EFR - M4 Protein

COMPOSITION OF PROTEIN TYPES OF PROTEIN

Amino acids are organic substances containing two Type of FIBROUS GLOBULAR CONJUGATED
characteristic functional groups: the amino (—NH2) Protein
group and the carboxyl group (—COOH). Shape

● The amino and the acid groups and various

organic components are attached to a single carbon

(the α carbon).
Examples COLLAGEN ENZYMES HAEMOGLOBIN
● These various organic components (designated as R
KERATIN ANTIBODIES
groups) range from the single hydrogen atom of HORMONES
glycine to dual-ring structures, such as that in
tryptophan.
GLOBULAR
● Proteins are molecules composed of many amino ● all enzymes, some hormones, and oxygen-
acids joined together by peptide linkages. transporting proteins are globular proteins.
● protein may contain several hundred amino acid
● Within this large category are albumins, readily
moieties linked together into a complex molecule
coagulated by heat, and soluble in water.

● Globulins occur in meats and legumes. They also

are coagulated by heat, but their solubility in water
is quite limited unless sodium chloride or another
neutral salt is added (called salting in).

CONJUGATED
● Conjugated proteins are proteins joined with
another substance.
● Examples are lipoproteins
(lipid–protein complex) and glycoproteins
(carbohydrate– protein complex).

FIBROUS
● Fibrous proteins are noted for their insolubility.

● Fibrous proteins of particular interest from

the standpoint of food are collagen and elastin,
which are structurally important in meats and
poultry.
 CONJUGATED PROTEINS
● Mucoproteins (also called glycoproteins) contain a
carbohydrate moiety combined with protein.
○ Various sugars occur in mucoproteins.
○ Ovomucoid in egg white is an uncoagulable
mucoprotein.
○ Hemagglutinin is a mucoprotein in soybeans.
● Lipoproteins are composed of a protein and a lipid.
○ Among the lipids found in these water-insoluble
compounds are cholesterol,
triglycerides, and phospholipids.
● Metalloproteins, the protein is complexed with a
metal.
○ Ferritin, a metalloprotein- containing iron, is found
in the liver.
○ Myoglobin and hemoglobin are other iron-
containing metalloproteins.
● Nucleoproteins, proteins combined with nucleic
acids, also are found in foods.
● Phosphoproteins include the casein in milk.
○ In these conjugated proteins, inorganic phosphates
are linked with the protein.
DENATURATION AND COAGULATION
● DENATURATION- physical changes are caused by
alteration of the shape of the protein molecule
○ stresses, particularly heat, agitation, and ultraviolet
light, they may undergo modifications that result in
decreased solubility or loss of ability to catalyze
reactions (if the protein is an enzyme).
● COAGULATION- a second stage after denaturation
○ Denatured molecules clump together
○ During denaturation, protein molecules relax from
their tertiary state and begin to resemble more
closely their secondary helical structure without
distortion.
○ increase the viscosity of the mixture perceptibly,
even when the mixture is hot.
○ When concentration of protein is sufficiently high,
the fluid mixture may coagulate into a solid, as is true
when cooking eggs. physical rather than chemical
changes in the protein molecule.
● Sometimes enzymes are used in making food
products, such as chocolates and cheeses.
● The fact that enzymes are proteins must always be
remembered when foods containing enzymes are
prepared.
● If enzyme action is desired, as it is when invertase is
added to a fondant to aid in softening the center of a
chocolate-dipped candy, the enzyme cannot be added
until the heating and cooling of the fondant are
complete.
● Otherwise, the enzyme may be denatured and its
catalytic ability lost because of the change in its
physical shape.
● There are instances when enzyme activity should
be avoided, as in the preparation of a gelatin salad
with pineapple.
● Bromelain in fresh pineapple is a proteolytic
enzyme that hydrolyzes gelatin, resulting in a loss of
gel strength.
● Cooked or canned pineapple can be added to
gelatin, however, because heating the pineapple
inactivates the enzyme.
vegetables to be frozen are blanched to inactivate
(denature) the enzymes
○ could continue to cause some deterioration during
storage.
● adding an enzyme may enhance the usefulness of a
food.
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○ the addition of lactase to milk to produce a milk HYDROLYSIS
product that is low in lactose, making it suitable for
people with lactose intolerance ● Protein molecules may undergo hydrolysis to form
shorter chains.
● vegetables to be frozen are blanched to inactivate
(denature) the enzymes ● This reaction splits the primary chain into two
shorter peptides
○ could continue to cause some deterioration during
storage. ● The reaction usually is the result of enzymatic
action by peptidases, but sometimes collagen is
● adding an enzyme may enhance the usefulness of a
cleaved by acid hydrolysis.
food.
● The shorter chains resulting from hydrolysis show
○ the addition of lactase to milk to produce a milk
increased solubility and decreased ability to thicken
product that is low in lactose, making it suitable for
food product
people with lactose intolerance.
● both the pH and the temperature of the food must
be considered to achieve the desired result.

