Studies on the interaction of -epigallocatechin-3-gallate from green tea with bovine β-lactoglobulin by spectroscopic methods and docking

被引：53

作者：

Wu, Xuli ^{[1
,2
]}

Dey, Raja ^{[3
,4
]}

Wu, Hui ^{[1
]}

Liu, Zhigang ^{[2
]}

He, Qingqing ^{[2
]}

Zeng, Xiaojuan ^{[2
]}

机构：

[1] S China Univ Technol, Coll Light Ind & Food Sci, Guangzhou 510642, Guangdong, Peoples R China

[2] Shenzhen Univ, Sch Med, Shenzhen 518060, Guangdong, Peoples R China

[3] Univ So Calif, Dept Biol Sci, Los Angeles, CA 90089 USA

[4] Univ So Calif, Dept Chem, Los Angeles, CA 90089 USA

来源：

INTERNATIONAL JOURNAL OF DAIRY TECHNOLOGY | 2013年 / 66卷 / 01期

关键词：

Epigallocatechin-3-gallate; ss-Lactoglobulin; Spectroscopy; Docking studies; Binding; SERUM-ALBUMIN; STRUCTURAL FLUCTUATIONS; COLLOIDAL STABILITY; BLACK TEAS; MILK; FLUORESCENCE; BINDING; PROTEINS; POLYPHENOL; EXTRACTS;

D O I：

10.1111/j.1471-0307.2012.00873.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The binding interaction between-epigallocatechin-3-gallate (EGCG) and bovine beta-lactoglobulin (beta LG) was thoroughly studied by fluorescence, circular dichroism (CD) and proteinligand docking. Fluorescence data revealed that the fluorescence quenching of beta LG by EGCG was the result of the formation of a complex of beta LGEGCG. The binding constants and thermodynamic parameters at two different temperatures and the binding force were determined. The binding interaction between EGCG and beta LG was mainly hydrophobic and the complex was stabilised by hydrogen bonding. The results suggested that beta LG in complex with EGCG changes its native conformation. Furthermore, preheat treatment (90 degrees C, 120 degrees C) and emulsifier (sucrose fatty acid ester) all boosted the binding constants (Ka) and the binding site values (n) of the beta LG-EGCG complex. This study provided important insight into the mechanism of binding interactions of green tea flavonoids with milk protein.

引用

页码：7 / 13

页数：7

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