Effect of covalent modification by (-)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate

被引：128
|
作者：
Jia, Zhenbao [1 ]
Zheng, Min [2 ]
Tao, Fei [3 ]
Chen, Wenwei [3 ]
Huang, Guangrong [1 ]
Jiang, Jiaxin [1 ]
机构：
[1] China Jiliang Univ, Key Lab Marine Food Qual & Hazard Controlling Tec, Hangzhou 310018, Zhejiang, Peoples R China
[2] Jiangxi Med Coll, Dept Basic Med, Shangrao 334000, Peoples R China
[3] China Jiliang Univ, Natl & Local United Engn Lab Qual Controlling Tec, Hangzhou 310018, Zhejiang, Peoples R China
来源：
LWT-FOOD SCIENCE AND TECHNOLOGY | 2016年 / 66卷
基金：
中国国家自然科学基金;
关键词：
Whey protein isolate; (-)-Epigallocatechin-3-gallate; Modification; Functional property; GREEN TEA CATECHINS; STRUCTURAL-CHANGES; PHYSICAL-PROPERTIES; CROSS-LINKING; PHOSPHORYLATION; COMPLEXES; GLYCATION; GALLATE;
D O I：
10.1016/j.lwt.2015.10.054
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
The physicochemical and functional properties of covalently modified whey protein isolate (WPI) by (-)-epigallocatechin-3-gallate (EGCG) were investigated. WPI was chemically modified by EGCG under alkaline conditions. The effect of modification on foaming and emulsifying properties was evaluated. The results of SDS-PAGE and size exclusion chromatography indicated that modification by EGCG induced cross-linking on proteins of WPI. Fourier transform infrared spectroscopy (FT-IR) analysis illustrated the incorporation of phenolic groups into the modified WPI and the changes in protein secondary structure. Intrinsic fluorescence spectra revealed that modified WPI had a more compact tertiary structure compared to unmodified WPI. The modified WPI exhibited better foaming and emulsifying properties than unmodified WPI. These results suggest that EGCG modification is a potential method for improving the functional properties of WPI. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码：305 / 310
页数：6
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