 shows the relationship between
shear rate and shear stress for the same treatments shown in the previous figure.
The relationship is nonlinear and displays Bingham pseudo plastic behavior. The
shearing rate tends to increase faster than the shearing stress; i.e., also showing a
certain yield value. It was suggested that particles (e.g., muscle/connective tissue
fibers) in a meat batter are initially randomly oriented and become increasingly
more aligned as shear is applied. The contribution of particle interactions to the
apparent batter viscosity was reported to decrease when shearing stress increased.
All meat batters required the application of a certain shearing force before
any noticeable flow took place. On a molecular level, Bingham materials are
envisioned as a three-dimensional network at rest. Forces applied to this network
can be resisted up to a certain point, but then the network breaks down and the
flow becomes essentially pseudo plastic. Both NaCl treatments had the same pH
103
(6.35), TPP slightly increased the pH to
6.45, and SAPP addition decreased the
pH to 6.25. These relatively small pH differences are not believed to play a major
role in the viscosity differences observed. Rather, the type and concentration of
the salt ions involved seem to be most influential. The general power law model

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

(Herschel-Bulkley) with yield stress was used to fit the data. The 95% confidence
interval for yield stress (To) was 291 to 580 Pa, for the consistency coefficient (b)
was -11 to 191.0 Pa.sn, and for the flow behavior index (n) was 0.50 to 0.82. The
To for the emulsion containing 1.5 % NaCl + SAPP was significantly lower than
those of the other treatments. Thus, SAPP decreased the Bingham behavior of the
meat batter. Similarly, the To value for the control (2.5% NaC1) was significantly
higher than those of the other treatments. Thus, low NaCl (1.5%) reduced the To
value. The b value of the meat batters with 1.5% NaCl was significantly higher
than those of the 2.5% NaCl or 1.5% NaCl + phosphate batters. The n value was
between 0 and 1, indicating pseudoplasticity. Similarly, the n value of meat batters
containing 1.5% NaCl was significantly lower than those of other treatments.
According to previous work, more stable formulations tended to have higher b
values, lower n values, and larger values for yield stress. As indicated above, these
values and the relationships between them are important for equipment selection
in a meat processing plant.
Returning to the effect of pH on meat protein gelation, it is important to note that
pH can affect gel characteristics (hard, soft) and certain pH values can actually
prevent gel formation. Xiong and Brekke (1991) reported that the optimum pH
for gelation of chicken muscle in 0.6 M NaCl (or KCL) was about 6.0 for breast
myofibrils and 5.5 for leg meat myofibrils. Wang et al. (1990) studied the effect
of pH on the gelation (30 to 80C) of 3% salt soluble proteins (SSPs) extracted
from chicken breast. Table 13.5.2 shows the storage modulus (G, the elastic
element) and the loss modulus (G, the viscous element). Salt soluble proteins at
all conditions exhibited higher G than G throughout the heating process which
indicated the elastic nature of SSPs during the sol-to-gel transformation. The pH
5.5 and 6.5 treatments show the highest final G values, indicating the strong
effect of pH on gel formation. At the end point, the G of SSPs at pH 4.5 was
not significantly different from that at pH 7.5. Salt soluble proteins at pH 5.5 and
6.5 tended to have a higher G at the end point, which indicated the formation of
a more elastic gel matrix and more cross-linking between the protein molecules.
Protein gels at pH 5.5 exhibited the highest G at the end point, which indicated the
formation of a more viscous matrix.
The increase in G was thought to be due to the partial unfolding of protein structure,
which caused an initial increase in the viscous characteristics of the SSPs. The
subsequent increase in G, which indicated an increase in the elastic or solid nature
of the material, indicated that the SSPs were cross-linking to form an elastic gel.
An examination of the tangent delta (G/G) showed the relative viscous:elastic
properties of the material (i.e., in an elastic solid the tangent delta is zero and for a
viscous fluid it is infinite). For all pH levels, there were no significant differences in

13-43

13-44

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

the tangent delta values for the SSP preparations at the initial point prior to heating.
No second peak was observed in SSPs at pH 4.5, which corresponded to the lack
of transitions in both G and G. Similarly, no significant differences in tangent
delta were observed at the first and second peaks in SSPs at 5.5, 6.5, and 7.5. At the
end point, protein gels at pH 4.5 showed higher viscous properties than at pH 6.5
and 7.5. This indicated that gels at pH 6.5 and 7.5 formed a more elastic network.
Table 13.5.2 Effect of pH on the storage modulus (G), loss moduli (G), and loss tangent
(tangent delta) of 3% chicken breast salt-soluble proteins heated from 30 to 80C at
1C/min and with 0.6 M NaCl. Adapted from Wang et al. (1990).

Parameters

pH
4.5

5.5

6.5

7.5

34.2b

141.6ab

196.0a

Storage modulus (Pa)

Initial point
Peak maximum

187.0a

1,000.3

1,190.7

614.7a

216.3b

1,725.7a

1,286.0a

575.9b

Initial point

6.8b

32.8ab

38.8a

31.4ab

Peak maximum

End point

Loss modulus (Pa)

116.6a

128.6a

82.8a

123.1

30.6

24.9b

30

30

30

30

0.22a

0.23a

0.20a

0.17a

37b

34c

47a

49a

0.24a

0.20a

0.19a

0.17a

Temperature, C

53b

57a

58a

Tangent delta

0.15a

0.12a

0.15a

End point

24.4

Loss tangent (temp;C)

Initial point
Temperature, C
Tangent delta
First peak
Temperature, C
Tangent delta
Second Peak

End point
Temperature, C
Tangent delta

80

80

80

80

0.12a

0.07ab

0.02b

0.04b

Means within the same row with no common superscripts are significantly
different (P < 0.05), n=3.
a,b

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

The authors also reported the complex modulus (G*, the amount of force required
to deform a sample). There were no major transitions at pH 4.5 when SSP
solutions were heated. This was because the proteins coagulated at this low pH
and did not from a gel network. This is typical of protein systems at pH levels
close to their isoelectric point (i.e., where the net charge on the proteins is close
to zero). The isoelectric point of actomyosin is around 5.0 and at this point an
electrostatic attraction between the molecules can be seen. Electrostatic attraction
minimizes protein unfolding during heating and prevents gel formation. At pH
5.5, 6.5 and 7.5, G* increased after the first transition at 35-47C. Afterwards,
it peaked, then decreased on further heating to the third transition around 5460C, and then increased again until 80C. The first transition, which led to the
development of gel elasticity, was attributed to unfolding in the tail portion of the
myosin molecule. The G* values at the end of cooking were significantly higher
at pH 5.5 and 6.5 than at pH 4.5 and 7.5 (P < 0.05). The authors mentioned that
the thermal transitions, graphed as differential plots of the complex modulus
against temperature (dG*/dT versus T; not shown here), were pH-dependent
throughout the heating process. The differential plot illustrated the rate of G*
change during heating and provided additional information on how pH affects
protein conformational changes during sol-to-gel transition. No rate changes were
observed for the SSPs kept at pH 4.5 during the heating process. The first transition
of the pH 6.5 and 7.5 treatments occurred at temperatures above 45C. At pH 5.5
even the third transition had occurred before any changes were observed in the
higher pH treatments. However, further transitions at pH 5.5 were similar to those
of the higher pH treatments; temperature differences between the first and sixth
transition were 18C, 14C, and 12C for pH 5.5, 6.5, and 7.5, respectively. The
pH 6.5 and 7.5 treatments showed almost identical transition temperatures and
rheological transitions, which suggested similar changes in protein conformation
during the gelation process. These results also demonstrate that pH influences the
unfolding and aggregation of native protein molecules during heating and results
in different gel properties.
Overall, the data presented above indicate that pH should be monitored and
adjusted (if needed) to obtain consistent meat product quality. The texture and
water binding capacity of meat products can be manipulated by adjusting the pH
and by adding various salts and binders to optimize meat formulations.

