Solubility and molecular properties of heat-cured soy protein films

被引：47

作者：

Rangavajhyala, N ^{[1
]}

Ghorpade, V ^{[1
]}

Hanna, M ^{[1
]}

机构：

[1] UNIV NEBRASKA, DEPT BIOL SYST ENGN, LINCOLN, NE 68583 USA

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1997年 / 45卷 / 11期

关键词：

protein film; heat curing; solubility; disulfide bonds;

D O I：

10.1021/jf9702048

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Changes in solubility and molecular weight distribution of protein in heat-cured soy protein film were investigated to understand the mechanism of protein-protein interactions that occur during heat treatment. Soy protein films were heated at 65, 80, or 95 degrees C for 6, 18, or 24 h. The solubility of the proteins decreased with increasing temperature of heat treatment in various buffers. Buffers containing urea, a hydrogen bond-disrupting agent, and 2-mercaptoethanol, a disulfide bond-disrupting agent, dissolved more than 95% of protein in all the heat-treated samples. SDS-PAGE patterns indicated aggregation of proteins during film formation and in heat-treated films. The combined effects of urea and 2-mercaptoethanol suggested that proteins were aggregated primarily through hydrogen bonds and intermolecular disulfide bonds. This aggregation increased molecular weight and decreased film solubility.

引用

页码：4204 / 4208

页数：5

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