Desmin and troponin T are degraded faster in type IIb muscle fibers than in type I fibers during postmortem aging of porcine muscle

被引：58

作者：

Muroya, Susumu ^{[1
,2
]}

Ertbjerg, Per ^{[2
]}

Pomponio, Luigi ^{[2
]}

Christensen, Mette ^{[2
]}

机构：

[1] Natl Inst Livestock & Grassland Sci, Tsukuba, Ibaraki 3050901, Japan

[2] Univ Copenhagen, DK-1958 Frederiksberg C, Denmark

来源：

MEAT SCIENCE | 2010年 / 86卷 / 03期

关键词：

Myofibrillar protein isoforms; Proteolysis; Pork; Myosin heavy chain isoform; Single fiber isolation; AMINO-ACID-SEQUENCES; OVINE SKELETAL-MUSCLES; MU-CALPAIN; MEAT QUALITY; BIOCHEMICAL-PROPERTIES; MECHANICAL-PROPERTIES; BOVINE LONGISSIMUS; PROTEOLYSIS; ISOFORMS; SLOW;

D O I：

10.1016/j.meatsci.2010.06.019

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

A novel approach was applied in this study to directly evaluate the effect of muscle fiber type on postmortem protein degradation. Porcine muscle fibers were isolated from longissimus muscle at day 1, 3, and 6 postmortem. Fibers were sorted by immunochemical myosin heavy chain isoform typing. Western blot analysis of fibers pooled separately into type I or IIb showed that the relative amounts of 39- and 50-kDa desmin degradation fragments at day 6, and 28- to 31-kDa fragments of troponin T fast type isoform (fTnT) at day 1 and 6 postmortem were higher in type IIb than in type I fibers. At day 6 troponin T slow type isoform (sTnT) was less degraded than fTnT in type I fibers. These results indicated greater rate and extent of proteolysis in type IIb than in type I fibers and higher susceptibility of fTnT to proteolysis than that of sTnT isoform. (C) 2010 The American Meat Science Association. Published by Elsevier Ltd. All rights reserved.

引用

页码：764 / 769

页数：6

共 34 条

[1] Cleavage of desmin by cysteine proteases: Calpains and cathepsin B [J].