13-45

13-46

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

13.6 Fat Binding and Emulsification

Meat products that are finely comminuted, sometimes referred to as meat
emulsions (e.g., bologna and frankfurters), are basically composed of protein,
fat, water, and salt. Products in this category are produced from different meat
and non-meat ingredients (e.g., salt, soy proteins, starch) all around the world. In
North America their estimated market share is over 35%. Producing high quality
comminuted products is an ongoing challenge to processors who deal with a large
selection of raw materials whose prices fluctuate daily (see Section 13.3 on Least
Cost Formulation). The basic structure of a comminuted product is shown in
Figure 13.5.4 where fat globules are dispersed in a protein gel matrix. The matrix
has a structure that can be described as a sponge where there are lots of small
spaces that confine water. The products shown in the figure have about 60% water,
20% fat, and 14% protein. The protein matrix represents the main structure that
forms the product/holds the water and fat components. It consists of the salt soluble
proteins and small pieces of intact muscle and collagen fibers. All ingredients are
comminuted either in a bowl chopper or an emulsion-mill (see Chapter 10) in
order to reduce the lean meat particles, open their structure, and extract the salt
soluble proteins. This process also reduces fat particle sizes to increase their
stability (see later discussion) and obtain a homogeneous mass. However, as the
fat particle/globule size can be above 20m, these products cannot be classified
as true emulsions and the forces that govern a true emulsion cannot explain their
entire stability. In any case, the challenge to the meat processor is to produce a
stable meat product that can withstand the cooking process without fat and water
separation (Acton et al., 1983; Barbut et al., 1996).
A good understanding of the mechanism(s) responsible for stabilizing/binding
the fat within the product is essential to the meat processor because most
comminuted products contain 15-40% fat that is held by a smaller amount of
protein. As the proteins are also needed to retain water, they should be of high
quality. Studying the mechanisms affecting meat batter stability is important
because an emulsion breakdown can be very costly especially in high volume
processing plants. In addition, understanding the relationship between meat
batter stability and processing equipment can help the processor select the right
equipment (i.e., different machines are available) and utilize the best ingredients
for a specific product. It should be noted that this is not an easy task as there are
many binders available on the market. Understanding meat batter stability also
helps the processor effectively use least-cost-formulation programs and respond to
consumer demands (e.g., reduced fat/salt meat products which cannot actually be
prepared by a straight fat/salt reduction).

batters with two phosphates (1 = 2.5% NaCl; 2 = 1.5% NaCl; 3 = 1.5% NaCl +
0.5% TPP; 4=1.5% NaCl + HMP; 5 = 1.5% NaCl + 0.5% SAPP). From Barbut
and Mittal (1989). With permission.
THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

13-47

From a practical standpoint, one of the major reasons for studying meat batter
stabilization is that during chopping the processor cannot see/detect any warning
signs indicative of a later emulsion breakdown (a term referring to fat separation
during cooking). This point is illustrated in Figure 13.6.1, which shows the effect of
chopping time on meat batter stability. As chopping time increases, more proteins
are extracted, fat particle size is reduced, and less liquid and fat is separated from
the product. This is known to most meat processors; however, just looking at the
raw meat batter usually does not provide any hint to the amount of liquid/fat losses
that can be expected during cooking. This is a constant challenge because meat
block formulations can change daily depending on the availability of raw materials,
cost, etc. Therefore, meat processors usually use pretty high safety margins (e.g.,
more proteins and longer chopping time; both of which increase processing costs)
to protect themselves against emulsion breakdown incidents. The data in Figure
13.6.1 are used to illustrate the point that understanding the process should benefit
the processor. This material was also used in the development of an automated
fiber-optic
to monitor
Figure 13.6.1
Effect system
of chopping
timethe
onemulsification
cooking lossprocess.
(ml) from comminuted beef meat batter.
Temperature values (C) at each time are listed above bars. From Barbut (1998).

103 loss (ml) from comminuted beef meat batter.

Figure 13.6.1 Effect of chopping time on cooking
Temperature values (C) at each time are listed above bars. From Barbut (1998).

There is still debate in the scientific community as to the correct definition of finely
comminuted meat products: meat emulsion or meat batter? The controversy arises
from the interpretation of the mechanisms responsible for holding the fat within the

13-48

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

product. Figure 13.5.4 shows the microstructure of finely comminuted products

Figure where
13.6.2the SEM
-protein
envelope
aroundwithin
the afatwater
globule.
protein film
small fat
globules
are dispersed
solubleInterfacial
protein matrix.
surrounding the fat globules. The film is responsible for stabilizing the fat.
Borchert et(p45).
al. (1967)
were among
first to showofthe
Scanning
electronthemicrographs
fatpresence
globulesofinanainterfacial
cooked, low salt
protein film
(IPF)
surrounding
the
fat
globules
(Fig.
13.6.2)
and suggested
thatadequate
the
poultry meat batter formulated with 1.5% NaCl (A),
and with an
salt
film is responsible
stabilizing
level of for
2.0%
NaCl the
(B).fat.Bars = 10 m. From Barbut (1988). With
permission.

Figure 13.6.2 Scanning electron micrographs of fat globules with

surrounding interfacial protein104
film in a cooked, low salt poultry
meat batter formulated with 1.5% NaCl (top), and with an
adequate salt level of 2.5% NaCl (bottom).
Bars = 10 m. From Barbut (1988).
With permission.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

The myofibrillar proteins, which have hydrophilic and hydrophobic sites, arrange
themselves in such a way that they reduce surface tension and forces responsible
for fat globule coalescence and prevent separation. The same phenomenon is
observed in homogenizing milk, where small fat globules are covered with the milk
protein caseinate (to help reduce fat separation/creaming). If finely comminuted
meat products hold fat using this mechanism, they would be considered true
emulsions. However, other researchers have suggested that the protein matrix is
the main factor responsible for physically entrapping the fat globules (Lee, 1985).
According to the physical entrapment theory, the viscous protein matrix restricts
fat globule movement, hence coalescence. This mechanism would suggest that
finely comminuted products are behaving as meat batters. In any case, the whole
issue of which mechanism is more important is not so simple, since numerous
changes take place during the production of products such as frankfurters/bologna.
During the initial stage of chopping, a flowable product, with a toothpaste-like
texture, is formed and the meat batter can be easily pumped (note: care should be
taken to limit shear forces, which can cause fat globules to coalesce and destabilize
the meat batter). The structure formed in the raw stage is shown in Figure 13.5.4.A.
Later, during the initial heating process (20-40C), the fat starts to melt and is
present in a liquid form. Myofibrillar protein denaturation and gelation starts at a
higher temperature (around 50C; see Fig. 13.5.4.E). At that point, the melted fat
starts to expand, collagen starts to be transformed into gelatin (i.e., liquid form),
and the salt soluble proteins form a gel. The texture of the product at the end of
the cooking process (70C) is semi-rigid and does not flow anymore because the
salt soluble proteins have been denatured. As indicated above, there is continuing
debate about which mechanism is more important but today there is support for
the notion that fat stabilization is a combination of the ability of proteins to form an
interfacial film, as well as the formation of a gel matrix which physically restricts
the movement of fat globules prior to cooking (Youssef and Barbut, 2011).
The thickness of the interfacial protein film, its elasticity, complete or partial
coverage of the fat globules, and weak spots along the film have been discussed
by various researchers (Borchert et al., 1967; Jones and Mandigo, 1982; Barbut,
1999; Ramirez-Suarez and Xiong, 2003). The authors discussed the formation
of a relatively thin, flexible protein film around fat globules, and emphasized
the importance of pore formation as a pressure release mechanism during the
cooking stage (i.e., when fat is heated and expands). Some have experimentally
modified the thickness of the protein film by varying chopping procedures. Overall,
it appears that the formation of a relatively thin and flexible protein film provides
the best stability, whereas a thick inflexible film results in large ruptured holes
during cooking. Figure 13.6.3 illustrates the microstructure of stable and unstable
finely comminuted meat products. In the stable product, fat globules are confined
within a distinct globular structure. In the unstable product (in this figure caused

13-49

13-50

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

by Tween 80 addition) they are distorted in shape and start to form fat channels.
Destabilization can also be caused by decreasing the salt level (e.g., 2.5 to 1.5%),
which is associated with lower protein extractability and subsequently higher fat
and moisture losses during cooking (Acton et al., 1983). The combined loss of
fat and moisture from finely comminuted meat products has been mentioned by
Schmidt (1984), who observed that fat exudation usually follows moisture loss.
Schmidt postulated that the formation of channels through the meat batter was
important to allow some moisture and fat losses. Figure 13.6.2 shows a fat globule
that has lost some of its fat, during cooking, due to salt reduction in the raw meat
formulation (2.5 to 1.5%). The scanning electron micrograph reveals a protein
envelope around the fat globule. When too much fat is exuded from the globule, the
protein envelope shrinks and indentations plus small exudative holes are seen on
the surface. When salt is increased, little or no fat is lost and round globules can be
seen. Whiting (1987) has also reported that 1.5% salt is a threshold in frankfurters,
as determined by the amount of fat and water released during cooking. It should be
mentioned that the amount of salt required to produce a stable batter also depends
on factors such as the amount of fat and protein and their quality.
The connection between the texture of the meat protein matrix and the size of the fat
globules can be seen in Table 13.6.1. Youssef et al. (2011) indicated that increasing
the meat protein level (915%) increased the hardness of finely comminuted meat
batters prepared with beef and animal fat or canola oil (CO). Overall, a higher
protein level formed a denser protein network (microstructure not shown here),
which had increased resistance to compression. The meat emulsions prepared with
animal fat showed lower fracturability and hardness values compared to the CO
emulsions. This is most probably due to the higher number of small CO globules
present in a given volume (similar results were also shown for milk protein gels).
In a previous experiment the authors showed that fat globule size was reduced
from 6627 to 121 m2 when beef fat was substituted with CO at 8% protein. The
same idea can also be seen here in Figure 13.6.3. Overall, the presence of smaller
fat globules and higher protein increase resistance to compression. This is in line
with the composite gels discussed at the beginning of the section.
The treatments with Tween 80 + animal fat resulted in higher fat and moisture
losses than the CO-Tween 80 or animal fat treatments (Table 13.6.1). This resulted
in an increased protein concentration and higher hardness values in the cooked
products; i.e. they formed denser protein matrixes.

