Conversion of Muscle to Meat

• Prerigor state
– Muscle tissue is soft and pliable
– Characterized by a fall in ATP and creatine phosphate levels , as well as
by active glycolysis
– Postmortem glycolysis results in conversion of glycogen to lactic acid
causing the pH to fall
– Extent of pH change varies from one species to another as well as
among different muscles
– In well fed ,rested animals , the pH value fall from 7.2 to around 5.2
– Ultimate pH (pHU) varies between muscle and also the pattern of
acidification
 Post-mortem acidification

ANIMAL Acidification period

pig 4-8 hours
sheep 12-24 hrs
cattle 15-36 hrs
Poultry (turkey) 10 -15 minutes
Relationship between (a) initial glycogen and (b) final lactate and
ultimate pH in the longissimus dorsi of ox
 Effect of acidification
• Muscle protein tends to denature as pH falls
• Myofibrillar proteins reach their isoelectric pH
• Leads to exudation of fluid from muscle fiber
– When meat is cut the fluid also exudes on to the
cut surface and can cause in weight loss
• There is increase in the light scattering
properties of the contractile elements of the
muscle fiber
– Meat changes from relatively dark and
transluscent to being opaque and paler in color
 Development of Rigor Mortis
• Development of the stiff and rigid condition in the
muscle
• Occurs as the pH falls w/c is associated with the
formation of actomyosin
• Loss of extensibility associated with the formation of
actomysosin
 As rigor develops after slaughter, carcass muscles
may be stretched or contracted, depending largely
on their position in the hanging carcass

 Relaxed muscles produce meat that is more tender

than that from contracted muscles
 Post Rigor
• muscle gradually tenderize also called resolution of
rigor
– Myofibrils become fragmented
• becomes organoleptically acceptable
 Meat tenderization
• Conditioning –term applied to natural process
of tenderization of meat during ageing
– Structural weakening of intramuscular connective
tissues (slow)
– Change in the myofibrillar component
• Important enzymes
– Cathepsins
– Calpains
 Meat tenderization
• Cathepsins – lysosomes in the sarcoplasm
– Important in post mortem degradation of fish
muscle and in tenderization that occurs in meat
at high temperatures
– Released post mortem
– Have maximum activity in mildly acid conditions
– Degrade troponin T some collagen cross liknk and
mucopolysaccharides of the connective tissues
– They degrade actin and myosin at below pH 5
(unlikely to occur under normal meat condition)
 Meat tenderization
• Calpains - calcium activated sarcoplasmic
factor
– Activated by calcium ions
– Maximum activity in neutral to alkaline condition
– Active at high temeprature
– Catalyse the hydrolysis of desmin w/c links the
myofibrils together and troponin T
– Activity results to weakening of the Z lines as well
as disappearance of the M lines
 Factors Affecting Biochemical
Changes
• Genetics
– Genetic type –content and less backfat
• Breeding strategies focus on increases growth rate ,
lean meat
• Difference in tenderness between cattle breeds
– Steaks from an Angus breed are more tender than steaks
from 2/2 Angus-1/2 Brahman breed
– Difference in the activity proteolytic enzymes, like calpains
that are involved in the degradation of Z-line proteins have
major role in the tenderness differences between breeds
Factors Affecting Biochemical Changes
– Genes
• RN allele or the Napole gene common in the Hampshire
breed of pigs – has high glycogen content and extended pH
decline
– Has leaner meat and better eating quality in terms of tenderness
and juiciness
– The processing industry i reject this because most pork meat
gives low technological yield
• Halothane gene – in stressed susceptible pigs (porcine stress
syndrome (PSS)
– Pigs are very excitable during transport and change in
environmental situation
– Has higher carcass yield and leaner meat (advatageous to
farmers)
– Has higher percentage of PSE with high drip loss , poor color and
deficient technological properties
 Factors Affecting Biochemical Changes
• Age and Sex of animal
– Intramuscular fat content increases w/ age of animal
– Meat tend to be more flavorful and colorful due to
increased concentration of volatiles and myoglobin
– Muscle proteolytic and lipolytic activity are affected
• Muscles from heavy pigs have more peptidase to proteinase
ratio and higher lipases
– Meat from burrows contain more fat than gilts
– Meat from males have odor problems due to high
content of nadrostenone or escatol
 Factors Affecting Biochemical Changes
• Type of feed
– PUFA composition towards lower n-6:n-3 ratio
• Fats w/ higher PUFA have lower melting points that affect the fat firmness
• Softer fats may raise problems during processing if the integrity of the
muscle is disrupted by any mechanical treatment
• major troubles are related to oxidation , generation of off-flavors
during heating and color deterioration
– Rate and extent of oxidation of muscle foods mainly depends on the level of
PUFA
– An alternative for effective protection against oxidation is the addition of
natural antioxidants like vitamin E
– Antioxidant also improve color stability in meat by protection of myoglobin
against oxidation
– Fatty acid of ruminants is more saturated than pigs thus fat is firmer
– Good level of nutrition increase the amount of intramuscular fat
– Fasting within 12-15 hours pre slaughter usually reduce the risk
of microbial cross contamination during slaughter
 Meat Color
• Meat color is the initial impression a
consumer gets of a product
• Color has major impact on purchase decision
• Color is dependent on :
– Pigment content
– Ultimate pH
– Rate of pH decline postmortem
– Physical characteristics of muscle
 Meat Color
• Pigments in meat
– Hemoglobin and myoglobin
– Majority of color due to myoglobin
– Color reactions similar for both pigment
– Hemoglobin (MW 67,000)
• Four heme molecules and 4 globin proteins
Myoglobin
MW 16,000, Sarcoplasmic protein
􀁡 Iron porphyrin compound with
globin moiety attached

