THERMAL-DENATURATION OF HAKE (MERLUCCIUS-HUBBSI) MYOFIBRILLAR PROTEINS - A DIFFERENTIAL SCANNING CALORIMETRIC AND ELECTROPHORETIC STUDY

被引：47

作者：

BEAS, VE ^{[1
]}

WAGNER, JR ^{[1
]}

CRUPKIN, M ^{[1
]}

ANON, MC ^{[1
]}

机构：

[1] UNIV NACL LA PLATA,CTR INVEST CARDIOVASC,CONSEJO NACL INVEST CIENT & TECN,RA-1900 LA PLATA,BUENOS AIRES,ARGENTINA

来源：

JOURNAL OF FOOD SCIENCE | 1990年 / 55卷 / 03期

关键词：

D O I：

10.1111/j.1365-2621.1990.tb05206.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Denaturation of hake (Merluccius hubbsi) proteins was studied with DSC by monitoring Tmax of transitions and denaturation enthalpies. Whole muscle free of connective tissue showed two transitions (Tmax 46.5°C and 75.3°C), and ΔH of 4.27 cal/g. The exudative sarcoplasmic fraction showed three transitions (Tmax 45.2°C, 59.0°C and 75.5°C) and ΔH of 3.92 cal/g. The sarcoplasmic proteins from whole hake muscle contributed to both denaturation peaks. Muscle depleted of sarcoplasmic proteins by chloride extraction showed a higher thermal sensitivity and a diminished denaturation enthalpy on the second transition. This suggested an additional effect of chloride upon actin in addition to sarcoplasmic protein extraction. pH had an effect upon the native conformation of thick filament proteins, specifically myosin. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：683 / &

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