15M + CO-T80

12

0.81

31.33
0.85

69.78
0.76

46.27

31.64 0.61a

27.98 1.02
de

7.87 0.47j

30.84 0.55ab

a-p

71.91bc

0.83

0.80

33.81
g

0.59

0.78

11.73k

80.16a

32.60g

0.74

0.60

12.48

30.75 0.68abc

10.54 0.33

0.84

63.59e

27.71h

29.06 0.50cd

25.29 0.66f

0.71

0.57

13.78

10.31 0.44

0.78

73.69b

31.30 0.44a

29.01 0.82

0.71

cd

20.42i

19.38 0.68g

29.27 0.35

0.81

bcd

66.35d

31.54 0.48a

29.53 0.28

0.79

61.50e

0.77

0.68

Springiness
(cm)

bcd

33.99g

17.13j

Hardness
(N)

29.99 0.39abc

26.98 0.38e

16.57 0.24h

Fracturability
(N)

Means within a column no common superscript are significantly different (P < 0.05).

15P* + CO-SC

12M + CO-T80

11

18

9M + CO-T80

10

12P* + CO-SC

15M + BF-T80

17

12M + BF-T80

9P* + CO-SC

9M + BF-T80

16

15M + CO

15P* + BF-SC

12M + CO

15

9M + CO

9P* + BF-SC

15M + BF

12P* + BF-SC

12M + BF

14

9M + BF

13

Treatment
Identification

Treatment

0.41

0.31

0.26

0.33

0.24

0.21

0.40

0.26

0.23

0.37

0.31

0.25

0.43

0.46

0.34

0.28

0.26

0.22

Cohesiveness
(ratio)

1.57 0.06

24.47 0.66a

8.38 0.53

1.79 0.18i

20.63 0.85b

5.78 0.21fg

21.36 0.33b

5.11 0.21g

1.80 0.11

21.26 0.69b

10.90 0.70

3.62 0.20h

25.50 0.67

24.72 0.55a

8.62 0.25
e

13.60 0.36c

6.80 0.19f

2.56 0.10hi

Chewiness
(n cm)

31.23 0.59a

10.73 0.62f

3.15 0.19j

29.48 0.79c

10.48 0.21gh

3.04 0.07j

26.45 0.41c

7.20 0.21h

3.31 0.12j

27.26 0.45b

14.34 0.90e

5.10 0.26i

30.00 0.75a

30.52 0.60a

10.65 0.28f

17.22 0.28d

8.83 0.17g

3.76 0.14j

Gumminess
(N)

Table 13.6.1 Effects of meat protein level and fat type on texture profile analysis parameters of cooked finely comminuted meat batters Meat batters were produced with 9, 12 or
15% protein, with either beef fat (BF), or canola oil (CO; all treatments contain 25% fat or oil). An emulsifier (Tween 80 indicated as T-80) was added to one set of products,
and sodium caseinate (SC) was used to replace 2% of the meat proteins in another set. M=meat protein; P*=indicates total protein when 2% SC was used.
Data adapted from Youssef et al. (2011).

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13-52

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

The CO-T80 batters had lower hardness values than batters prepared with CO,
possibly related to the formation of an incoherent protein matrix (Fig. 13.6.3).
When Tween 80 surrounds fat globules it can interfere with the interaction of the
interfacial protein film with the actual protein matrix. Theno and Schmidt (1978)
observed that fat particles coated with proteinaceous material could cross link with
the protein matrix and therefore stabilize frankfurters. It was suggested that the
physical
binding
fat might be
the result
proteinprotein
interactions
between
Figure 13.6.3
Lightofmicrographs
of meat
battersof
with
pre-emulsified fat/oil
with T-80.
Fat
globule
(FG);
Meat
protein
(MP);
canola
oil
(CO)
made
with
beef
fat
(BF);
prethe interfacial protein film and the matrix proteins.
emulsified with Tween 80 (T80) or with the addition of sodium caseinate (SC).
Bar = 200m. From Youssef et al. (2011). With permission.

Figure 13.6.3 Light micrographs of meat batters with pre-emulsified fat/oil with T-80. Fat globule
(FG); meat protein (MP); made with canola oil (CO), or beef fat (BF); pre-emulsified with Tween
80 (T80) or with the addition of sodium caseinate (SC). Bar = 200m.
From Youssef et al. (2011). With permission.

The use of sodium caseinate (SC), which is used by the meat industry to stabilize
fat, lowered fracture and hardness values at the 9% protein level (hardness of 12.48
vs. 17.13 N with and without SC, respectively) when 2% of meat proteins were
replaced with SC. This was because SC cannot form a heat induced gel (at 72C)
and the amount of meat protein (7%) was insufficient to produce a hard texture.
However, when 12% protein and 2% SC was used, the texture was comparable to
the 12% meat protein. At 15% protein105
(13% meat protein and 2% SC), hardness
surpassed the control (15% meat proteins). CO-SC batters showed reduction in
hardness values at the 9% and 12% protein levels compared to the comparable CO
treatments. This change in hardness indicates that incorporation of pre-emulsified
fat/oil with SC can significantly modify the textural properties of meat batters.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Replacing beef fat with CO also increased springiness and cohesiveness; this
is possibly related to the size and distribution of the fat globules (Table 13.6.1),
which agrees with previously published data.
Overall, the control beef fat treatment revealed a typical meat batter in which
fat globules are embedded within a homogenous protein matrix (Fig. 13.6.3).
Microstructure was affected by the type of fat/oil and protein content. In all
treatments, increasing protein resulted in the formation of a denser protein matrix
structure, caused by the higher amount of extracted salt soluble proteins forming
more proteinprotein interactions. Replacing beef fat with CO showed a larger
number of small, closely packed, fat globules compared to the beef fat treatment.
This is because of the liquid nature of CO relative to the more solid nature of
beef fat, which plays an important role during chopping. As meat protein level
was raised in the CO emulsions, irregularly shape fat globules began to appear
as fat globules coalesced into larger globules that later led to the formation of fat
channels. The discontinuity of the protein matrix allowed fat and liquid to leach
out of the matrix.
The beef fat -Tween 80 (BF - T80) showed more protein matrix aggregation
than the beef fat treatment, suggesting that fat mobility overcame the ability of
the protein matrix to contain the fat. This resulted in large irregularly shaped and
elongated fat pools; this also caused meat batter instability (Fig. 13.6.3). The COTween 80 treatment, at 9% protein, showed an incoherent matrix with very few fat
globules with visible IPF. In the past, non-protein emulsifiers, particularly Tween
80, were shown to be preferentially absorbed by fat globules than meat proteins
because of their higher hydrophiliclipophilic balance values. This can reduce
proteinlipid interactions by interfering with the adsorption of protein molecules
to the fat globule surfaces and can result in decreased binding of fat globules to the
protein matrix.
Pre-emulsification of fat/oil with sodium caseinate produced a finer dispersion of
fat globules compared with the control (Fig. 13.6.3); this was probably because
caseinate has a higher emulsifying capacity than lean beef meat. The protein
matrixes were also less dense than in the all other meat matrixes. This is believed
to be due to the dilution effect of replacing 2% meat protein with SC (which does
not gel at 72C).

13-53

Figure 13.6.4 Means of fat and fluid losses of meat batters prepared with 25% beef fat (BF) or canola oil (CO) and pre-emulsified
fat/oil with T-80 or sodium caseinate (SC) at different protein levels. All treatments contain 25% fat or oil; 2% of the
meat protein was substituted with SC; M, meat protein; BF-T80, beef fat pre-emulsified with T-80; CO-T80, CO preemulsified with T-80; P, protein; BF-SC, beef fat pre-emulsified with SC; CO-SC, CO pre-emulsified with SC. Means
to fluid
(r-z), and fatOF
loss
(a-f), PROCESSING
with no common superscript are significantly different (P<0.05). Last six
13-54 related
CHAPTER
13:loss
PRINCIPLES
MEAT
treatments; 2% of the meat proteins (M) were substituted with SC and then denoted as P* to show total protein in the
whole treatment. From Youssef et al. (2011). With permission.

106fluid losses of meat batters prepared with 25% beef fat (BF) or canola
Figure 13.6.4 Means of fat and
oil (CO) and pre-emulsified fat/oil with T-80 or sodium caseinate (SC) at different protein levels. All
treatments contain 25% fat or oil; 2% of the meat protein was substituted with SC; M, meat protein;
BF-T80, beef fat pre-emulsified with T-80; CO-T80, CO pre-emulsified with T-80; P, protein;
BF-SC, beef fat pre-emulsified with SC; CO-SC, CO pre-emulsified with SC. Means related
to fluid loss (r-z), and fat loss (a-f), with no common superscript are significantly different
(P < 0.05). Last six treatments; 2% of the meat proteins (M) were substituted with SC and
then denoted as P* to show total protein in the whole treatment.
From Youssef et al. (2011). With permission.

