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. 2012 Oct 24;17(5):966–971. doi: 10.1007/s12257-012-0242-8

Inhibitory effects of epigallocatechin gallate and its glucoside on the human intestinal maltase inhibition

Thi Thanh Hanh Nguyen 1, Sun-Hwa Jung 2, Sun Lee 1, Hwa-Ja Ryu 1, Hee-Kyoung Kang 1, Young-Hwan Moon 3, Young-Min Kim 4, Atsuo Kimura 5, Doman Kim 1,✉
PMCID: PMC7091073  PMID: 32218677

Abstract

Human intestinal maltase (HMA) is an α-glucosidase responsible for the hydrolysis of α-1,4-linkages from the non-reducing end of malto-oligosaccharides. HMA has become an important target in the treatment of type-2 diabetes. In this study, epigallocatechin gallate (EGCG) and EGCG glucoside (EGCG-G1) were identified as inhibitors of HMA by an in vitro assay with IC50 of 20 ± 1.0 and 31.5 ± 1.0 μM, respectively. A Lineweaver-Burk plot confirmed that EGCG and EGCG-G1 were competitive inhibitors of maltose substrate against HMA and inhibition kinetic constants (K i) calculated from a Dixon plot were 5.93 ± 0.26 and 7.88 ± 0.57 μM, respectively. Both EGCG and EGCG-G1 bound to the active site of HMA with numerous hydrophobic and hydrogen bond interactions.

Keywords: alpha-glucosidase, human intestinal maltase, EGCG, EGCG glucoside, molecular docking

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