Protein denaturing conditions in beef deep semimembranosus muscle results in limited μ-calpain activation and protein degradation

被引：42

作者：

Kim, Yuan H. ^{[1
]}

Lonergan, Steven M. ^{[1
]}

Huff-Lonergan, Elisabeth ^{[1
]}

机构：

[1] Iowa State Univ, Dept Anim Sci, Meat Sci & Muscle Biol Grp, Ames, IA 50011 USA

来源：

MEAT SCIENCE | 2010年 / 86卷 / 03期

关键词：

Beef; mu-calpain; Protein denaturation; Proteolysis; Semimembranosus; Tenderness; WATER-HOLDING CAPACITY; COLOR STABILITY; PORK QUALITY; PH DECLINE; PROTEOLYSIS; MEAT; GLYCOLYSIS; TENDERNESS; OXIDATION; SYSTEM;

D O I：

10.1016/j.meatsci.2010.06.002

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The objective was to determine the effect of muscle location on protein solubility and protein degradation in deep (DSM) and superficial (SSM) portion of beef semimembranosus. At 24 h postmortem, the semimembranosus was removed from beef carcasses (n = 10), packaged in high-oxygen modified atmosphere (80% O-2 + 20% CO2), and displayed for 7 d at 1 degrees C. DSM had higher (P<0.05) L*, a*, b*, and hue values than SSM throughout display. DSM had significantly higher protein denaturation and less protein concentration than SSM. Western blotting for mu-calpain autolysis revealed that DSM maintained more (P<0.05) unautolyzed mu-calpain than SSM. This result coincided with less desmin and troponin-T degradation in samples from the DSM. These results confirm the hypothesis that increased protein denaturation in DSM results in minimal proteolysis by negatively affecting mu-calpain activation. This demonstrates a potential to alter progression of proteolysis and improvement in tenderness associated with postmortem storage. (C) 2010 The American Meat Science Association. Published by Elsevier Ltd. All rights reserved.

引用

页码：883 / 887

页数：5

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