13.7 Casings
Meat and sausages have been stuffed into natural casings for thousands of years.
Today this continues in the industry but with increased automation, a larger variety
of pre-formed casings (Fig. 13.7.1), and the option for co-extrusion. The latter has
been one of the most significant developments in sausage casings over the past
century. This process allows continuous, direct deposit of an initially semi-liquid
material (e.g., collagen paste) onto the product as it is extruded from the stuffer.
This has allowed the industry to move from a batch type operation to a continuous
operation (see also Chapter 1 discussing automation). The continuous operation is
a key concept in reducing labour cost, increasing efficiency, and introducing more
mechanization into the process. However, it should be pointed out that the process
does not fit all products (e.g., large diameter sausages) and the initial capital cost
can be high.

Figure 13.7.1 Different typesTHE

of SCIENCE
casings OF
used
for various
meat PROCESSING
products. Products
at the
13-55
POULTRY
AND MEAT
BARBUTmade
University of Guelph. Photo by S. Barbut.

Figure 13.7.1 Different types of casings used for various meat products.
Products made at the University of Guelph. Photo by S. Barbut.

When producing a sausage, the raw meat batter consists of ground/chopped meat
which is a fairly viscous material that can be pumped and stuffed into different sized
casings. During cooking, the meat proteins are denatured and form a heat stable
gel (see Section 13.5). At that point, the cooked firm product can be removed from
the casings (e.g., cellulose casings stripped off hot dogs at the meat plant), or by
the consumer prior to slicing/consumption (e.g., salami casings removed at home
by the consumer). In the case of edible casings (natural or manufactured collagen)
the casing is left on the product (see recipe for European Style Chicken Weiners at
the end of the chapter).
As mentioned above, humans have been using natural casings, such as those
derived from the gastrointestinal tracts of sheep, cattle, etc., for thousands of
years. These casings are still popular in certain products and to some represent
the golden standard. Over the past century, there has been a rapid development of
new packaging materials, including casings (Savi and Savi, 2002), and currently
there are hundreds of different casings on the market. Overall, they can be divided
into a few groups based on their origin.
a. Natural collagen casings are derived from the digestive tracts of sheep and
107encephalopathy (BSE) problem, cattle
hogs. Because of the bovine spongiform

13-56

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

casings are not so popular today. Preparation of casings involves thorough

cleaning, removal of the mucosa layer, and washing the casings several times.
This is done in dedicated plants and requires a lot of manual labour. The cleaned
and inspected casings are then stored in a saturated salt solution and have a shelf
life of a few months. The microstructure of such casings can be seen in Figure
13.7.2, which shows the collagen fibers in the casing. These fibers provide
elasticity during stuffing of the raw product and a bite/snap in the cooked product.
The casings are permeable to water and smoke, and can shrink with the product
ure 13.7.2 Light
micrographs
raw collagen
casings.
frame
showing: (1a) and (1
since they
adhere to theofsurface.
This is a desired
feature,First
especially
in sausages
natural
sheep;
(1c)
and
(1d)
natural
hog;
(1e)
and
(1f)
manufactured
collagen f
that shrink during the smoke house operation and/or later on. An example for the
fresh
Polarized where
light the
was
used
(1b), (1d)
and (1f) to reve
latter is sausage.
dry sausage manufacturing,
product
losesina substantial
amount
of water duringtissue
the drying
process (can
be 30 frame
50%), and
loose casings
make
connective
fibers.
Second
showing:
(2a)willand
(2b) manufactur
the
product
unsalable.
Most
natural
casings
are
edible
and
digestible,
and
do
not
for smoked sausage; (2c) and (2d) manufactured for large diameter ring sausag
need to
be peeled
off prior to consumption.
However,
a veryshows
thick casing
used batter. Polariz
2(e)
and
(2f) co-extruded;
the lower
rightifpart
the is
meat
consumers
will
peel
it
off.
Overall,
natural
casings
are
relatively
expensive
because
light was used in (2b), (2d) and (2f) to reveal connective tissue fibers. Bar = 2
of theFrom
labour involved
their cleaning
application. Today they are used for
m.
Barbut in
(2010).
Withand
permission.
selected products to provide an old fashioned look and a certain snap.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Figure 13.7.2 Light micrographs of raw collagen casings. First frame

showing: (1a) and (1b) natural sheep; (1c) and (1d) natural hog; (1e) and
(1f) manufactured collagen for fresh sausage. Polarized light was used
in (1b), (1d) and (1f) to reveal connective tissue fibers. Second frame
showing: (2a) and (2b) manufactured for smoked sausage; (2c) and
(2d) manufactured for large diameter ring sausage; 2(e) and (2f) coextruded; the lower right part shows the meat batter. Polarized light
was used in (2b), (2d) and (2f) to reveal connective tissue fibers.
Bar = 200 m. From Barbut (2010). With permission.

b. Manufactured collagen casings are made from regenerated collagen extracted

from the skins and hides of various red meat animals (Savi and Savi, 2002). The
microstructure of such casings can be seen in Figure 13.7.2. The casings are usually
edible (depending on the thickness) and therefore do not have to be removed prior
to consumption. They are very uniform and do not have size variations or weak
spots like the natural casings. Because of this, manufactured casings are easier to
work with than natural casings. They are also very uniform, which is important
for portion control, and they are less expensive to buy and require less labour (i.e.,
they arrive at the plant as a roll that can be put directly onto the stuffing horn). Since
they can be made by extruding the regenerated collagen, they can be made with

13-57

13-58

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

different thicknesses and degrees of cross linking. They are made at special plants
and cross linking agents such as ammonia or gluteraldehyde can be used as well
as special colouring agents. Their microbial counts are much lower than natural
casings since they are manufactured from collagen that was extracted at high pH.
Like natural casings they are permeable to water and smoke and can also adhere to
the product and shrink with it.
c. Co-extruded casings are made from pretty much the same material as the
manufactured casings described above and are often made by the same companies.
The collagen gel is usually sold to the industry as a 3.5 5.5% protein dough. It is
used by the meat processor with a special counter rotating head (see Chapter 10
for description of the equipment) that dispenses the gel on top of the product while
it is coming out of the stuffer. Later on, the casing is dewatered to some extent in a
salt bath, dried in an oven, and the collagen molecules are cross-linked with liquid
smoke (i.e., using the aldehyde components; see discussion on liquid smoke in this
chapter). This is usually followed by a full cook cycle inside or outside a cook-inbag. Note that there is also a process where alginate is used for co-extrusion but
the sensory characteristics are different compared to collagen casings. New hybrid
gels of collagen and alginate have also started to appear on the market (Harper et
al., 2013).
d. Manufactured cellulose casings are very popular for the manufacturing of
high volume products such as hot dogs, bologna, and salami. They are made from
cotton liners and can be produced at various sizes (e.g., 1.5 to 15 cm in diameter).
The microstructure of such casings can be seen in Figure 13.7.3. The casings are
very strong and lend themselves to highly automated equipment. Because they are
so uniform and manufacturers control the degree of stretching, portion control is
easy. They are non-edible and have to be peeled off prior to consumption. In the
case of many small diameter products such as hot dogs they are peeled at the plant
by an automated high speed peeler. In the case of products such as large diameter
salami, they are sometimes left on the product and peeled off by the consumer.
Where some shrinkage of the product is expected, the inside of the casing is coated
with protein to improve adherence to the product. Cellulose casings are water and
smoke permeable unless they are coated with plastic (see below combination
casings). The casing can be dyed with different colours and information can be
printed on them. They also have low microbial counts due to the way they are
made. In order to keep them that way, they should be kept in a dry environment;
otherwise mold can grow on them.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

111

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

112

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

113

Figure 13.7.3 Light micrographs of cellulose and plastic casings. First frame
shows: (1a) and (1b) thin cellulose type Fast-peel; (1c) and (1d) large diameter regular casings covering the actual meat batter; (1e) and (1f) outside
polyvinylidene dichloride (PVDC) coated cellulose casings; (1g) and (1h)
inside PVDC coated cellulose. Polarized light was used in (1b), (1d), (1f),
and (1h) to reveal cellulose fibers. Bar = 200 m. Second frame shows:
(2a) and (2b) fibrous/cotton casing covering a meat batter; (2c) and (2d)
outside coated fibrous/cotton; (2e) and (2f) extruded plastic casing. Polarized light was used in (2b), (2d) and (2f) to reveal cellulose fibers/
special plastic. Bar = 200 m. Third frame shows scanning electron
micrographs of casings: (3a) thin cellulose type Fast-peel; (3b)
large diameter cellulose sausage; (3c) outside PVDC coated
cellulose; (3d) inside PVDCcoated cellulose; (3e) regular
fibrous/cotton; (3f) outside coated fibrous/cotton; 3(g)
extruded plastic; and (3h) lower magnification of
micrograph f - see box. Bars = 25 m for all,
except (3h) which is 120 m. From Barbut
(2011). With permission.

