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Muscle to Meat Conversion Process

The document discusses the biochemical and biophysical changes that occur in muscle after the death of an animal, leading to the conversion of muscle to meat. Key processes include the depletion of oxygen, anaerobic glycolysis, and the onset of rigor mortis, which affects meat quality. It also highlights the importance of factors such as temperature and stress prior to slaughter in influencing postmortem changes and meat characteristics.

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0% found this document useful (0 votes)
16 views14 pages

Muscle to Meat Conversion Process

The document discusses the biochemical and biophysical changes that occur in muscle after the death of an animal, leading to the conversion of muscle to meat. Key processes include the depletion of oxygen, anaerobic glycolysis, and the onset of rigor mortis, which affects meat quality. It also highlights the importance of factors such as temperature and stress prior to slaughter in influencing postmortem changes and meat characteristics.

Uploaded by

diyabajaj2709
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

18-07-2025

Postmortem changes
&
Conversion of muscle to meat

Meat is the post-rigor aspect of muscle

The conversion of 'Muscle' to 'Meat'


Result of series of biochemical and biophysical
changes initiated in muscle at the death of the animal
due to stoppage of the blood circulation.

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➢ Immediate loss of oxygen supply to the muscle due to


bleeding as the stored oxygen in myoglobin gets depleted.
➢ As the Oxidation reduction potential is reduced, there is
inhibition of aerobic pathway through TCA cycle as
well as cytochrome system.
➢ The store of creatinine phosphate (CP) used for
rephosphorylation of ADP to ATP (creatine phosphate + ADP
= ATP + creatine) gets soon exhausted.

• Energy metabolism is then shifted to anaerobic


pathway resulting in the breakdown of glycogen to
lactic acid.

• This process continues till all the glycogen stored in the


muscle is exhausted or the ultimate pH is reached.

• This resynthesis of ATP by anaerobic pathway is not


enough to maintain the required ATP level and as it
depletes, there is formation of actomyosin resulting in
the onset of rigor mortis.

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1. Exsanguination/Bleeding
2. Loss of Homeostasis
3. Circulatory failure to the muscle
4. Postmortem Glycolysis and pH Decline
5. Rigor Mortis
6. Loss of Protection from Invading Microorganisms
7. Degradation due to Proteolytic Enzymes
8. Loss of Structural Integrity
9. Changes in the physical appearance of muscle

➢ Exsanguinations or removal of blood from animal body is


the first step in conventional slaughter practices.

➢ Exsanguinations marks the beginning of series of post


mortem changes in the muscle.

➢ Blood is a good medium for bacterial growth it is


necessary to remove maximum blood during bleeding.

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➢ Homeostatic mechanism, a system for the physiologically


balanced internal environment which helps the body to cope
up with the stresses of oxygen deficiency, extreme variation
in temperature, energy supply, blood pressure etc. is lost.
➢ The homeostasis is controlled by nervous system, which
ceases within 4-6 minutes after bleeding.
➢ In the absence of blood supply, there is loss of body heat and
temperature starts declining.

• Exsanguination eliminates the supply of nutrients,


oxygen and removal of metabolites from the muscle
i.e. virtually cut off muscle form its external
environment.
• Oxygen is stored in limited amount in myoglobin and
in living animals it is supplied to the muscle cells.
• After death stoppage of oxygen supply initiates
Anaerobic Glycolysis and the end products being
lactic acid.

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• Post Mortem glycolysis involves conversion of glycogen to


lactic acid under anaerobic condition accompanied by
reduction in pH from 7.2-7.4 to 5.4-5-6.
• Ultimate pH is the result to either lack of glycogen or
inactivation of glycolytic enzymes.
• The rate of PM glycolysis is increased by higher temperature,
initial glycogen store, influx of adrenaline and calcium ions.
• In the absence of oxygen, anaerobic glycolysis leads to the
formation of lactic acid from the glycogen reserves:

Anaerobic
Glycogen——————————  lactic acid + 2 ATP
Conditions

➢ The accumulation of lactic acid lowers down the muscle pH,


which is an important postmortem change during the
conversion of muscle to meat.
➢ The rate and extent of pH decline are variable being
influenced by the species of food animal, various pre-slaughter
factors, environmental temperature etc.
➢ In most species a gradual decline continues from
approximately pH 7.2-7.4 in the living muscle during first few
hours (5-6 hours) giving an ultimate pH in the range of 5.5
– 5. 7
➢ The rate of pH decline is enhanced at high environmental
temperature.
➢ A low ultimate pH is desired to have a check on the
proliferating microorganisms during storage.

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• A sharp decline in postmortem pH even before the dissipation of


body heat through carcass chilling may cause denaturation of
muscle proteins.
• So, the muscles depict pale, soft and exudative (PSE) condition.
• Contrary to this, muscles which maintain a consistently high pH
during postmortem conversion to meat depict a dark firm and
dry (DFD) condition.
• Both the conditions are undesirable.

✓ Sharp decline: PSE


✓ Consistently high pH: DFD

DFD Normal PSE

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Pale, Soft Exudative (PSE) muscle Dirk, Firm and Dry (DFD) muscle

Due to acute stress prior to slaughter Due to Chronic stress prior to slaughter

Rapid initial acidification Reduced glycogen

Low initial pH at high carcass High ultimate pH


temperature
Protein denature Proteins do not denature

Low water holding capacity High water holding capacity

Bound water lost Water held by proteins

Muscle fibers separate Fibers tightly packed

Large extra cellular space Small extra cellular space

Light scattering high Light scattering low

Surface appears pale Surface dark

Low pH promotes oxidation of Oxygen diffusion is inhibited by closed


myoglobin structure
Reduction in absorption of light by Oxygen is used by high cytochrome
myoglobin activity
Meat look less red Oxymyoglobin layer thin and underlying
myoglobin( purple) shows through

 It refers to stiffening of muscles after death and is another

important postmortem change.

