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Issue 7, 2019
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Different inhibition properties of catechins on the individual subunits of mucosal α-glucosidases as measured by partially-purified rat intestinal extract

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Abstract

Mucosal α-glucosidases from rat intestinal powder were employed, with a step to remove α-amylase, to measure the possibility of different inhibition of catechins, particularly those found in tea, on the four α-glucosidase enzymes. Inhibition of catechins was investigated for the slowing of digestion of glycemic carbohydrates, thus regulating glucose release and absorption. The α-glucosidases were fractionated using size-exclusion chromatography. The partially purified fractions showed higher α-glucosidase activity without any α-amylase activity. Catechins had selective inhibition properties on the α-glucosidases. In particular, (−)-epigallocatechin gallate (EGCG) and (−)-epicatechin gallate (ECG) showed comparably high inhibitory effect on all four individual α-glucosidases, while (−)-epicatechin (EC), and (+)-catechin (C) indicated a more discriminating effect with relatively higher inhibitory effects on sucrase-isomaltase. The findings suggest that catechins differently inhibit the individual subunits of the α-glucosidases, and that they could modulate postprandial blood glucose levels through slowing digestion rate of starch and other glycemic carbohydrates, including sucrose.

Graphical abstract: Different inhibition properties of catechins on the individual subunits of mucosal α-glucosidases as measured by partially-purified rat intestinal extract

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Article information


Submitted
09 May 2019
Accepted
02 Jul 2019
First published
04 Jul 2019

Food Funct., 2019,10, 4407-4413
Article type
Paper

Different inhibition properties of catechins on the individual subunits of mucosal α-glucosidases as measured by partially-purified rat intestinal extract

J. Lim, D. K. Kim, H. Shin, B. R. Hamaker and B. Lee, Food Funct., 2019, 10, 4407
DOI: 10.1039/C9FO00990F

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