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13-62

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

e. Plastic polymer casings are very popular for water/steam cooked sausages
because they are impermeable to water (this is advantageous as water is a more
efficient medium to transfer heat than dry, hot air). A simple way to demonstrate this
is by imagining putting your hand into an oven set at 100C compared to a boiling
pot of water. Where smoking and drying of the sausage surface is not required,
plastic casings represent a viable option. The microstructure of a plastic casing can
be seen in Figure 13.7.3 and a product in this casing is shown in Figure 13.7.4.
The micrograph shows the lamination of the layers and is basically a dense barrier.
Extruded plastic casings are strong and uniform, and can therefore be used for very
large diameter products. They also offer protection against oxidation since they
are usually impermeable to oxygen. This also means that they are impermeable to
smoke. Thus, if smoke flavourings are desired they should be added to the meat
mix. There are also some new developments where liquid smoke can be applied
to the inside of the casings prior to stuffing. Materials such as polyethylene, nylon
and polypropylene are used as a single layer or as a combination of different layers
in the manufacture of plastic polymer casings (Savi and Savi, 2002). These
casings are extruded so usually there is no seam/weak point in the casing. The
casings can be coloured and material printed on them can be used to describe the
product (e.g., nutritional label). Casings can also be extruded with a UV-barrier so
colour fading is not a problem (see Chapter 16).
Figure 13.7.4 Plastic casings used for a jelly meat loaf. Photo by Barbut.

Figure 13.7.4 Plastic casings used for a jelly meat loaf. Product made at the University of Guelph.

Photo by
Figure 13.8.1.1 Oven roasted chicken. Photo
byBarbut.
Barbut and Jinde.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

f. Metal casings/molds are commonly used for canned meats (e.g., meat
loaf processed at high temperature, 121C, in hermetically sealed cans) or for
producing large sausages/hams/loaves at lower temperature (70 - 80C). The
mold provides the product with a certain defined shape. This is important for large
meat masses and it also helps in precise portion control when using high speed
automated systems. In some cases, a cellulose or plastic casing is used to stuff
the product before it is placed in a metal press to facilitate removal of the cooked
product (no sticking and/or peeling surfaces) and cleaning of the molds. When
plastic casings are used, prior to placing the meat in the mold, they are often left
on the product after cooking and act as the packaging material that also provides a
barrier against cross/re-contamination of the product. This technology can be seen
in the preparation of oven roasted turkey breast, 4 4 hams, etc.
g. Retortable pouches are flexible pouches usually made from several layers of
synthetic polymers, of which aluminum foil is one. They provide good moisture
and oxygen barrier properties. It is interesting to note that although the pouch
thickness appears small, it can contain a dozen different layers. The pouches can
be used for meat products that are sterilized at high temperatures. Slices of meat
loaf-type products and chicken soup/stew are commonly packaged in such a
way and then retorted at a temperature of about 121C. The advantage of these
thin pouches is that they can reach the desired cooking temperature much faster
than a traditional round can. As with cans, the product is shelf stable after the heat
treatment and no refrigeration is needed.
h. Combination casings are manufactured casings made from two or more
materials such as collagen reinforced with a cotton mesh, or cotton fibers coated
with plastic. Figure 13.7.3 shows an example of this where two components
(cellulose and plastic) are included. By combining two or more layers, the
processor can take advantage of both materials (e.g., strength of the plastic mesh
with the smoke permeability of cellulose, or peeling ease of cellulose casings with
the strength of large cotton fibers).

13.8 Formulations
In this section you will find various recipes of further processed meat products
popular around the world. The recipes are courtesy of Hermann Laue Spice
Company, Canada. These formulations are used by the industry but here they only
serve as general guidelines and should be used as such. Also, local government
regulations vary among countries (e.g., use of additives such as nitrite, phosphate)
and therefore careful examination of local legislation is required. The section

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contains formulations related to whole muscle products, restructured products,

boneless, bone in, ground and emulsified products.

13.8.1 Smoked Chicken Roast Naturally Cured

Ingredients
Meat:
72.0 kg boneless skinless chicken breast
8.0 kg white chicken trim
Brine:
20.0 kg
The brine is made by mixing:

12.0 kg cold water

3.4 kg ice flakes
1.7 kg sea salt
1.2 kg vinegar (serves as a bacteriostat)
1.0 kg evaporated cane sugar
0.6 kg fermented celery extract
0.058 kg onion powder
0.040 kg ground white pepper
0.002 kg rosemary extract

Processing
Grind the chicken breast through a 25 mm plate.
Grind the white chicken trim through a 5 mm plate.
Mix the brine and add to the ground chicken meat inside a vacuum
tumbler.
Vacuum tumble for 1.5-2.0 hr at 10-12 rpm.
Rest overnight.
Firmly stuff the product into a 105 mm caliber, cellulose casings.
Process in a preheated smokehouse.
Heat at 55C and 30% RH for 30 min.
Dry at 65C for 20 min.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Hot smoke at 65C for 45 min or to the desired colour

Steam cook at 85C to an internal temperature of 74C (Fig. 13.8.1.1).
Chill down rapidly and store under refrigeration prior to shipping.
Figure 13.8.1.1 Oven roasted chicken. Photo by Barbut and Jinde.

Figure 13.8.1.1 Oven roasted chicken. Photo by Barbut and Jinde.

114

13.8.2 Traditional Chicken/Turkey Roast (30% pump; optional 50%

pump)
Ingredients
Meat:
100.0 kg boneless skinless chicken/turkey breast
Brine:
30.0 kg
The brine is made by mixing:
22.0 kg cold water
3.6 kg ice flakes
4.0 kg brine and cure unit (salt, sugar, phosphate, erythorbate, nitrite)

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0.4 kg roast seasonings (natural roast flavour, spices)

Spice rub: 6 g roast flavoured rub mixed with 18 ml of water, per 1 kg
of tumbled roast.
Processing
Inject the turkey breast meat with 30% brine.
Vacuum tumble for 4 hr at 12-15 rpm; start immediately after injecting.
Rest overnight and tumble for 1 hr at 12-15 rpm.
Combine 2 turkey breasts together (thick end over thin end) and wrap
with a collagen film before stuffing it into a net #22-3 (i.e., a net with
22 squares around the circumference made up of 3 stitches between
squares). Clip both ends of the net.
Mix 5 parts of roast flavoured rub together with 3 parts of water until a
thick paste has been formed and rub the roasts evenly.
Place roasts on smoke screens, place in an oven and cook.
Dry at 90C for 1 hr or until the surface is completely dry.
Steam cook at 78C to an internal temperature of 71C (Fig. 13.8.2.1).
Shower with cold water to cool down quickly.
Note: a 50% pump roast can also be made by adding 50 kg brine to 100
kg of boneless skinless turkey/chicken breast meat. The brine consists of
35 kg cold water, 9 kg of ice flakes, 5 kg of turkey/chicken roast brine
unit (salt, sugar, phosphate) and 1.3 kg spice unit (soy protein isolate,
sugar, spice extracts).

Figure 13.8.2.1 Oven roasted chicken prepared in netting. Photo by Barbut and Jinde.

Figure 13.8.2.1 Oven roasted chicken prepared in netting.

by by
Barbut
and Jinde.
Figure 13.8.3.1 Oven roasted turkey.Photo
Photo
Barbut
and Jinde.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Figure 13.8.2.1 Oven roasted chicken prepared in netting. Photo by Barbut and Jinde.

13.8.3 Smoked Turkey Roast

Ingredients
Similar to previously described Traditional Chicken/Turkey Roast.
Processing
Similar to injection and stuffing of Traditional Chicken/Turkey Roast.

Dry at 65C for 45-60 min.

Hot smoke at 65C for 1.5 hr or to the desired colour.
Steam-cook at 78C to an internal temperature of 71C (Fig. 13.8.3.1).
Shower with cold water to cool down quickly.

Figure 13.8.3.1 Oven roasted turkey. Photo by Barbut and Jinde.

Figure 13.8.3.1 Oven roasted turkey. Photo by Barbut and Jinde.

Figure 13.8.6.1 Turkey ham. Photo by Barbut and Jinde.

13.8.4 Turkey Roast Slicing Log Salt Free

Ingredients

115

Meat:
100.0 kg skinless turkey breast

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Brine:
15.0 kg
The brine is made by mixing:

7.2 kg cold water

2.8 kg potassium lactate/diacetate
4.28 kg salt free turkey roast pumping unit
0.72 kg transglutaminase powder

Processing

Grind the turkey breast meat through a kidney plate.

Mix the transglutaminase with cold water.
Mix the ground turkey meat with the dry ingredients for 8 min.
Add the transglutaminase slurry and mix for 8 min.
Add the potassium lactate/diacetate and mix for 4 min.
Firmly stuff into moisture proof casings of desired caliber.
Store under refrigeration for at least 2-3 hr prior to cooking (time for
enzyme to work).
Steam cook at 80C to an internal temperature of 72C.
Cool down quickly with a cold water shower.

