Inhibitory effect of α-glucosidase inhibitors varies according to its origin

Tomoyuki Oki; Toshiro Matsui; Yutaka Osajima

doi:10.1021/jf980788t

Inhibitory effect of α-glucosidase inhibitors varies according to its origin

Tomoyuki Oki, Toshiro Matsui, Yutaka Osajima

Food Science and Biotechnology

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

186 Citations (Scopus)

Abstract

The inhibitory effect of α-glucosidase (AGH) inhibitors against its origins (baker's yeast and rat, rabbit, and pig small intestines) was investigated. All inhibitors used in this study showed quite different inhibitory activities according to AGH origins. Voglibose, acarbose and glucono-1,5-lactone strongly inhibited mammalian AGHs, whereas no or less inhibition was observed in yeast AGH. On the contrary, (+)-catechin, a good inhibitor against yeast AGH (IC₅₀ = 1.3 x 10^-1 mM) as well as voglibose (IC₅₀ = 2.6 x 10^-2 mM), did not retard the mammalian AGH activity. Subsequent inhibition study with various food components revealed that all of foods except for green (IC₅₀ = 0.735 mg/mL) and oolong teas (IC₅₀ = 1.34 mg/mL) showed no inhibitory activity against rat AGH, whereas they inhibited yeast AGH. Consequently, the magnitude of AGH inhibition was greatly affected by its origin, and more attention relating to AGH origin would be needed to evaluate in vitro AGH inhibitory effect.

Original language	English
Pages (from-to)	550-553
Number of pages	4
Journal	Journal of Agricultural and Food Chemistry
Volume	47
Issue number	2
DOIs	https://doi.org/10.1021/jf980788t
Publication status	Published - Feb 1 1999

All Science Journal Classification (ASJC) codes

Chemistry(all)
Agricultural and Biological Sciences(all)

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title = "Inhibitory effect of α-glucosidase inhibitors varies according to its origin",

abstract = "The inhibitory effect of α-glucosidase (AGH) inhibitors against its origins (baker's yeast and rat, rabbit, and pig small intestines) was investigated. All inhibitors used in this study showed quite different inhibitory activities according to AGH origins. Voglibose, acarbose and glucono-1,5-lactone strongly inhibited mammalian AGHs, whereas no or less inhibition was observed in yeast AGH. On the contrary, (+)-catechin, a good inhibitor against yeast AGH (IC50 = 1.3 x 10-1 mM) as well as voglibose (IC50 = 2.6 x 10-2 mM), did not retard the mammalian AGH activity. Subsequent inhibition study with various food components revealed that all of foods except for green (IC50 = 0.735 mg/mL) and oolong teas (IC50 = 1.34 mg/mL) showed no inhibitory activity against rat AGH, whereas they inhibited yeast AGH. Consequently, the magnitude of AGH inhibition was greatly affected by its origin, and more attention relating to AGH origin would be needed to evaluate in vitro AGH inhibitory effect.",

author = "Tomoyuki Oki and Toshiro Matsui and Yutaka Osajima",

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AU - Oki, Tomoyuki

AU - Matsui, Toshiro

AU - Osajima, Yutaka

PY - 1999/2/1

Y1 - 1999/2/1

N2 - The inhibitory effect of α-glucosidase (AGH) inhibitors against its origins (baker's yeast and rat, rabbit, and pig small intestines) was investigated. All inhibitors used in this study showed quite different inhibitory activities according to AGH origins. Voglibose, acarbose and glucono-1,5-lactone strongly inhibited mammalian AGHs, whereas no or less inhibition was observed in yeast AGH. On the contrary, (+)-catechin, a good inhibitor against yeast AGH (IC50 = 1.3 x 10-1 mM) as well as voglibose (IC50 = 2.6 x 10-2 mM), did not retard the mammalian AGH activity. Subsequent inhibition study with various food components revealed that all of foods except for green (IC50 = 0.735 mg/mL) and oolong teas (IC50 = 1.34 mg/mL) showed no inhibitory activity against rat AGH, whereas they inhibited yeast AGH. Consequently, the magnitude of AGH inhibition was greatly affected by its origin, and more attention relating to AGH origin would be needed to evaluate in vitro AGH inhibitory effect.

AB - The inhibitory effect of α-glucosidase (AGH) inhibitors against its origins (baker's yeast and rat, rabbit, and pig small intestines) was investigated. All inhibitors used in this study showed quite different inhibitory activities according to AGH origins. Voglibose, acarbose and glucono-1,5-lactone strongly inhibited mammalian AGHs, whereas no or less inhibition was observed in yeast AGH. On the contrary, (+)-catechin, a good inhibitor against yeast AGH (IC50 = 1.3 x 10-1 mM) as well as voglibose (IC50 = 2.6 x 10-2 mM), did not retard the mammalian AGH activity. Subsequent inhibition study with various food components revealed that all of foods except for green (IC50 = 0.735 mg/mL) and oolong teas (IC50 = 1.34 mg/mL) showed no inhibitory activity against rat AGH, whereas they inhibited yeast AGH. Consequently, the magnitude of AGH inhibition was greatly affected by its origin, and more attention relating to AGH origin would be needed to evaluate in vitro AGH inhibitory effect.

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Inhibitory effect of α-glucosidase inhibitors varies according to its origin

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