Inhibitory Effect of α-Glucosidase Inhibitors Varies According to Its Origin

• Published in: Journal of agricultural and food chemistry 1999-02, Vol.47 (2), p.550-553
• Main Authors: Oki, Tomoyuki, Matsui, Toshiro, Osajima, Yutaka
• Format: Article
• Language: English
• Subjects: Animals; Biological and medical sciences; Endocrine glands; Enzyme Inhibitors - pharmacology; Food; Glycoside Hydrolase Inhibitors; Intestine, Small - enzymology; Kinetics; Medical sciences; Rabbits; Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects); Rats; Saccharomyces cerevisiae - enzymology; Swine
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf980788t

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 × 10-1 mM) as well as voglibose (IC50 = 2.6 × 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. Keywords: α-Glucosidase; inhibition; non-insulin-dependent diabetes mellitus