Author:
Hopkins D. L.,Thompson J. M.
Abstract
This review seeks to examine the current theories of tenderisation with
respect to red meat where tenderisation is defined as the reduction in
toughness post-rigor. This examination is in the light
of recent research on meat biochemistry, and from this, areas of research that
may prove fruitful are highlighted. Based on available data, the major
candidate to explain tenderisation post-rigor is the
calpain protease system. Evidence that change in the binding of actomyosin
(the complex of contractile proteins formed at rigor) or
cleavage of myofibrillar proteins due to Ca2+ ions
contributes to tenderisation is far from compelling. Equally it appears that
the cathepsin proteases are unlikely to have a role in early post-mortem
cleavage of proteins (proteolysis) and thus tenderisation. The mode of action
of the calpains is not yet fully defined and questions remain as to the role
of m-calpain given the in vitro requirement for a
Ca2+ ion concentration exceeding that observed in
post-mortem muscle. The existence of the calpains in
living muscle and other tissues suggests a mode of action more subtle than
currently thought. Additionally, the observation that the degradation of
myofibrillar proteins occurs in the presence of effective synthetic and
natural calpain inhibitors suggests that other enzymes may also have a role in
tenderisation. Inevitably, the accumulated evidence points to a complex system
likely to involve interacting proteases and ions, and only through open minded
investigation with reliance on developments in the medical and biochemical
fields will a more complete model of tenderisation be developed.
Subject
General Agricultural and Biological Sciences
Cited by
107 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献