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Chapter 5
Quality
Chapter 6
Chapter 7
Chapter 8
Chapter 9
Chapter 10
Chapter 11
Chapter 12
Chapter 13
Chapter 14
Chapter 15
Chapter 16
Tables 5.2 Summary of changes that occur in skeletal muscle during postmortem
aging
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 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
another.
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.
CONTRACTION PHASE
Resting state
RELAXATION PHASE