􀁡 Iron has 6 bond orbitals, four

covalently attached to four nitrogen
of the porphyrin ring structure,
one attached to a globin protein

􀁡 The 6th bond orbital is open for

formation of complexes with
several compounds

􀁡 Oxidation state of iron and

chemical occupying the 6th orbital
determine color of meat.
 Color Reaction

Immediately after cutting, meat color is quite dark - beef would be a deep purplish-red.
As oxygen from the air comes into contact with the exposed meat surfaces it is
absorbed and binds to the iron. The surface of the meat blooms as myoglobin is
oxygenated. This pigment, called oxymyoglobin, gives beef its bright cherry red color. It
is the color consumers associate with freshness.
.
 Color reaction
Myoglobin and oxymyoglobin
have the capacity to lose
an electron (called
oxidation) which turns the
pigment to a brown color
and yields metmyoglobin.
• Myoglobin can change
from a dark purple color to
a bright red color simply
from oxygenation or to a
brown color by losing
electrons.
Fresh Meat
Color
Reactions
 Effect of Meat pH

•If the pH does not drop postmortem, the meat will be dark
•The color changes observed with PSE (Pale Soft Exudate) and DFD (Dark
firm, Dry) meat are mostly due to structural changes in muscle
,
 Pale Soft Exudate (PSE)
• Caused by rapid drop in pH to 5.3-5.8 within 1
hour postmortem at high temperature
• Protein denaturation occurs at low pH w/c
lower the water holding capacity of the
muscle protein
• Meat has pale color, abundant drippings and
loose texture
 DFD
• DFD beef exhibits a dark, purplish red
to almost black lean color and a dry,
often-sticky lean surface
• Due to high pH, lean surfaces act
similarly to a dry sponge resulting in
increased water binding capacity
within the muscle.
• The muscle appears dark because
of higher intracellular water, which
reflects less light
• Changes in protein changes alter
the spacing between the fibers
of the meat, and this affects how
light is reflected and absorbed
and thus affects the visual
appearance
 Color Stability
• High ultimate pH affects enzyme activity and
the rate of myoglobin oxygenation.
• 􀁡The dry surface of DFD meat inhibits the
penetration of oxygen into the meat and thus
slows down the oxygenation process.
• 􀁡The length of time the meat has been
stored postmortem affects the color stability
of the meat or meat product
 Color Stability
􀁡Increased time from slaughter results in reduced
color stability because co-factors necessary for
the reduction of metmyoglobin are depleted as
postmortem time increases.
• 􀁡 Color acceptability decreases as storage time
increases; however, the length of time the color
is acceptable is greatly affected by storage
temperature.
• 􀁡Fresh meat and mea t products should be
stored at -1.5O C to give maximum color shelf-
life and safety of the products
 Color Stability
• Particle size reduction & mixing
– More air is incorporated into meat product
helps maintain oxymyoglobin pigment stability
– Longer mixing times and smaller mean
particles result innshorter color shelf-life for
meat products
– Use of vacuum mixers helps to improve color
stability , but will not completely bring the
stability back to what is expected in whole
muscle
 Cooked meat Pigment
• During the cooking process, myoglobin is
denatured.
• All of the pigment is not affected at the
same time or to the same extent and this is
why you get reddish color at dfferent end
point temperatures when cooking.
• The cooked pigment is denatured
metmyoglobin.
• Certain meat conditions can result in
protection of the myoglobin.
• The ultimate pH of meat or meat products
will affect how the meat color changes
during cooking.
• If the meat has a high pH, it wll have to be
cooked to higher end-point temperatures to
get the same visual degree of doneness as
one with normal pH.
 Cured meat
•Nitrite dissolve in water forms
nitrous acid and nitric oxide
•Reacts with meat by rubbing or
injection
• Combines with myoglobin to form
nitric oxide myoglobin
•Meat become stable after cooking
when nitrosylhemochrome , the
final cured pigment is formed
 Pinking of uncured Cooked Products
• Pink color can also be formed in slow cooked
meat products that have not been
contaminated with nitrite
• It is caused by specific conditions that
promote interaction of natural pigment and
nitrogen containing constituents of meat
• Naturally occuring nitrates in water, vegetable
and some ingredients can also cause pinking
of meat (usually in soup or stew0
 Preservation of Meat Pigment
• Store or pack meat under oxygen –enriched
atmosphere
– Oxygen level higher than normal preserve
oxymyoglobin
– Problem: development of fat rancidity
– Solution : use of anti oxidants
• Combination of CO2 and oxygen
– CO2 inhibit spoilage bacteria; oxygen maintain
oxymyoglobin pigment
• Storage in under CO2 or nitrogen