Effect of oxidation on the emulsifying properties of soy protein isolate

被引：174

作者：

Chen, Nannan ^{[1
]}

Zhao, Mouming ^{[1
,2
]}

Sun, Weizheng ^{[1
]}

Ren, Jiaoyan ^{[1
]}

Cui, Chun ^{[1
]}

机构：

[1] S China Univ Technol, Coll Light Ind & Food Sci, Guangzhou 510640, Guangdong, Peoples R China

[2] S China Univ Technol, State Key Lab Pulp & Paper Engn, Guangzhou 510640, Guangdong, Peoples R China

来源：

FOOD RESEARCH INTERNATIONAL | 2013年 / 52卷 / 01期

基金：

国家高技术研究发展计划(863计划); 中国国家自然科学基金;

关键词：

Soy protein isolate; Protein oxidation; Emulsifying properties; Structural properties; AAPH; LIPID OXIDATION; PEROXIDATION; AGGREGATION; SPECTROSCOPY; DITYROSINE; STABILITY; EMULSIONS; CASEIN;

D O I：

10.1016/j.foodres.2013.02.028

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Soy protein isolate (SPI) was oxidized by peroxyl radicals derived from 2,2'-azobis (2-amidinopropane) dihydrochloride (AAPH) and the structural and emulsifying properties of oxidized SPI were evaluated. Increasing extent of oxidation resulted in gradual carbonyl group generation, free sulfhydryl group degradation and dityrosine formation. Moderate oxidization could generate soluble protein aggregates with more flexible structure while over-oxidization would induce the formation of insoluble aggregates. Compared with the control, emulsions stabilized by moderately oxidized SPI had smaller droplet size and better thermal stability. Results from creaming index and microstructure measurement after 15 days indicated that emulsions stabilized by SPI of over-oxidation underwent severe droplet aggregation during storage while moderate oxidation had a positive effect on the emulsion stability. (c) 2013 Elsevier Ltd. All rights reserved.

引用

页码：26 / 32

页数：7

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