��-Glucosidase Inhibitor Isolated from Coffee
Author(s) -
Shin-Duk Kim
Publication year - 2015
Publication title -
journal of microbiology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 64
eISSN - 1738-8872
pISSN - 1017-7825
DOI - 10.4014/jmb.1411.11057
Subject(s) - chemistry , enzyme , sucrase , stereochemistry , ic50 , nuclear magnetic resonance spectroscopy , fractionation , alkaloid , biochemistry , chromatography , in vitro
The potent α-glucosidase inhibitor (compound I) was isolated from coffee brews by the activity-based fractionation and identified as a β-carboline alkaloid norharman (9H-pyrido[ 3.4-b]indole) on the basis of mass spectroscopy and nuclear magnetic resonance spectra ((1)H NMR, (13)C NMR, and COSY). The norharman showed a potent inhibition against α-glucosidase enzyme in a concentration dependent manner with an IC50 value of 0.27 mM for maltase and 0.41 mM for sucrase, respectively. A Lineweaver-Burk plot revealed that norharman inhibited α-glucosidase enzyme uncompetitively, with a Ki value of 0.13 mM.
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