 ATP complexed with Mg++ is required for breaking the

actomyosin bond and bringing the muscle to a relaxed state


and as it drops.

 Permanent actomyosin cross-bridges begin to form and

muscle gradually becomes less and less extensible under an


externally applied force.

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Most important post mortem change in muscle after the death of the animal. It
is characterized by :

• Hardening and contraction of all the muscles

• Loss of transparency of the muscle surface and loss of bloom

• Stiffening of joints

• Slight rise in the temperature ( about 1.50 C) followed by


decrease

Delay phase:
During the period immediately following exsanguination, the
actomyosin formation proceeds very slowly at first and the muscle is
relatively extensible and elastic.

Onset phase:
Then actomyosin formation picks up and the muscle begins to loose
extensibility. When all the creatine phosphate (CP) is depleted, ADP can
no longer be phosphorylated to ATP, muscle becomes quite inextensible
and stiff. This stage marks the completion of rigor mortis. When
postmortem pH decline is very slow or very fast, the onset and completion
of rigor mortis is rapid. The onset of rigor mortis is enhanced at ambient
temperature above 20°C.

Resolution of rigor:
The resolution phase of rigor mortis takes place due to enzymatic and
microbial degradation of muscle structure in due course of time. It causes
increased tenderness due to mechanical breaking of myofilaments.

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• Rigor mortis is irreversible under normal conditions.


• Pre-rigor meat is quite tender but its toughness keeps on increasing
until rigor mortis is completed.
• It continues to be tough for some more time.
• The resolution of rigor due to denaturation or degradation or
ageing, meat again becomes tender.
• The onset of rigor mortis is also accompanied by a decrease in
water holding capacity.
• Rigor mortis affects first the muscles that have been most active
and best-nourished prior to death e.g. heart.
• The rigor mortis commence from head , neck extending backwards
to involve body and limbs.

Species Delay phase Onset phase Resolution

Cattle Up to 6-7 hours 7- 20 hours 36 hours of


death

Sheep , goat Up to 3 hours 3- 8 hours 24 hours of


death

Pig Up to 4 hours 4-10 hours 26 hours of


death

Rabbit Up to 4 hours 4-19 hours 19-36 hours

Poultry Up to 40 minutes 40 min to 2 hours 12 hours of


death

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Advantages of rigor mortis in commercial trade

 Low pH prevents the microbial growth.


 lactic acid helps in conversion of collagen in to
gelatin hence increasing tenderness
 Improves flavour of meat on cooking.

Factors influencing speed of rigor mortis


 Temperature ( ambient temperature favours the development of
rigor mortis)
 Stress prior to death or handling of animals prior to death
 Glycogen content at the time of death
 Species
 Fat covering
1

• During postmortem period, body defense mechanism


stops operating and membrane properties are altered.
• So, during conversion to meat, muscle is quite
susceptible to invading microorganisms.
• Except for low pH, most of the other postmortem changes
favour bacterial growth.
• Hence, utmost handling precautions are necessary to
prevent contamination of meat.

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➢ Multicatalytic proteinase complex (calpains) and lysosomal


enzymes (cathepsins) which remain inactive in a living muscle
tissue, are activated as the muscle pH declines.
➢ These enzymes initiate the degradation of myofibrillar proteins.
➢ Disrupt the Z line structure (Titin & desmin).
➢ Actomyosin bond remains intact.
➢ Cause tenderization of meat during aging.
➢ Calpastatin is the inhibitor of calpains

• Postmortem alteration of membrane properties initiates


the degradation of muscular proteins.
• There is a progressive disruption of myofibrillar
structure.
• The resolution of rigor mortis is known to occur due to
disintegration of Z-line structure.
• A rapid decline in muscle pH also causes denaturation of
collagenous connective tissue.

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➢ Colour :- Denaturation of myoglobin results in change of color


form bright red to dark red or purple.
➢ Firmness:- Usual tone of muscle is lost and they show less
firmness or may become very soft due to protein denaturation.
➢ Water binding properties:- This depends on the changes in pH
and rate and extent of pH drop. In normal muscle water binding
capacity if retained up to 60-65%. While during sudden drop of
pH it is drastically reduced.

Death

No blood supply – no oxygen

Inactivation of aerobic pathways (TCA & ETC) to produce ATP


Stimulation of anaerobic glycolysis

Very less ATP production ( 2 ATP) as compared to aerobic glycolysis ( 37 ATP)


Conversion of pyruvic acid to lactic acid and reduction of pH

Formation of actomyosin ( rigor mortis)

Reaching ultimate pH ( 5.5-5.7)

Activation of autolytic enzymes (calpains / cathepsins)

Resolution phase of rigor mortis

Increase in tenderness due to mechanical breaking of myofilaments

Putrefaction ( if not stored properly )

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➢ Physiological responses during stress


Porcine stress syndrome as a result of general acidosis due to
circulation of excess of lactic acid
➢ Environmental elements
Temperature, humidity, light and space – these are the stressors
that lead to stress
➢ Stress and muscle characteristics
PSE (pale soft and exudative ) and DFD (Dark firm and dry)
➢ Animal production factors
Heritability, Diet and Growing environment
➢ Preslaughter handling
Transport and holding:- transport losses
Immobilization and bleeding :- imperfect bleeding

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