Changes in physiochemical properties of water-soluble proteins from crucian carp (Carassius auratus) during heat treatment

被引：3
|
作者：
Li, Kaifeng [1 ]
Shen, Huixing [2 ]
Li, Bo [1 ]
Wang, Hang [1 ]
Luo, Yongkang [1 ]
机构：
[1] China Agr Univ, Coll Food Sci & Nutr Engn, Beijing Higher Inst, Engn Res Ctr Anim Product, Beijing 100083, Peoples R China
[2] China Agr Univ, Coll Sci, Beijing 100083, Peoples R China
来源：
JOURNAL OF FOOD SCIENCE AND TECHNOLOGY-MYSORE | 2014年 / 51卷 / 07期
基金：
中国国家自然科学基金;
关键词：
Water-soluble proteins; Heat treatment; Crucian carp; Physicochemical properties; SARCOPLASMIC PROTEINS; PHYSICOCHEMICAL PROPERTIES; FUNCTIONAL-PROPERTIES; MYOFIBRILLAR PROTEIN; THERMAL-DENATURATION; STRUCTURAL-CHANGES; MUSCLE; ACTOMYOSIN; SURIMI; GEL;
D O I：
10.1007/s13197-012-0651-x
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
In order to understand physicochemical properties of water-soluble proteins obtained from crucian carp, turbidity, total sulfhydryl content, hydrophobicity and SDS-PAGE of crucian carp water-soluble proteins during heat treatment were investigated. Turbidity remained unchanged up to 44A degrees C and considerably increased from 46A degrees C to 54A degrees C, one peak of increase rate was found at 50A degrees C; total SH content decreased rapidly when heated from 50A degrees C to 55A degrees C; hydrophobicity increased sharply when heated up to 45A degrees C, indicating the conformation of water-soluble proteins from crucian carp began to unfold and expose the buried nonpolar amino acids at temperatures above 45A degrees C; analysis of SDS-PAGE indicating the formation of disulfide linkage of creatine kinase and glyceraldehy-3-phosphate dehydrogenase when the temperature reached 65A degrees C and 80A degrees C, respectively.
引用
收藏
页码：1396 / 1400
页数：5
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