Key Laboratory of Meat Processing and Quality Control, Ministry of Education China, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Key Laboratory of Meat Processing and Quality Control, Ministry of Education China, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Food Chem. 2011 Sep 1;128(1):22-7. doi: 10.1016/j.foodchem.2011.02.062. Epub 2011 Feb 18.
The objective of this study was to investigate the potential contribution of caspase-3 to meat postmortem tenderisation by examining the role of caspase-3 in the degradation of myofibrillar proteins and disruption of myofibril structure in vitro. Myofibrillar protein prepared from chicken muscle was incubated with EDTA or EDTA plus caspase-3 at 25°C for 16h and used for detecting muscle protein degradation and ultrastructure of myofibril. Results revealed that caspase-3 reproduced the degradation patterns of titin, nebulin and α-actinin during postmortem storage of meat, but caused little proteolysis of desmin and no appearance of 28-30kDa peptides. Meanwhile, caspase-3 also induced the weakening in the I band adjacent to Z-lines, which occurred during meat postmortem ageing. Therefore, caspase-3 could account only for a part of the myofibrillar protein degradation observed in naturally aged meat and is likely involved in postmortem tenderisation of meat together with other endogenous proteases.
本研究旨在通过研究 caspase-3 在肌原纤维蛋白降解和体外肌原纤维结构破坏中的作用,探讨 caspase-3 对肉品宰后嫩化的潜在贡献。从鸡肌肉中提取肌原纤维蛋白,用 EDTA 或 EDTA 加 caspase-3 在 25°C 下孵育 16 小时,用于检测肌肉蛋白降解和肌原纤维的超微结构。结果表明,caspase-3 复制了肉品宰后贮藏过程中肌联蛋白、nebulin 和 α-辅肌动蛋白的降解模式,但对结蛋白的水解作用很小,也没有出现 28-30kDa 肽段。同时,caspase-3 还诱导了 I 带在 Z 线附近的弱化,这发生在肉品宰后老化过程中。因此,caspase-3 只能解释部分自然老化肉中观察到的肌原纤维蛋白降解,并且可能与其他内源性蛋白酶一起参与肉品宰后嫩化。