Inhibition of .ALPHA.-Glucosidase and .ALPHA.-Amylase by Flavonoids

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  • TADERA Kenjiro
    Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
  • MINAMI Yuji
    Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
  • TAKAMATSU Kouta
    Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
  • MATSUOKA Tomoko
    Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University

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  • Inhibition of α-Glucosidase and α-Amylase by Flavonoids
  • Inhibition of アルファ Glucosidase and アルファ Amylase by Flavonoids

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The inhibitory activity of six groups of flavonoids against yeast and rat small intestinal α-glucosidases and porcine pancreatic α-amylase was compared, and chemical structures of flavonoids responsible for the inhibitory activity were evaluated. Yeast α-glucosidase was potently inhibited by the anthocyanidin, isoflavone and flavonol groups with the IC50 values less than 15 μM. The following structures enhanced the inhibitory activity: the unsaturated C ring, 3-OH, 4-CO, the linkage of the B ring at the 3 position, and the hydroxyl substitution on the B ring. Rat small intestinal α-glucosidase was weakly inhibited by many flavonoids, and slightly by the anthocyanidin and isoflavone groups. 3-OH and the hydroxyl substitution on the B ring increased the inhibitory activity. In porcine pancreatic α-amylase, luteolin, myricetin and quercetin were potent inhibitors with the IC50 values less than 500 μM. The 2, 3-double bond, 5-OH, the linkage of the B ring at the 3 position, and the hydroxyl substitution on the B ring enhanced the inhibitory activity, while 3-OH reduced it.

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