Affiliation

Faculty of Veterinary and Agricultural Sciences, University of Melbourne, Australia

Corresponding Author

Ken Ng,Faculty of Veterinary and Agricultural Sciences, University of Melbourne, Royal Parade, Parkville, Melbourne, Victoria, Australia, Tel: 61-3-90353141; E-mail: ngkf@unimelb.edu.au

Citation

Ng, K., et al. Evaluation of Α-Amylase and Α-Glucosidase Inhibitory Activity of Flavonoids. (2015) Int J Food Nutr Sci 2(2): 174-179.

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© 2015 Ng, K. This is an Open access article distributed under the terms of Creative Commons Attribution 4.0 International License.

Keywords

Abstract

A number of phenolic acids and flavonoids were screened for inhibitory activity against rat intestinal α-glucosidase and porcine pancreatic α-amylase. The phenolic acids were not inhibitory to both enzymes at 1 mM. Inhibition of α-amylase by flavonoids mirrored the inhibition of α-glucosidase in that both baicalein and myricetin inhibited the enzyme most strongly, but differs in that spectrum of flavonoid inhibition for α-amylase only restricted to these two flavonoids while it was more wide spread for the inhibition of α-glucosidase. Baicalein inhibited α-amylase and α-glucosidase activity by 41.1±2.6% and 56.9±1.7% at 1 mM, respectively. Myricetin inhibited α-amylase and α-glucosidase activity by 35.9±3.8% and 47.7±2.4% at 1 mM, respectively. The IC50 (concentration required for 50% reduction activity) of baicalein (0.713±0.034 mM) and myricetin (1.030±0.026 mM) confirmed that baicalein is the most potent flavonoid inhibitor against α-glucosidase in the flavonoid series studied.