The structural characteristics of hydroxyl and galloyl groups determine the inhibitory activity of α-amylase in four catechin monomers

IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY
Rourou Wen , Xianghua Chai , Pingping Wang , Kegang Wu , Xuejuan Duan , Jiasi Chen , Xiumei Li
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Abstract

In this study, the effect of hydroxyl and galloyl groups structure of catechin monomers on the inhibitory activity of α-amylase were studied by substrate depletion, inhibition kinetics, fluorescence quenching, circular dichroism analysis, molecular docking, and molecular dynamics methods. The catechin monomers of EGCG and ECG with more phenolic hydroxyl groups and specific gallate esters showed the stronger inhibitor effect, higher fluorescence quenching effects and more intense structural disruption on α-amylase than EGC and EC. Molecular simulation further elucidated that EGCG and ECG, due to their specific gallate esters and more phenolic hydroxyl groups, interact more favorably with amino acid residues in the α-amylase active site compared to EGC and EC. These findings reveal the mechanism of α-amylase inhibition by catechin monomers with different structures and provide the theoretical basis for the role of catechins as anti-glycemic components in the dietary management of diabetes.

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来源期刊
LWT - Food Science and Technology
LWT - Food Science and Technology 工程技术-食品科技
CiteScore
11.80
自引率
6.70%
发文量
1724
审稿时长
65 days
期刊介绍: LWT - Food Science and Technology is an international journal that publishes innovative papers in the fields of food chemistry, biochemistry, microbiology, technology and nutrition. The work described should be innovative either in the approach or in the methods used. The significance of the results either for the science community or for the food industry must also be specified. Contributions written in English are welcomed in the form of review articles, short reviews, research papers, and research notes. Papers featuring animal trials and cell cultures are outside the scope of the journal and will not be considered for publication.
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