蛋白质水解
蛋白酵素
卡尔帕因
温柔
肌原纤维
肉的嫩度
蛋白水解酶
生物
半胱氨酸蛋白酶
结缔组织
细胞生物学
生物化学
细胞凋亡
化学
食品科学
酶
遗传学
程序性细胞死亡
出处
期刊:Meat Science
[Elsevier]
日期:2012-11-01
卷期号:92 (3): 252-259
被引量:144
标识
DOI:10.1016/j.meatsci.2012.03.013
摘要
Meat tenderness is considered to be one of the most important attributes of meat quality; however it is also one of the most variable. Ultimate meat tenderness is influenced by the amount of intramuscular connective tissue, the length of the sarcomere and also the proteolytic potential of the muscle. Post-mortem proteolysis by endogenous proteases causes the weakening of myofibril structures and associated proteins, which results in tenderisation. The caspase proteolytic system was first identified to be a potential contributor to post-mortem proteolysis and tenderisation in 2002. Since then research has both supported and challenged this hypothesis. The purpose of this review is to examine the experimental evidence available for caspases' involvement in post-mortem proteolysis, and to highlight cross-talk between this proteolytic system and the calpain system, a known contributor to meat tenderisation.
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