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A COMPARATIVE STUDY OF THE CHANGES IN HEN PECTORAL MUSCLE DURING STORAGE AT 4°C AND –20°C
Author(s) -
YAMAMOTO KATSUHIRO,
SAMEJIMA KUNIHIKO,
YASUI TSUTOMU
Publication year - 1977
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.1365-2621.1977.tb08446.x
Subject(s) - myofibril , tenderness , fragmentation (computing) , myosin , chemistry , myosin atpase , sarcomere , anatomy , pectoral muscle , troponin , myocyte , biochemistry , biology , food science , atpase , microbiology and biotechnology , enzyme , medicine , ecology , myocardial infarction
Evidence has been presented to show that myofibrillar fragmentation is the principal cause of the tenderness of poultry meat. Changes in actinmyosin interaction seems to play some role during frozen storage at −20°C. The changes in shear force and myofibrillar fragmentation of hen pectoral muscle during storage at 4°C and −20°C were studied, comparatively. The shear force values of postrigor muscle stored at 4°C and those of frozen muscle were about half of the fresh muscle values. Myofibrillar fragmentation in samples stored at 4°C was complete on 3rd day postmortem; whereas it proceeded gradually during storage at −20°C. Myosin heavy chain was degraded in frozen muscle samples, which in turn affected myofibrillar ATPase activity. 27,000 and 30,000 dalton proteins, possibly the degradation products of troponin, appeared in muscle samples stored both at 4°C and −20°C.