Heat treatment effect on whey protein-epigallocatechin gallate interaction: A fluorescence spectroscopic analysis

文献类型： 外文期刊

第一作者： Song, Yu-qi

作者： Song, Yu-qi;Dong, Rong-shu;Song, Yu-qi;Yao, Guanglong;Chen, Jian;Zhao, Ying

作者机构：

关键词： Epigallocatechin gallate; Whey protein; Interaction; Quenching mechanism

期刊名称：FOOD CHEMISTRY-X （ 影响因子：6.1； 五年影响因子：6.4 ）

ISSN： 2590-1575

年卷期： 2023 年 20 卷

页码：

收录情况： SCI

摘要： This study aimed to examine the interaction mechanism of polyphenol protein in a heat-treated aqueous solution system using epigallocatechin gallate (EGCG) and whey protein (WP) as raw materials. Further, we hypothesized the binding characteristics of these two compounds. The results were as follows: The quenching mechanism between WP and EGCG was characterized as static quenching. As the temperature increased, the binding constant and the binding force between EGCG and WP both increased. The number of binding sites (denoted as n) between WP and EGCG was approximately 1. Hence, WP provided a single site to bind to EGCG to form a complex. The main binding modes between WP and EGCG were hydrophobic and electrostatic interactions, and they were spontaneously combined into complexes (Delta G < 0). This study provided a basis for the interaction between WP and EGCG under different heating conditions and their combination mode.

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