Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins

被引：311

作者：

Morzel, Martine ^{[1
]}

Gatellier, Philippe ^{[1
]}

Sayd, Thierry ^{[1
]}

Renerre, Michel ^{[1
]}

Laville, Elisabeth ^{[1
]}

机构：

[1] INRA, Ctr Theix, F-63122 St Genes Champanelle, France

来源：

MEAT SCIENCE | 2006年 / 73卷 / 03期

关键词：

myofibrils; protein oxidation; carbonyl; free thiol; bityrosine; electrophoresis; proteolysis; OXIDIZED PROTEINS; OXYGEN RADICALS; AMINO-ACIDS; DIETARY-FAT; VITAMIN-E; DEGRADATION; PROTEASOME; MYOSIN; BEEF; TURKEY;

D O I：

10.1016/j.meatsci.2006.02.005

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The objective of this study was to investigate the effect of chemical oxidation on proteolysis susceptibility of myofibrillar proteins. Myofibrils were prepared from pig M. longissimus dorsi and oxidised by a hydroxyl radical generating system. Protein oxidation level was measured by the carbonyl content, free thiol group content and bityrosine formation. Oxidised or non-oxidised myofibrillar proteins were exposed to papain and proteolysis was estimated by fluorescence using fluorescamine. Oxidation of myofibrillar proteins was dependent upon the oxidising agent concentration. Disulfide bridge and bityrosine formation indicated that oxidation by OH degrees can induce protein polymerization. Electrophoretic study showed that myosin was the protein most sensitive to oxidation. Results showed a direct and quantitative relationship between protein damages by hydroxyl radical and decreased proteolytic susceptibility. Electrophoretic observations suggest that polymerization and aggregation may explain in part decreased susceptibility of myofibrillar proteins to proteolysis. (c) 2006 Elsevier Ltd. All rights reserved.

引用

页码：536 / 543

页数：8

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