13.8.5 Smoked Chicken Ham Naturally Cured

Ingredients
Meat:
72.0 kg chicken thigh meat (defatted)
8.0 kg chicken drum meat
Brine:
20.0 kg
The brine is made by mixing:
12.0 kg cold water
3.3 kg ice flakes
1.8 kg sea salt

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

1.25 kg vinegar (serves as a bacteriostat)

0.90 kg evaporated cane sugar
0.600 kg fermented celery extract
0.058 kg onion powder
0.050 kg sweet cherry powder
0.040 kg garlic powder
0.002 kg rosemary extract

Processing

Grind the chicken thigh meat through a 25 mm plate.

Grind the drum meat chicken trim through a 3 mm plate.
Mix the brine and add to the ground chicken meat in a vacuum tumbler.
Vacuum tumble for 2.5 hr at 10-12 rpm.
Rest overnight and vacuum tumble for 20 min.
Firmly stuff the product into a 105 mm caliber, cellulose casings.
Process in a preheated smokehouse.
Heat at 55C and 30% RH for 30 min.
Dry at 65C for 20 min.
Hot smoke at 65C for 45 min or to the desired colour
Steam cook at 85C to an internal temperature of 74C.
Chill down rapidly and store under refrigeration prior to shipping.

13.8.6 Turkey Ham (4 6)

Ingredients
Meat:
100 kg boneless lean turkey thigh meat
Brine:
40 kg
The brine is made by mixing:

28 kg cold water
6.5 kg ice
5.5 kg brine and cure unit
(salt, soy/whey proteins, phosphate, spices, erythorbate, nitrite)

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Processing
L
 acerate the turkey thigh meat (especially from the skin side) to increase
the surface area.
Tumble the meat with the brine in a well-chilled vacuum tumbler for 6
hr at 12-15 rpm.
Rest overnight and tumble for 1.5 hr the next day.
Stuff the meat into cook-in-bags (also referred to as cook & ship bags).
Place hams into 4 6 inches ham molds and press firmly.
Cook in a smoke house by using steam at a temperature of 78C, until
reaching an internal temperature of 71C (Fig. 13.8.6.1).

Shower with cold water to chill quickly prior to transferring to a
refrigerator.

Figure 13.8.6.1 Turkey ham. Photo by Barbut and Jinde.

Figure 13.8.11.1 Turkey kolbossa. Photo by Barbut and Jinde.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

13.8.7 Turkey Pastrami

Ingredients
Meat:
100 kg skinless turkey breast
Brine:
50 kg
The brine is made by mixing:

14.0 kg cold water

12.3 kg ice flakes
8.7 kg sodium lactate/diacetate
1.85 kg brown sugar
0.35 kg pastrami liquid seasoning
13.5 kg brine and cure unit
(salt, soy/whey proteins, phosphate, spices, erythorbate, nitrite)
Rub per 1.0 kg of tumbled turkey breast: 10g fine/coarse pastrami rub.

Processing
Completely dissolve all of the dry ingredients in the cold water.
Add ice and the sodium lactate/diacetate and mix until all of the ice has
melted.
Pump the turkey breast 50% and immediately start the tumbling process.
Vacuum tumble for 3-4 hrs at 10-12 rpm.
Rest under refrigeration overnight and tumble again for 30 min under
vacuum.
Add the spices and rub ingredients into the tumbler and tumble at slow
speed until an even coating is created.
Place the turkey breast onto smoke screens and process in the
smokehouse:
Dry at 75C for 1 hr or until the surface feels dry.
Hot smoke at 65C for 30 min.
Steam cook at 78C to an internal temperature of 71C.
Shower for 5 min, then quick chill with air.
Store under refrigeration overnight prior to shipping.

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13.8.8 Regular Smoked Turkey Sausage

Ingredients
Emulsion part (60 kg):
42.0 kg turkey thigh meat (first ground 3 mm)
8.0 kg turkey skin (frozen, first ground 3 mm)
10.0 kg ice
Coarse insert (40 kg):
34.0 kg turkey thighs (ground 5 mm)
6.0 kg cold water
Spice and ingredients:

3.0 kg seasoned binder (salt, potato starch, dextrose, spices, erythorbate)

1.0 kg brown sugar
0.3 kg curing salt
0.3 kg phosphate
0.2 kg garlic powder
0.1 kg black pepper (fine grind)

Processing
M
 ix the coarse ground meat, one day prior to processing, together
with water and 40% of the spice and ingredient mix, until a good bind
develops. Store the meat under refrigeration overnight.
Chop the ground meat and skin, intended for the emulsion part, while
adding the rest of the spice and ingredient mix. Chop for a few revolutions
at the slow speed before adding about half of the ice. Continue cutting at
high speed to a temperature of 12C, add the rest of the ice and proceed
cutting to a final temperature of 8C.
Add the pre-seasoned coarse insert and mix well before cutting at slow
speed to the desired size.
Stuff the meat into collagen casings (caliber 29/32) or any other smoked
sausage casing.
Dry in a smoke house at 55C for 15 min.
Hot smoke at 60C, 25-30% relative humidity for 30 min or desired
colour is reached.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Steam cook at 78C to an internal temperature of 71C.

Shower with cold water for fast cooling.

13.8.9 Smoked Maple Flavour Turkey Sausage

Ingredients
Emulsion part (60 kg):
50.0 kg skin on turkey thigh meat (first ground 3 mm)
10.0 kg ice
Coarse insert (40 kg):
25.0 kg turkey drum meat (ground 5 mm)
5.0 kg turkey skin and fat
10.0 kg cold water
Spice and ingredients:

3.0 kg seasoned binder

1.0 kg maple flavour
1.5 kg brown sugar
1.0 kg specialty starch
0.3 kg curing salts (erythorbate, nitrite)
0.3 kg phosphate
0.1 kg black pepper (32 mesh)

Processing
F
 ollow procedure of previous product (Turkey Sausage) up to the
stuffing stage.
Stuff into collagen casings, caliber 32/35 and link to 110g.
Warm up in a smokehouse set at 55C and 40% RH for 20 min.
Dry at 65C for 20 min.
Hot smoke at 65C for 40 min or to the desired colour.
Steam cook at 80C to a core temperature of 71C.
Cool down with shower and store under refrigeration overnight prior to
packaging.

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13.8.10 Tikka Masala Fresh Chicken Sausage

Ingredients
Meat:
30.0 kg chicken breast (ground 8 mm)
55.0 kg chicken thigh (ground 8 mm)
15.0 kg cold water
Spices and ingredients:

16.0 kg salt
5.0 kg Tikka Masala seasoning unit
1.0 kg potato starch
0.2 kg phosphate

Processing
M
 ix the ground chicken meat with all the ingredients until a good bind
has developed.
Add the water in 2-3 steps while mixing.
Stuff the meat batter into collagen casings of desired caliber, link to the
desired weight and pack. Product to be kept refrigerated or frozen prior
to shipping.

13.8.11 Turkey Kielbasa

Ingredients
Coarse meat insert (70 kg):
59.0 kg lean turkey thighs (ground 25 mm)
11.0 kg cold water
Fine meat part (30 kg):
25.0 kg turkey thighs (ground 3 mm)
5.0 kg cold water

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Spice ingredients:

1.9 kg salt
0.9 kg kielbasa seasoning
0.8 kg brown sugar
0.6 kg curing salt (includes erythorbate and nitrite)
0.3 kg phosphate

Processing
O
 ne day prior to processing, put the coarse meat in a vacuum-tumbler for
1.5 hr together with water and 70% of the dry ingredients.
Cover and store the tumbled coarse insert under refrigeration overnight.
Immediately before processing, tumble/mix again for 10 min.
Mix the fine ground turkey thigh meat together with the rest of the dry
ingredients and water, until a good bind has developed.
Add the tumbled coarse material to the fine ground meat and mix
together to an even distribution and a good bind.
Stuff the batter into collagen ring casings cal. 52 mm.
Process the product in a smokehouse:
Warm at 50C and 40% humidity for 30 min.
Dry at 60C for 15 min.
Hot smoke at 60C for 45 min or to the desired colour.
Steam-cook at 78C to a core temperature of 71C (Fig. 13.8.11.1).
Product to be cooled down with shower.
Store under refrigeration overnight prior to shipping.
Figure 13.8.11.1 Turkey kolbossa. Photo by Barbut and Jinde.

Figure 13.8.11.1 Turkey kielbasa. Photo by Barbut and Jinde.

