Phosphorylation inhibits the activity of μ-calpain at different incubation temperatures and Ca2+ concentrations in vitro

被引：29

作者：

Du, Manting ^{[1
,2
]}

Li, Xin ^{[1
]}

Li, Zheng ^{[1
]}

Li, Meng ^{[1
]}

Gao, Lingling ^{[1
]}

Zhang, Dequan ^{[1
]}

机构：

[1] Chinese Acad Agr Sci, Inst Food Sci & Technol, Key Lab Agroprod Proc, Minist Agr, Beijing 100193, Peoples R China

[2] Chinese Acad Agr Sci, Inst Food Sci & Technol, 1 Nong Da South Rd, Beijing 100193, Peoples R China

来源：

FOOD CHEMISTRY | 2017年 / 228卷

基金：

中国国家自然科学基金;

关键词：

Mutton; mu-Calpain; Phosphorylation; Temperature; Calcium; LONGISSIMUS MUSCLE; POSTMORTEM PROTEOLYSIS; MYOFIBRILLAR PROTEINS; CALCIUM-CHLORIDE; PORCINE MUSCLE; BOVINE MUSCLE; MEAT QUALITY; CALPASTATIN; TENDERNESS; SYSTEM;

D O I：

10.1016/j.foodchem.2017.02.003

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

This study aimed to investigate the effects of phosphorylation on the activity of mu-calpain and its sensitivity to temperature and Ca2+. For temperature sensitivity analysis, sarcoplasmic protein was treated with alkaline phosphatase (AP) and phosphatase inhibitor (PI) at 4, 25 and 37 degrees C. The results showed that the degradation degree of mu-calpain in the AP group was significantly higher after incubation for 12 h. For calcium sensitivity analysis, samples treated with AP and PI were incubated at 0.01, 0.05, 0.1 and 1 mM Ca2+. The results showed that the degradation rate of mu-calpain was maximum in the AP group and minimum in the PI group at 0.01, 0.05 and 0.1 mM Ca2+. The differences between the three groups reduced as concentration increased. These data demonstrate that phosphorylation plays a negative role in regulating mu-calpain activity. This study clarifies the regulatory mechanism of mu-calpain activation in vitro and/or in postmortem muscle. (C) 2017 Elsevier Ltd. All rights reserved.

引用

页码：649 / 655

页数：7

共 29 条

[1] Identification of different domains of calpain and calpastatin from chicken blood and their role in post-mortem aging of meat during holding at refrigeration temperatures [J].