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Meat Science

Chapter 5

Conversion of Muscle to Meat and Development of Meat

Chapter 6

Properties of Fresh Meat

Chapter 7

Principles of Meat Processing

Chapter 8

Microbiology and Deterioration of Meat

Chapter 9

Storage and Preservation of Meat

Chapter 10

Retail Meat Merchandising

Chapter 11

Meat for Food Service

Chapter 12

Palatability and Cookery of Meat

Chapter 13

Nutritive Value of Meat

Chapter 14

Meat Inspection and Food Safety

Chapter 15

Meat Grading and Evaluation

Chapter 16

By-products of the Meat Industry

Tables 5.2 Summary of changes that occur in skeletal muscle during postmortem

1. Z disk degradation, which leads to weakening and fragmentation of

2. Degradation of desmin, which causes disruption of transverse cross-linking
between myofibrils and leads to fragmentation of myofibrils.
3. Degradation and disappearance of troponin-T. Because of its location in
myofibrils,the exact relationship between meat tenderness and troponin-T
degradation is not yet understood.
4. Degradation of titin and nebulin. Because of their ability to maintain
longitudinal stability of myofibrils, disruption of these structures would
lead to fragmentation of myofibrils.
5. Degradation of these myofibrillar proteins results in appearance of new
polypeptides of 95,000 and 28,000 to 32,000 molecular weight as seen by
polyacrylamide gel electrophoresis.
6. Perhaps the most significant observation is that the major contractile
proteins, myosin and actin, are not affected even after 56 days of
postmortem aging.
Sources : Gool et al. (1983), Robson and Huiatt (1983), Koohmaraie (1992) and
Robson et al. (1997).

Qualify as the active participant, the enzyme(s) must degrade the same
myofibrils proteins that are degraded during postmortem storage of meat as
shown in table 5.2. the multicatalytic proteinase complex does not cause
postmortem proteolysis of any myofibrillar protein that plays a role in improving
meat tenderness. Evidence indicates that the cathepsins are not released from
lysosomes even after electrical stimulation and extended postmortem storage.
Without their release, these enzymes cannot degrade myofibrillar proteins. The
proteins would have to be endocytosed into lysosomes for proteolysis to occur as
is the case in living muscle, but this is impossible in postmortem muscle because
endocytosis is an active process requiring energi. Of these three enzyme
systems, the calpains produce all of the proteolytic changes in myofibrillar
proteins during postmortem storage presented in table 5.2. the calpain system
consists of two calcium-dependent enzymes, and a specific inhibitor, calpastatin.
The two enzymes of this system differ in their calcium requirement for activation.
One calpain requires milimolar calcium (m-calpin) and the other, micromolar
calcium (u-calpain) concentrations for activation. Calcium released from
mitochondria and the sarcoplasmic reticulum during postmortem storage
activates the calpains.
Evidence is rather convincing that calpains are the enzymes accountable
for the proteolytic changes in postmortem muscle. Infusion of calcium into
carcasses or meat increases meat tenderness and produces all of proteolytic
changes presented in table 5.2. in contrast, when a chelator of calcium infused
to tie up calcium ions, none of the proteolytic changes occur and tenderness is
not improved. Compared with the calpain system, however, neither the
multicatalytic proteinase complex nor the cathepsins are affected by calcium.
Infusion of calcium into meat, especially beef, to improve tenderness is currently
receiving much attention in the industry.