● Alteration of the pH can greatly retard or even

block catalysis by the enzyme

○ because of changes in the electrical profile on its

surface.

○ Heat can alter the surface shape of the enzyme,

making impossible for it to lock with the substrate to
catalyze a reaction.

● Egg proteins are effective as thickening agents

when they are denatured and coagulated by heat.

● When custards are baked, the proteins denature by

gradually unwinding from their tertiary structure to
their secondary structure.
MILK AND MILK PRODUCTS
● Then the denatured egg proteins coagulate to form
a gel structure by cross-linking as hydrogen and other
2 Major Proteins in Milk
secondary bonds form to establish a continuous
network of protein molecules. 1. WHEY
PROTEINS PRODUCT 2. CASEIN
Egg yolk and egg white Hollandaise, Cooked
Salad Dressings The reason for this distinction is evident when the pH
Milk protein (casein) Cheese of milk is adjusted to 4.6, for at this acidity, casein is
Soy protein Tofu quite insoluble and precipitates readily to form a soft
curd, which can be separated from the remaining
liquid (whey) by cutting and draining the casein curd

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 WHEY CASEIN ○ These designations are confused a bit by the finding
● 20% milk protein ● 80% milk proteins that one of the lactalbumins is called b- lactoglobulin.
● a watery mixture ● Insoluble Whey proteins are sensitive to heat.
● contains lactose, ● colloidal
some minerals, and suspension; WHAT ARE THE DIFFERENT MILK PROCESSING
water-soluble hydrophobic
PASTEURIZATION
vitamins. ● Denatured by
● Denatured by heat acid/enzyme HOMOGENIZATION
● Precipitate readily
and form a soft curd EVAPORATION

DRYING
WHAT CAN BE USED TO PRECIPITATE CURD?
FERMENTATION
● CURD FORMATION - Acid or rennin

● Rennin PASTEURIZATION

the proteolytic enzyme in the stomach lining of ● heated to kill potentially harmful microorganisms.
calves, destabilizes casein micelles in quite a different
● Destroys 95-99% of pathogenic bacteria; increases
way.
shelf life; combination of heat and time minimizes
○ This enzyme (also called chymosin) splits off the breakdown of vitamins and protein
hydrophilic portion of k-casein that was primarily

responsible for the stabilizing effect of k-casein on the HOMOGENIZATION

surface of the casein micelles.
● mechanical process in which milk is forced
● Rennet
through tiny apertures under a pressure ranging
a mixture of rennin and similar enzymes
from 2,000 to 2,500 psi
○ is substituted for rennin to clot milk.
● Prevents fat separation; performed mechanically;
○ Clearly, the two mechanisms—the alteration of the
fat is forced through small orifices at high pressure to
pH to approach the isoelectric point of casein and the
break up fat modules
use of rennin—are quite different, but both are
effective in precipitating casein. ● Fat globules become too small to coalesce - milk
can no longer cream;
WHEY
● proteins coagulate more easily - softer curd; richer
● The various caseins account for a little less than 80 texture; blander flavor; whiter; less heat stable; more
percent of the total protein in milk foamy
● The various whey proteins contribute the
remainder.

● whey proteins sometimes are categorized as either

lactalbumins or lactoglobulins.

