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Studies in Meat Tenderness. 6. The Nature of Myofibrillar Proteins Extracted from Meat During Aging
Author(s) -
DAVEY C. L.,
GILBERT K. V.
Publication year - 1968
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1968.tb03627.x
Subject(s) - myofibril , tropomyosin , myosin , tenderness , chemistry , actin , meat tenderness , myofilament , biochemistry , biophysics , food science , biology
SUMMARY– A study has been made of the myofibrillar proteins extracted from beef and rabbit meat by a buffer that dissociates the actomyosin complex of the muscle cell. Myosin, which constitutes 50‐52 per cent of the myofibrillar protein, can be wholly extracted throughout aging, whereas actin can be extracted in increasing amounts as aging proceeds. In contrast, tropomyosin cannot be extracted and remains firmly held within the myofibrillar structures throughout aging. A complex mixture of extra protein, soluble at low ionic strength, is also released in increasing quantity during aging. It is proposed that in meat aging there is a progressive loss of the tensile strength of the myofibrillar component of muscle brought about by the weakening and final dissolution of the Z‐band structures. Such a disintegration would lead to the observed changes in the extractabilities of the myofibrillar proteins.