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Effects of (-)-epigallocatechin gallate and quercetin on the activity and structure of α-amylase


Jianhui Su
Zhe Tang

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.


Journal Identifiers


eISSN: 1596-9827
print ISSN: 1596-5996