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Original Research Article | OPEN ACCESS

Effects of (-)-epigallocatechin gallate and quercetin on the activity and structure of ^5;-amylase

Jianhui Su, Zhe Tang

School of Marine and Bioengineering, Yancheng Institute of Technology, Yancheng 224051, PR China;

For correspondence:-  Zhe Tang   Email: tangzhe1983@163.com

Accepted: 18 February 2019        Published: 31 March 2019

Citation: Su J, Tang Z. Effects of (-)-epigallocatechin gallate and quercetin on the activity and structure of ^5;-amylase. Trop J Pharm Res 2019; 18(3):585-590 doi: 10.4314/tjpr.v18i3.20

© 2019 The authors.
This is an Open Access article that uses a funding model which does not charge readers or their institutions for access and distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0) and the Budapest Open Access Initiative (http://www.budapestopenaccessinitiative.org/read), which permit unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited..

Abstract

Purpose: To investigate the effects of (-)-epigallocatechin gallate (EGCG) and quercetin on the activity and structure of α-amylase.
Methods: The inhibitory effects of 7 functional factors were compared by measuring half maximal inhibitory concentration (IC50) values. Lineweaver-Burk plots were used to determine the type of inhibition exerted by EGCG and quercetin against α-amylase. The effect of EGCG and quercetin on the conformation of α-amylase was investigated using fluorescence spectroscopy.
Results: Quercetin and EGCG inhibited α-amylase with IC50 values of 1.36 and 0.31 mg/mL, respectively, which were much lower than the IC50 values of the other compounds (puerarin, paeonol, konjac glucomannan and polygonatum odoratum polysaccharide). The Lineweaver−Burk plots indicated that EGCG and quercetin inhibited α-amylase competitively, with ki values of 0.23 and 1.28 mg/mL, respectively. Fluorescence spectroscopy revealed that treatment with EGCG and quercetin led to formation of a loosely-structured hydrophobic hydration layer.
Conclusion: This study has unraveled the mechanism underlying the inhibition of α-amylase activity by EGCG and quercetin in vitro. This should make for better understanding of the mechanisms that underlie the antidiabetic effects of EGCG and quercetin in vivo.

Keywords: ^5;-Amylase, (-)-Epigallocatechin gallate, Quercetin; LineweaverW22;Burk plots, Antidiabetic, Fluorescence spectroscopy

Impact Factor
Thompson Reuters (ISI): 0.523 (2021)
H-5 index (Google Scholar): 39 (2021)

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