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 EVAPORATION
● The large percentage of water in milk (just under 90
percent) contributes greatly to the bulk of milk that is
to be stored.
● Consequently, various canned milks are produced
by evaporation of enough of the water to about
double the concentration of protein and fat
● The milk is evaporated under a partial vacuum so
that water can be removed at a temperature well
below that required at normal atmospheric pressure.
● This process is of some help in minimizing the flavor
and color changes that would occur if the
temperature of evaporation were higher.
WHAT IS EVAPORATED MILK?
● Milk is homogenized;
● most of the free water is removed by evaporation;
● milk is canned and sterilized;
● reconstituted 1:1 with water;
● slightly tan in color due to Maillard reaction during
canning
WHAT IS SWEETENED CONDENSED MILK
● Most of the free water is removed by evaporation;
40-45% sucrose added
● milk is pasteurized then canned
● more extensive browning
FERMENTATION
● Uses microbes to ferment lactose into lactic acid;
● streptococcus lactis initiates the fermentation
process
● and various lactobacillus species
● careful sanitation to ensure only desired bacteria
are cultured
FERMENTATION PRODUCTS
Yogurt, buttermilk, kefir, cheeses
KEFIR- Kefir or kephir, is a fermented milk
drink similar to a thin yogurt or ayran that is
made from kefir grains, a specific type of
mesophilic symbiotic culture
MEAT
COMPOSITION OF MEAT
● Muscle Tissue
● Connective Tissue
● Adipose Tissue
● Bone
Muscle Tissue
Muscles are made up of a collection on individual
muscle cells, called” muscle fibers” that are each
surrounded by an outer membrane called
“sarcolemma”
Each muscle fiber is in turn filled with cellular fluid
(sarcoplasm) containing about 2,000 smaller muscle
fibrils that serve as the contractile components of the
muscle fiber
Muscle Contraction and Relaxation
Muscle fibrils play an important role in muscle
contraction and relaxation
The muscle fibril is separated into segments called
sarcomeres, which are bordered by dark bands called
Z lines
The sarcomeres contain 2 proteins:
Actin (thin)
Myosin (thick), alternately aligned
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When muscle contraction occurs, actin and myosin
react repeatedly at specific sites to form actomysosin
crosslinks and the sarcomeres shorten When the
muscle relaxes. The actomyosin cross links are broken
,and the sarcomeres return to their relaxed length.
The energy for muscle contraction is provided by ATP
CONNECTIVE TISSUE
-a part of ligaments and tendons, and it also acts as a
glue that holds muscle cells together . Composed
primarily of a mixture of proteins and
mucopolysaccharides
TYPES OF CONNECTIVE TISSUE
COLLAGEN - The most abundant connective tissue
Tough and fibrous but converts to a gel when exposed
to moist heat.
ELASTIN – elastic qualities
RETICULIN - very small fibers of connective tissues
that form a delicate interlace around muscles cells
COMPOSITION OF MEATS
Effect of collagen in tenderness
▪Type and amount of connective tissues determines
tenderness or toughness and the best type of cooking
method
▪Cuts high in connective tissue are naturally tough
and needs to be properly prepared using techniques
that increases tenderness.
Effect of collagen in tenderness
Muscles used for movement are high in collagen but
generally tough than muscles like loin and rib areas
which gets less exercise.
▪Collagen increases as animal age (meat is tougher in
older animals)
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▪Less expensive, tougher meat requires slow, moist
heating at low temperatures to convert or hydrolyze,
the tough connective tissue to softer gelatin

▪Conversely, tougher cuts have more flavour than

tender one

Effect of elastin in tenderness

Less effect on cooking

Elastin – yellowish and rubbery- does not soften with

heating, should be removed before preparation if
possible (silver skin)

MARBLING/IMF

Effect of reticulin in tenderness

Less effect on cooking

ADIPOSE TISSUE

Serves as insulation under the skin

Padding in the abdominal cavity for sensitive internal

organs Well marbled meat- fetches a higher price

COVER FAT - Fat outside the meat
- helps retain moisture of meats
- Often trimmed from meats
Intramuscular fat (IMF) or Marbling
- Fat found in the muscle
- a month or weeks before slaughter, some are
fed with richer grain
- uses hormone – medroxyprogesterone
acetate – to speed up fattening
Lower fat meat
- recent technique uses growth hormone
somatotropin which results to lower animals

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 FAT COLOR AND TEXTURE MARROW

Age, diet and species affect color and texture of fat ▪Soft, fatty materials in the center of most large
bones
- white in younger animals
- turns progressively more yellow as the animal ▪Yellow and red marrow
age
▪yellow in long bones
- due to the presence of carotenoid pigments
in the feed. ▪Red in short bones
Feedlot - provide swine with fats that are primarily ▪Marrow provides much of the flavor in soups
saturated

- yield pork fat that is more saturated and hard

Including polyunsaturated fat in the diet will makes it

fat softer

Species and breed influence softness of fat

BONES

Use as landmarks for identifying meat cuts

BONES IDENTIFY RETAIL CUTS OF MEAT

CUT BONE
SHOULDER
ARM

PIGMENTS
SHOULDER
BLADE PIGMENTS
RIB - The higher the concentration of myoglobin in
raw meat, the more intense is its bright red
color
- More exercised have redder color – due to its
high demand of oxygen – higher in
SHORT myoglobin
LOIN - Red color increase as the animal ages, beef is
redder than veal

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 ▪Vacuum wrap which eliminates the oxygen causes
the meat to appear purplish red (oxygen is not
present)

Pigment Oxygen Color

Deoxymyoglobin Protected Purplish
from contact red
with air
Oxymyoglobin Presence of Bright red
air color
Metmyoglobin Oxygen is Brownish
limited red
Exposed to pigment
fluorescent
PIGMENTS varies according to age or
incandescent
✔Mutton is darker that the pink hue of lamb
for too long
Varies also from species to species

