2007Food Science and Technology InternationalRequires access

The function of activity regulation and the relationship between calpain and meat tenderness

Zhao Wen-bao

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Abstract

Calpain is one of the important endogenous proteases which correlate meat tenderness. It consists in cytoplasm and needs certain Ca2+ to activate. It is approved that Calpain activated by Ca2+ can degradate myofibrillar protein to improve meat tenderness. Nevertheless. Activity regulation of calpain becomes adjustive complex course in virtue of restrain on calpain activity by calpastatin.This paper reviews how activity regulation of calpain influence meat tenderness base on introducing the relationship between structure and function.

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What this paper is about

Calpain is one of the important endogenous proteases which correlate meat tenderness. It consists in cytoplasm and needs certain Ca2+ to activate. It is approved that Calpain activated by Ca2+ can degradate myofibrillar protein to improve meat tenderness. Nevertheless. Activity regulation of calpain becomes adjustive complex course in virtue of restrain on calpain activity by calpastatin.This paper reviews how activity regulation of calpain influence meat tenderness base on introducing the relationship between structure and function.

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Available abstract

Calpain is one of the important endogenous proteases which correlate meat tenderness. It consists in cytoplasm and needs certain Ca2+ to activate. It is approved that Calpain activated by Ca2+ can degradate myofibrillar protein to improve meat tenderness. Nevertheless. Activity regulation of calpain becomes adjustive complex course in virtue of restrain on calpain activity by calpastatin.This paper reviews how activity regulation of calpain influence meat tenderness base on introducing the relationship between structure and function.

Key concepts: Tenderness, Calpastatin, Calpain, Proteases, Myofibril, Meat tenderness, Chemistry, Food science

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