Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging

被引：58

作者：

Huang, Ming ^{[1
]}

Huang, Feng ^{[1
]}

Xu, Xinglian ^{[1
]}

Zhou, Guanghong ^{[1
]}

机构：

[1] Nanjing Agr Univ, Coll Food Sci & Technol, Key Lab Meat Proc & Qual Control, Minist Educ China, Nanjing 210095, Peoples R China

来源：

FOOD CHEMISTRY | 2009年 / 115卷 / 01期

关键词：

Caspase3; Skeletal muscle protein; Calpain; Inhibitor; Post mortem aging; Proteolysis; STRIATED-MUSCLE; BOVINE MUSCLE; MU-CALPAIN; APOPTOSIS; MEAT; IDENTIFICATION; DEGRADATION; TENDERNESS; BEEF; TENDERIZATION;

D O I：

10.1016/j.foodchem.2008.11.095

中图分类号：

O69 [应用化学];

学科分类号：

070301 [无机化学];

摘要：

The objective of this study was to investigate the potential contribution of apoptosis related downstream executioner caspase3 to post mortem skeletal muscle proteolysis by use of caspase3 selective inhibitor DEVD-CHO (N-acetyl-Asp-Glu-Val-Asp-CHO). After slaughter, four chicken breast muscles were removed and cut into small pieces, then marinated in treatment solution containing DEVD-CHO, or in control solution, and stored at 4 degrees C for 1, 3 or 7 d. Meat samples were obtained and used for detecting muscle protein degradation or calpain activity. Results showed that DEVD-CHO had inhibited the degradation of muscle skeletal proteins (titin, nebulin, desmin and troponin-T) significantly, whereas the activity of calpains had not been influenced. Therefore, the degradation of muscle proteins should not been exclusively attributed to the calpain system, and the effector caspase3 may be a new protease involved in meat post mortem tenderization. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：181 / 186

页数：6

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