Figure 13.8.12.1 Chicken wieners. Photo by Barbut and Jinde.
116

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

13.8.12 European Style Chicken Wieners

Ingredients
Meat:

40.0 kg chicken thigh meat

26.0 kg chicken drum meat
7.0 kg fine textured chicken meat (frozen)
5.0 kg chicken skin and fat

Ice:
28.0 kg
Spices and additives:

1.7 kg salt
1.4 kg dextrose
1.0 kg modified starch
0.8 kg Wiener seasoning
0.6 kg curing salt (with erythorbate and nitrite)
0.2 kg phosphate
0.1 kg paprika
0.1 kg onion powder

Processing
Grind all meats and skin through a 3 mm plate.
Use a bowl cutter to cut the meat for a few revolutions at slow speed
before adding all of the spices and ingredients plus 1/3 of the ice.
Cut at high speed to 8 - 10C.
Add the remaining ice in 2 steps while cutting at high speed to 6C.
Cut at slow speed to 8C.
Stuff into sheep casings and link to the desired size.
Smoke and cook:
Pre heat in a smokehouse at 55C and 40% RH for 20 min.
Dry at 65C for 15 min.
Hot smoke at 65C for 30 min.
Steam-cook at 78C to a core temperature of 71C (Fig. 13.8.12.1).
Cool down with a cold water shower.
Store under refrigeration overnight prior to packaging.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Figure 13.8.12.1 Chicken wieners. Photo by Barbut and Jinde.

Figure 13.8.13.1 Chicken bologna. Photo by Barbut and Jinde.

13.8.13 Chicken/Turkey Hot Dogs/Bologna

Ingredients
Meat:
86.0 kg mechanically deboned chicken/turkey meat
Ice:
14.0 kg
Spices and additives:
Binder unit 8.70 kg (salt, soy/whey117
proteins, spices, erythorbate)
Curing salt 0.3 kg (includes nitrite)
Phosphate 0.3 kg
Processing
S
 lowly cut the slightly frozen meat with about 5 kg of flaked ice in a
bowl chopper for a few revolutions.
Add the binder unit, salt and phosphate and chop at the high speed setting
while adding the rest of the ice until temperature reaches 8-10C.

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

Remove the emulsion from the chopper.

Stuff into easy-peel hot dog casings and link to desired size.
Place the product on a smoke house tree.
Smoke and cook:

Dry the surfaces in a smoke house at 55C for 5 min or as required.

Hot smoke at 55C and 25% RH for 20-30 min.
Steam cook at 75C to an internal temperature of 71C (Fig. 13.8.13.1).
Shower with cold water for 10 min.
Refrigerate overnight prior to peeling the casings.
Note: for bologna use the same formulation and procedure, and then
stuff into large diameter cellulose or fibrous casings. Heat process should
be lengthened to achieve a 71C internal temperature.

Figure 13.8.13.1 Chicken bologna. Photo by Barbut and Jinde.

117by Barbut and Jinde.

Figure 13.8.13.1 Chicken bologna. Photo

13.8.14 Turkey Pepperoni Sticks

Ingredients
Meat:
60.0 kg turkey thigh meat
22.0 kg turkey drum meat

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Water:
18.0 kg cold water
Spices and additives:

1.7 kg salt
1.5 kg mild pepperoni seasoning
1.5 kg potato starch
1.2 kg liquid vinegar
1.0 kg corn syrup solids
0.6 kg curing salt (including erythorbate and nitrite)
0.3 kg phosphate

Processing
Grind the turkey thigh meat through the 5 mm plate.
Grind the turkey drum meat through the 3 mm plate.
Mix for 2 3 min all the meat and dry ingredients before adding 6 kg of
the cold water.
Add the remaining water in 2 steps while mixing to a good bind.
Stuff into collagen casings (19 21 mm caliber) and link to 60 65 g.
Smoke and cook:
Use a smoke house to dry the surfaces at 65C for 20 min.
Hot smoke at 65C for 20 min or to the desired colour.
Cook at 70C and 60% RH for 20 min.
Cook at 78C and 60% RH to a core temperature of 71C (Fig. 13.8.14.1).
Figure
Cool 13.8.14.1
down with
shower
and store
under
refrigeration
Turkey
pepperoni
sticks.
Photo
by Barbutovernight
and Jinde.prior to
packaging.

Figure 13.8.14.1 Turkey pepperoni sticks. Photo by Barbut and Jinde.

Figure 13.8.16.1 Chicken wings. Photo by Barbut and Jinde.

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CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

13.8.15 Hot Habanero Turkey Sticks

Ingredients
Meat:
40.0 kg turkey drum meat, ground 3 mm
10.0 kg turkey fat, frozen, ground 5 mm
50.0 kg turkey thigh, ground 5 mm
Spices and cure:
5 .55 kg seasoning and cure mix (salt, dextrose, paprika, spices,
erythorbate, nitrite)
Processing
M
 ix all of the ground meat and fat together with the spices and cure until
a good bind has developed.
Stuff the batter into natural casings or collagen casings (calibre 15-20
mm).
Process the product in a smokehouse:
Dry heat at 55C for 2 hr.
Dry heat at 60C for 1 hr.
Dry heat at 65C for 1 hr.
Dry heat at 72C for 1 hr or until the desired dryness is reached.
If desired, hot smoke can be applied during the second drying cycle.
Product to be air cooled only.

13.8.16 Honey Garlic Marinated Chicken Wings

Ingredients
Meat:
90.0 kg chicken wings
Water:
10.0 kg (cold)

Figure 13.8.14.1 Turkey pepperoni sticks. Photo by Barbut and Jinde.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Spice:
5 .5 kg honey garlic marinade (sugar, salt, garlic, natural honey flavour,
vinegar, spices)
Processing
Dissolve the spice unit in the cold water.
Vacuum tumble the well-chilled chicken wings together with the liquid
marinade; use slow speed for 30-45 min.
Remove the marinated chicken wings from the tumbler and pack in
vacuum bags or immediately freeze (IQF).
Keep product refrigerated or frozen prior to shipping.
Cook at home/restaurant to 72 C internal (Fig. 13.8.16.1).
Figure 13.8.16.1 Chicken wings. Photo by Barbut and Jinde.

Figure 13.8.16.1 Chicken wings. Photo by Barbut and Jinde.

118

13.8.17 Mesquite Chicken Wings

Ingredients
Meat:
95.0 kg chicken split wings

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Water:
5.0 kg (cold)
Spice:
5.0 kg Mesquite marinade
Processing

Put the fresh chicken wings into a vacuum tumbler.

Mix the BBQ marinade together with the cold water and add to tumbler.
Vacuum tumble for 15-20 min.
Remove the seasoned chicken wings from the tumbler, tray pack and
overwrap.

13.8.18 Ginger Lemon Chicken Drum Sticks

Ingredients
Meat:
85.0 kg chicken drum sticks
Water:
15.0 kg (cold)
Spice:
6.5 kg ginger lemon marinade
(salt, sugar, lemon juice, spices)
Processing
Mix the spices together with the cold water.
Vacuum tumble the well-chilled chicken drum sticks together with the
liquid marinade; use slow speed for 30-45 min.
Remove the marinated chicken drum sticks from the tumbler and pack in
plastic bags or immediately freeze.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

N
 ote: other variations, such as Hot Buffalo Chicken Wings can also be
made the same way, but with a different spice mix.
Keep product refrigerated or frozen prior to shipping.

13.8.19 Caribbean Jerk Chicken Drum Sticks

Ingredients
Meat:
95.0 kg chicken drum sticks
Water:
5.0 kg (cold)
Spice:
1.2 kg salt, fine
1.5 kg Caribbean Jerk seasoning
0.2 kg phosphate
Processing
Place the well chilled fresh chicken drum sticks into a vacuum tumbler.
Dissolve the dry ingredients in the cold water and vacuum tumble for
15 20 min.
Remove the seasoned chicken drum sticks from the tumbler, tray pack
and overwrap.

13.8.20 Fajita Chicken/turkey/duck/goose

Ingredients
Meat:
82.0 kg chicken/turkey/duck/goose breast filets or breast strips
14.8 kg cold water

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Spice:
3 .2 kg chicken Fajita seasoning (salt, dextrose, soy sauce powder,
phosphate, garlic powder, spices)
Processing
Completely dissolve the Fajita seasoning in the cold water.
Vacuum tumble the chicken meat and seasoning solution for 40-50 min
at 8-10 rpm.
The marinated chicken strips can then be individually quick frozen (IQF)
and packed or put onto a skewer and frozen.
Prior to serving, pan fry together with red, yellow and green bell pepper
strips and fresh or frozen diced onions.
Serve on pita bread or in taco shells; a sauce can be added if desired.

13.8.21 Jellied Chicken/Turkey/Duck Roll

Ingredients
Meat:
45 kg white turkey/chicken roast (see second recipe)
Vegetables:
15 kg canned mushrooms and/or broccoli heads
Gelatin:
40 kg gelatin solution (7 kg seasoned gelatin powder plus water)
Processing
Dice the chicken/turkey roast into approximately 1 1 1 cm cubes.
Rinse the mushrooms (and/or broccoli) with hot water and mix with the
diced meat.
Completely dissolve the dry gelatin powder in hot water (> 80C). You
can add a little bit of oil to the hot water to avoid foaming.
Fill clear plastic casings (e.g., 12 cm diameter) with the diced meat and
vegetable mix.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

A
 dd the proper amount of gelatin solution into the casings and remove
all air bubbles prior to clipping.
Cool down in a cold water bath (see Fig 13.7.4).

