摘要
钙蛋白酶(calpain)是与肉嫩度相关的重要内源性蛋白酶之一,广泛存在于细胞质中,且需要一定量的Ca2+激活。研究表明,钙蛋白酶在Ca2+的激活下能降解肌原纤维蛋白,从而改善肉品嫩度。但是,由于钙蛋白酶抑制蛋白(calpastatin)等因素对钙蛋白酶活性的抑制作用,钙蛋白酶的活性调节成为一系列高度可调的复杂过程。在综述钙蛋白酶结构与功能关系的基础上,进一步阐述了钙蛋白酶的活性调节如何影响肉品嫩度。
Calpain is one of the important endogenous proteases which correlate meat tenderness. It consists in cytoplasm and needs certain Ca^2＋ to activate. It is approved that Calpain activated by Ca^2＋ can degradaie 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.
出处
《食品科技》
CAS
北大核心
2007年第12期115-118,共4页
Food Science and Technology
基金
甘肃省教育厅项目(0502-01)
