사후 저장기간에 따른 계육 근원섬유단백질의 추출성과 분해도

초록

The pH value of both muscle stored at 4oC gradually fell during postmortem storage and that of breast and leg muscle reach to 5.9 and 6.0, respectively. While, that of the chicken muscle stored at 30oC decreased rapidly from 6.8 to 5.6 in breast muscle and 6.9 to 5.7 in leg muscle. After 4oC 8 hours of slaughter, ultimate pH value was attained. No apparent change was observed in the extractability of myofibrillar proteins during 12 hours of storage at 4oC and the first 2 hours of storage at 30oC But, after 2 hours of postmortem storage at 30oC the extractability decrease rapidly. The change occuring in the myofibrillar protein of both muscle during postmortem storage was the gradual degradation of troponin T. The relative weight of troponin T in the myofibrillar proteins extract decreased during postmortem aging. Myofibrils from pectoralis major and adductor longus muscle aged at 30oC (higher storage temperature) illustrated the disapperance of troponin T are caused by the action of endogenous proteolytic enzymes during the storage of the chicken meat. 30,000 dalton component from chicken muscle during the postmortem storage at 4oC and 30oC, it was observed that there was a simultaneous increment of a 30,000 dalton component during postmortem storage in myofibrils isolated from leg and breast muscle. the change occuring in the myofibrillar proteins of chicken muscle during postmortem storage was the gradual degradution of troponin T and the increment of the 30,000 dalton component.

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