The third component of the calpain system, calpastatin, which inhibits

calpain activity, varies in amount beef. Cattle whose meat tends to be tough
(bulls or those with Bos indicus breeding,

The process that establishes and maintains sodium and potassium gradients
across nerve and muscle fiber membranes. This pumps utilizes ATP as an energi
source and pumps calcium back into the sarcoplasmic reticulum where it is
stored in the terminal cisternae until release by a subsequent stimulus. The
calcium pumps is activated by increased cytolosic calcium. As free calcium
concentrations in the sarcoplasm decrease, cross-bridge formation is inhibited by
interaction of troponi I and tropomyosin with actin. In the absence of crossbridges, tension is not generated and the stretching imposed by elastic
components in the muscles causes the filaments to slide passively over one
Thus, calcium has multiple effects on muscle when released into the
sarcoplasm. First, calcium activates troponin, which shifts the conformation of
tropomyosin, exposes the myosin binding sites on actin, and allow cross-bridge
formation. Second, calcium activates myosin ATPase, which releases energi for
contraction. And finally, calcium stimulates the ATPase of the calcium pumps,
which pumps calcium back into the terminal cisternae to end the contraction.
Figure 4.7 is a flow diagram of the events that occur during a complete
contraction-relaxation cycle in skeletal muscle.


From the discussion presented to this point, it should be evident that ATP
is the ultimate source of energi for :
The contractile process
The pumping of calcium back into the sarcoplasmic reticulum during
Maintaining the sodium/potassium ion gradients across the sarcolemma.
Of these three uses of energi, contraction is by far the most energetically
demanding process. It has been estimated that, during a single muscle twitch,
contraction uses a thousand times more energi than does reversal of membrane
potential, and at least ten times more energi than does the calcium pump in teh
sarcoplasmic reticulum. Yet, the amount of ATP present in the muscle is sufficient
to supply energi for only a few twitches. Therefore, a very rapid and efficient
means must be available for resynthesis of ATP within living muscle.
When an animal is slaughtered, the muscle does not instantaneously stop
living and become meat. In fact, replenishment of ATP continues to provide
energi for all of the above muscle functions for some time after the initiation of
the harvesting process. Pathways that provide for ATP synthesis by

rephosphorylation (conversion of ADP to ATP) in the living muscle attempt to

maintain ATP levels after death. Postmortem boichemical reactions that occur as
muscle attempt to maintain these homeostatic conditions (stable equilibrium)
cause profound changes in muscle properties. These reactions constitute a major
part of the processes described as the conversion of muscle to meat in chapter
The most immediate source of energi that may be mobilized for ATP synthesis
is phosphocreatine. This is accomplished by the reaction :
ADP + phosphocreatine > ATP= creatine.
This reaction occur in the sarcoplasm, and the enzyme that catalyzes it is
creatine kinase. Therefore, ATP broken down during a contraction is rapidly
restored. Unless special precautions are taken to prevent ATP resynthesis from
phosphocreatine, the reaction occurs so rapidly that ATP breakdown during a
single muscle twitch cannot be measured; only phosphocreatine breakdown is
seen. Concentration of phosphocreatine in resting muscle is about twice that of
the resting level of ATP. Therefore, it also is subject to depletion during extended
periods of contraction and must be replenished during rest periods by other
mechanisms. Rephosphorylation of creatine occurs at the mitochondrial

Resting state

Motor nerve action potential arrives at motor end plate

Acetylcholine released, sarcolemma and membranes depolarized

(Na+ flux into fiber)

Action potential transmitted via T-tubules to SR

Ca2+ released from SR terminal cisternae into sarcoplasm

Ca2+ binds to troponin C

Tropomyosin shift from myosin binding site on actin

Actin-myosin crossbridge formation

Myosin ATPase activated & ATP hydrolyzed

Repeated Formation & breaking of crossbridge resulting in sliding of filaments

and sarcomere shortening


Cholinesterase released and acetylcholine breakdwon

Sarcolemma & T-tubules repolarized

SR Ca2+ pump activated & Ca2+ returned to SR terminal cisternae

Actin-myosin croosbridge formation terminated

Return of tropomyosin to myosin binding site on actin

Mg2+ complex formed with ATP

Passive sliding of filaments

Sarcomeres return to resting state

Figure 4.7
flow diagram of the events during a complete muscle
contraction-relaxation cycle.