13.8.22 Chicken/Turkey/Duck Chili Con Carne

Ingredients
Meat:
31.25 kg chicken/turkey/duck thigh meat
Vegetables:

25.00 kg red kidney beans (canned)

28.15 kg ground tomatoes (canned)
7.80 kg diced onions (frozen)
7.80 kg hot water

Spice:
2.62 kg chili seasoning mix
(sugar, salt, paprika, garlic powder, spice)
Processing
Grind chicken/turkey thigh meat through a 3 mm plate.
Mix ground meat together with the chili seasoning mix and hot water.
Cook in a steam kettle over medium/high heat until meat is well done.
Add all of the canned and frozen vegetables, bring to a boil and simmer
over medium heat for 10-15 min.
Cool down completely prior to packing.

13.8.23 Chicken Nuggets

See Chapter 14

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References
Aberle, E.D., J.C. Forrest, D.E. Gerrard and E.W. Mills. 2012. Principles of Meat
Science. Kendall/Hunt Publ., Dubuque, IA.
Acton, J.C., G.R. Ziegler and D.L. Burge. 1983. Functionality of muscle
constituents in the processing of comminuted meat products. CRC Rev.
Food Sci. Nutr. 18:99.
Aguilera, J.M. and H.J. Kessler. 1989. Properties of mixed and filled type dairy
gels. J. Food Sci. 54:1213.
Asghar, A., K. Samejima and T. Yasui. 1985. Functionality of muscle proteins
in gelation mechanisms of structured meat products. CRC Crit. Rev. Food
Sci. Nutr. 22:27.
Barbut, S. 2011. Sausage casings microstructure of regular and coated cellulose
fabric and plastic casings. Ital. J. Food Sci. 23:208.
Barbut, S. 2010. Microstructure of natural, extruded and co-extruded collagen
casings before and after cooking. Ital. J. Food Sci. 22:126.
Barbut, S. 1999. Advances in determining meat emulsion stability. In: Quality
Attributes of Muscle Food. Xiong, Y.L., C.T. Ho and F. Shahidi (Eds).
Plenum Publ., New York, NY.
Barbut, S. 1998. Use of fiber optic probe to predict meat emulsion breakdown.
Ital. J. Food Sci. 10:253.
Barbut, S., A. Gordon and A. Smith. 1996. Effect of cooking temperature on
the microstructure of meat batters prepared with salt and phosphate. LWTFood Sci. Technol. 29(5):475.
Barbut, S. and C.J. Findlay. 1989. Sodium reduction in poultry products: A
review. CRC Crit. Rev. Poult. Biol. 2:59.
Barbut, S. and G. Mittal. 1989. Rheological and gelation properties of reduced
salt meat emulsions containing polyphosphates. J. Food Proc. & Preserv.
12:309.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Barbut, S. 1988. Microstructure of reduced salt meat batters as affected by

polyphosphates and chopping time. J. Food. Sci. 53:1300.
Barbut, S., D.B. Josephson and A.J. Maurer. 1985. Antioxidant properties of
rosemary oleoresin in turkey sausage. J. Food. Sci. 50:1356.
Borchert, L.L., M.L. Greaser, J.C. Bard, R.G. Cassens and E.J. Briskey. 1967.
Electron microscopy of a meat emulsion. J. Food Sci. 32:419.
Cassens, R.G. 1990. Nitrite- Cured Meat: A Food Safety Issue in Perspective.
Food Sci. and Nutr. Press. Trumbull, CN.
Davis, T.A., B. Volesky and A. Mucci. 2003. A review of the biochemistry of
heavy metal biosorption by brown algae. Water Res. 37(18):4311.
Foegeding, E.A., E.L. Bowland and C.C. Harding. 1995. Factors that determine
the fracture properties of globular protein gels. Food Hydrocolloids 9:237.
Graffagnini, M.J. 2010. Nanofoods: European and US regulatory approaches.
Nanotech. L. & Bus. 7:351.
Gravelle, A.J., A.G. Marangoni and S. Barbut. 2015. Influence of particle size
and interfacial interactions on the physical and mechanical properties of
particle-filled myofibrillar protein gels. Royal Soc. Chem. Adv. 5:60723.
Jones, K.W. and R.W. Mandigo. 1982. Effect of chopping temperature on the
microstructure of meat emulsions. J. Food Sci. 47:1930.
Harper, B.A, S. Barbut, L.T. Lim and M.T. Marcone. 2013. Characteristics
of wet alginate and composite films containing gelatin, whey and soy
proteins. Food Res. Int. 52:452.
LaBudde, R.A. and T.C. Lanier. 1995. Protein functionality and development
of bind values. In: Proc. Reciprocal Meat Conference, San Antonio, TX.
48:59.
Lee, C.M. 1985. Microstructure of meat emulsions in relation to fat stabilization.
Food Microstruct. 4:63.
Maga,J.A. 1989. Smoke in Food Processing. CRC Press, Boca Raton, FL.

13-87

13-88

CHAPTER 13: PRINCIPLES OF MEAT PROCESSING

Mezzenga, R. and P. Fischer. 2013. The self-assembly, aggregation and phase

transitions of food protein systems in one, two and three dimensions. Rep.
Prog. Phys. 76:046601.
Montejano, J.G., D.D. Hamann and T.C. Lanier. 1984. Thermally induced
gelation of selected comminuted muscle systems - rheological changes
during processing; final strengths and microstructures. J. Food Sci. 49:1496.
Pearson, A.M. and F.W. Tauber. 1984. Processed Meats. AVI Publ., Wesport,
CT.
Phillips, L.G., D.M. Whitehead and J. Kinsella. 1994. Structure-Function
Properties of Food Proteins. Academic Press, San Diego, CA.
Prakash, A., S. Sen and R. Dixit. 2013. The emerging usage and applications of
nanotechnology in food processing industries: the new age of nanofood. Int.
J. Pharm. Sci. Rev. Res. 22(1).
Ramrez-Surez, J.C. and Y.L. Xiong. 2003. Effect of transglutaminase-induced
cross-linking on gelation of myofibrillar/soy protein mixtures. Meat Sci.
65(2):899.
Savi, Z. and Savi, I. 2002. Sausage Casings. p.354. Victus Inc., Vienna, Austria.
Schmidt, G.R. 1984. Processing effects on meat product microstructure. Food
Micro. 3:33.
Sebranek, J.G. and J.N. Bacus. 2007. Cured meat products without direct addition
of nitrate or nitrite: what are the issues? Meat Sci. 77(1):136.
Shults, G.W. and E. Wierbicki. 1973. Effects of sodium chloride and condensed
phosphates on water holding capacity, pH and swelling of chicken muscle.
J. Food Sci. 38:991.
Sindelar, J.J. and A.L. Milkowski. 2012. Human safety controversies surrounding
nitrate and nitrite in the diet. Nitric Oxide. 26(4):259.
Theno, D.M. and G.R. Schmidt. 1978. Microstructural comparisons of three
commercial frankfurters. J. Food Sci. 43:845.

THE SCIENCE OF POULTRY AND MEAT PROCESSING BARBUT

Toledo, R.T. 2007. Wood Smoke Components and Functional Properties. In:
International Smoked Seafood Conference Proceedings. Kramer, D.E. and
L. Brown (Eds). Alaska, USA, p55.
Totosaus, A., J.G. Montejano, J.A. Salazar and I. Guerrero. 2002. A review of
physical and chemical protein-gel induction. Int. J. Food Sci Tech. 37:589.
Wang,S.F. and D.M. Smith. 1992. Functional properties and microstructure of
chicken breast salt soluble protein gels as influenced by pH and temperature.
Food Struct. 11:273.
Wang, S.F., D.M. Smith and J.F. Steffe. 1990. Effect of pH on the dynamic
rheological properties of chicken breast salt-soluble proteins during heatinduced gelation. Poultr. Sci. 69:2220.
Whiting, R.C. 1987. Influence of various salts and water soluble compounds on
the water and fat exudation and gel strength of meat batters. J. Food Sci.
52:1130.
Wright, D.J., I.B. Leach and P. Wilding. 1977. Differential scanning calorimetric
studies of muscle and its constituent proteins. J. Sci. Food Agric. 28(6):557.
Xiong, Y.L. and C.J. Brekke. 1991. Protein extractability and thermally induced
gelation properties of myofibrils isolated from pre- and post-rigor chicken
muscles. J. Food Sci. 56:210.
Yasui, T., M. Ishioroshi and K. Samejima. 1980. Heat-induced gelation of
myosin in the presence of actin. J. Food Biochem. 4:61.
Youssef, M.K., S. Barbut and A. Smith. 2011. Effects of pre emulsifying fat/
oil on meat batter stability, texture and microstructure. Int. J. Food Sci.
Technol. 46(6):1216.
Youssef, M.K. and S. Barbut. 2011. Effects of two types of soy protein isolates,
native and preheated whey protein isolates on emulsified meat batters
prepared at different protein levels. Meat Sci. 87(1):54.

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