离体条件下牛肉的嫩化机制(英文)  

The Mechanism of Beef Postmortem Tenderization in vitro

作　　者：黄明[1] 王俊[1] 徐幸莲[1] 周光宏[1] 

机构地区：[1]南京农业大学农业部农畜产品加工与质量控制重点开放实验室,江苏南京210095

出　　处：《江苏农业学报》2003年第4期242-245,共4页Jiangsu Journal of Agricultural Sciences

基　　金：Ministryofeducationfordoctoralprogramme(GrantedNo 2 0 0 2 0 3 0 70 0 6) ;NaturalsciencefoundationofJiangsuprovince(BK 2 0 0 3 0 78)

摘　　要：　基于有关牛肉嫩化机制的钙激活酶、Ca++、溶酶体组织蛋白酶理论,本试验模拟尸僵后牛肉的内在环境和成熟温度,将纯化后的钙激活酶I、钙激活酶I内源性专一抑制剂、肌原纤维和钙激活酶I外源性抑制剂抑亮酶肽用于6个不同的处理组合,反应不同时间后,分别做变性聚丙烯酰胺凝胶电泳和蛋白质印迹分析。结果表明,在含100μmol/LCa++的反应体系中,钙激活酶I对肌间线蛋白和肌钙蛋白T有明显的降解作用,且降解产物和宰后牛肉自然成熟条件下的降解产物类似;钙激活酶I内源性专一抑制剂不能完全抑制钙激活酶Ⅰ的活性。100μmol/LCa++单独存在时对肌间线蛋白和肌钙蛋白T无降解作用,但很可能通过激活钙激活酶I间接发挥对肌原纤维的降解作用。Based on theories of calpain system and calcium about tenderization mechanism for beef, purified μcalpain, calpastatin, myofibrils and leupeptin were used in six different reaction mixtures. After incubation for different time at 4℃ in mixed salt solution formulated on the basis of the postrigor beef muscle composition, SDSPAGE and Western blotting were conducted. The results showed that calcium (100 μmol/L) had no effects on myofibrils, while μcalpain, when incorporated with calcium, could degrade desmin and troponin T and the degraded products were similar with those of aged beef. Calpastatin was not capable of inhibiting μcalpain activity completely. These results indicated that it was most possible μcalpain degraded cytoskeletal proteins when activated by calcium, and as a result, improved beef tenderness. 

关 键 词：离体条件 牛肉 嫩化机制 环境条件 成熟温度 纯化 反应体系 

分 类 号：TS251.52[轻工技术与工程—农产品加工及贮藏工程]