In vitro survey of α–glucosidase inhibitory food components

Toshiro Matsui; Chiho Yoshimoto; Katsuhiro Osajima; Tomoyuki Oki; Yutaka Osajima

doi:10.1271/bbb.60.2019

In vitro survey of α–glucosidase inhibitory food components

Toshiro Matsui, Chiho Yoshimoto, Katsuhiro Osajima, Tomoyuki Oki, Yutaka Osajima

Food Science and Biotechnology

Research output: Contribution to journal › Article › peer-review

197 Citations (Scopus)

Abstract

A survey of food components with α-glucosidase (AGH) inhibitory activity was conducted to identify a prophylactic effect for diabetes in food. Sardine muscle hydrolyzed by alkaline protease showed potent activity (IC₅₀ = 48.7mg/ml) as well as green and oolong teas (IC₅₀ = 11.1 and 11.3mg/ml, respectively). Furthermore, hydrolyzates prepared by various proteases gave differing AGH inhibitory activity. DEAE-Sephadex chromatography of the alkaline protease hydrolyzate eluted potent AGH inhibitors (IC₅₀ = 15.6mg/ml) with a 50 mM phosphate buffer (pH 7.0) containing 0.3 m NaCl, and their subsequent separation by HPLC in an ODS column showed that there were some inhibitors possessing primary amino groups. This indicates that they would have been high anionic and peptidic compounds.

Original language	English
Pages (from-to)	2019-2022
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	60
Issue number	12
DOIs	https://doi.org/10.1271/bbb.60.2019
Publication status	Published - Jan 1996

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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10.1271/bbb.60.2019

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abstract = "A survey of food components with α-glucosidase (AGH) inhibitory activity was conducted to identify a prophylactic effect for diabetes in food. Sardine muscle hydrolyzed by alkaline protease showed potent activity (IC50 = 48.7mg/ml) as well as green and oolong teas (IC50 = 11.1 and 11.3mg/ml, respectively). Furthermore, hydrolyzates prepared by various proteases gave differing AGH inhibitory activity. DEAE-Sephadex chromatography of the alkaline protease hydrolyzate eluted potent AGH inhibitors (IC50 = 15.6mg/ml) with a 50 mM phosphate buffer (pH 7.0) containing 0.3 m NaCl, and their subsequent separation by HPLC in an ODS column showed that there were some inhibitors possessing primary amino groups. This indicates that they would have been high anionic and peptidic compounds.",

author = "Toshiro Matsui and Chiho Yoshimoto and Katsuhiro Osajima and Tomoyuki Oki and Yutaka Osajima",

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AU - Matsui, Toshiro

AU - Yoshimoto, Chiho

AU - Osajima, Katsuhiro

AU - Oki, Tomoyuki

AU - Osajima, Yutaka

PY - 1996/1

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In vitro survey of α–glucosidase inhibitory food components

Abstract

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