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of muscle, the fi ndings of proteomic studies
on postmortem muscle suggest that meta-
bolic enzymes and other water - soluble pro-
teins within muscle may be potentially useful
as markers for meat tenderness. With the
limited number of proteomic - based and high -
resolution studies on aged muscle, however,
it is still unclear if the protein changes
observed during postmortem storage play a
mechanistic role in aging tenderization or if
they are simply indicators of proteolysis.
Conclusions
In summary, we can state that skeletal muscle
is a product of exceedingly structured and
oriented proteins containing numerous
enzymes that drive various metabolic path-
ways in the living tissue and is destined to
undergo a variety of changes after death.
Dramatic changes take place both during
chilling and aging but most markedly during
the immediate postmortem period as muscle
is transformed to meat. The subject of utmost
importance in the minds of many is where do
we go from here in research on quality and
palatability of meat? Postmortem aging is a
process that occurs naturally in all muscle
tissues, whether vacuum packaged or in the
form of carcasses or wholesale cuts. In the
conversion of muscle to meat, postmortem
aging of carcasses and cuts is a natural
process that usually improves tenderness
under refrigerated conditions. Endogenous
enzymes found in muscle cells fragment key
proteins in such a way that the fundamental
integrity of the muscle ultrastructure is
altered, resulting in improved meat tender-
ness. Although postmortem aging has a pro-
found effect on meat tenderness, it does not
ensure total and uniformly tender meat.
Aging tenderization of meat is a complex
phenomenon with numerous factors (both
antemortem and postmortem) that infl uence
the underlying enzymatic mechanisms.