Interaction mechanism between green tea extract and human α-amylase for reducing starch digestion

被引：115

作者：

Miao, Ming ^{[1
]}

Jiang, Bo ^{[1
]}

Jiang, Huan ^{[1
]}

Zhang, Tao ^{[1
]}

Li, Xingfeng ^{[1
]}

机构：

[1] Jiangnan Univ, Synerget Innovat Ctr Food Safety & Nutr, State Key Lab Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China

来源：

FOOD CHEMISTRY | 2015年 / 186卷

基金：

中国国家自然科学基金;

关键词：

Green tea extract; Human pancreatic alpha-amylase; Interaction; Molecular docking; DIETARY POLYPHENOLS; GLYCEMIC CONTROL; BLACK TEA; GLUCOSE; INHIBITION; CATECHINS; LEAVES; PLANT; MICE;

D O I：

10.1016/j.foodchem.2015.02.049

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

This study evaluated the inhibitory effects of the green tea extract on human pancreatic alpha-amylase activity and its molecular mechanism. The green tea extract was composed of epicatechin (59.2%), epigallocatechin gallate (14.6%) and epicatechin gallate (26.2%) as determined by HPLC analysis. Enzyme activity measurement showed that % inhibition and IC50 of the green tea extract (10%, based on starch) were 63.5% and 2.07 mg/ml, respectively. The Michaelis-Menten constant remained unchanged but the maximal velocity decreased from 0.43 (control) to 0.07 mg/(ml x min) (4 mg/ml of the green tea extract), indicating that the green tea extract was an effective inhibitor against alpha-amylase with a non-competitive mode. The fluorescence data revealed that the green tea extract bound with alpha-amylase to form a new complex with static quenching mechanism. Docking study showed the epicatechin gallate in the green tea extract presented stronger affinity than epigallocatechin gallate, with more number of amino acid residues involved in amylase binding with hydrogen bonds and Van der Waals forces. Thus, the green tea extract could be used to manipulate starch digestion for potential health benefits. (C) 2015 Elsevier Ltd. All rights reserved.

引用

页码：20 / 25

页数：6

共 39 条

[11] THE INHIBITION OF ALPHA-AMYLASE BY TEA POLYPHENOLS [J].