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Aseptic autolysis in rabbit and bovine muscle during storage at 37°
Author(s) -
Sharp J. G.
Publication year - 1963
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740140704
Subject(s) - autolysis (biology) , sarcoplasm , myofibril , chemistry , biochemistry , aseptic processing , muscle protein , cathepsin , andrology , chromatography , food science , endocrinology , biology , skeletal muscle , enzyme , endoplasmic reticulum , medicine
The changes in a number of protein fractions in rabbit and bovine muscle have been observed during aseptic storage at 37°. Continuous breakdown of protein took place with formation of TCA‐soluble non‐protein N, the rates being 20.7 μmoles and 10.3 μmoles N/g./day for rabbit and beef respectively. No change was detected in the solubility of the collagen fraction over 6 months' storage. The fine structure of the myofibrils remained apparently unchanged during this period and the main autolytic effect of the cathepsins present would appear to be concentrated on the sarcoplasmic proteins. The degree of disintegration of muscle structure caused by homogenisation under standard conditions was much greater in muscle held for 30 days at 5° than in muscle after the same period at 37°.