✔Beef is darker than lamb,

✔Darker than pork

✔Fish and poultry- pigmented lightly

■ Hemoglobin contributes to the light coloration of Effect of Heat on Color

poultry
Cooking meat initially converts the color of raw meat
Some fish are deeply pigmented with myoglobin to bright red

Salmon- carotenoid pigment or asthaxanthin Denaturing the pigment –containing proteins yields
the classic color of well-done meat- grayish brown
Effect of oxygen in color
Storing too long- causes denatured protein to break
Exposure of meat to oxygen changes color of down further, causing meat to turn yellow, green or
myoglobin faded
After slaughter- meat undergoes several changes in
color over time due to modifications in the molecular
structure of myoglobin and haemoglobin

▪ After a while, meats left in storage may be exposed

to bacteria or less oxygen or kept under flourescent
or incandescent- turn meat brownish red (very low
oxygen)

▪ Using plastic wrap that is permeable to oxygen

allows meat retailers to maintain to bright red color
for a longer period of time

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 PIGMENT IN POULTRY and FISH POSTMORTEM CHANGES

● Hemoglobin contributes to the light coloration in Fish – begin to develop rigor mortis an hour before
poultry. being killed

● Quite a few vertebrate fish have two muscles—a - Onset maybe delayed for up to 7 hrs / iced
light-colored, large lateral muscle and a less desirable
- Bacterial spoilage commences after rigor mortis
dark muscle deeply pigmented with myoglobin.
Meat- some meat need to be aged 11 days before
● The lateral muscle in salmon derives its unique achieving tenderness
color from the presence of astaxanthin, which is
- Meat tenderness due to action of cathepsisn and
classified as a carotenoid pigment
calcium activated factor ( proteolytic enzymes)
○ present also in cooked crustaceans
- Break actomyosin linkage
FISH AND POULTRY
MEAT TENDERIZERS
● Essentially colorless when cooked
Artificial Tenderizing
● When poultry is cooked frozen- hemoglobin leaked
from the bone marrow- there is hemoglobin in the ✔Enzymes
flesh that is closed to the bone- dark when cooked
✔Salts
● Poultry- subjected to intense heat develops a
✔Acids
reddish pink color – hemoglobin reacts with carbon
monoxide and nitric oxide generated by electric ✔Mechanically Tenderized Beef
heating elements or flames- BBQ

Enzymes
Changes Effected during curing: •Enzymes are not active at room temperature

•Papain – optimum activity is at 131- 170F ( 55-76C)

– HEATING

■ Exceeding to 185% degrades the enzymes – inhibits

activity

•Bromelain- inactivated between 77 to 82C ( 170-

180F)

■ Fresh pineapple only

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SALTS
Addition of salts in the form of potassium, calcium
and magnesium chlorides
Retains moisture and breakdown the component that
surrounds the muscle fibers-release of proteins
Polyphosphate is also added – juiciness,water
retention, firmness, emulsion stability and anti
microbial
Enzymes are proteins, heat must be controlled to
prevent denaturing the protein and halting its
enzymatic function.
– TRUE
When proteins are subjected to stresses, particularly
heat, agitation, and ultraviolet light, they may
undergo modifications that result in decreased
solubility or loss of ability to catalyze reactions (if the
protein is an enzyme).

ACIDS Tofu is transformed by precipitating the egg whites

protein
•Using marinades
– FALSE
•- vinegar - fermented milk
Protein molecules may undergo hydrolysis to form
•- wine shorter chains.
•- lemon juice – TRUE

•-tomato juice Elastin is the most abundant connective tissue in

meat?
•-Fruit juice – FALSE COLLAGEN

MECHANICALLY TENDERIZED BEEF Milk is mostly ______ fat?

– SATURATED
•Grinding
What pasteurization allows you to not refrigerate the
•Cubing
milk until after opening?
•Needling
– UHT
•Pounding
Ultrahigh temperature -quickly heated to 138°C
(280°F), held there for at least 2 seconds, and then
TRUE OR FALSE stored in a sterile container

Many of the proteins in foods are globular proteins
– TRUE
The tertiary structure of protein is modified when
they undergo denaturation and coagulation
– TRUE
During denaturation, protein molecules relax from
their tertiary state and begin to resemble more closely
their secondary helical structure without distortion
What enzyme is tested for to determine if
pasteurization is complete?
– Alkaline phosphatase
is inactivated when milk is heat-treated adequately to
destroy potentially harmful microorganisms; thus,
testing for the presence of active alkaline
phosphatase can determine the adequacy of
pasteurization

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