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This paper describes the ability of a powerful antioxidant dihydroquercetin (DHQ) as a new inhibitor of the alpha-amylase. The enzyme activity was estimated in presence of different concentration of DHQ. The IC
50
of this compound is close to 9 mM. Competitive kinetic mechanism of inhibition was demonstrated. Inhibition constant was estimated as 2.25 ± 0.22 mM (684 ± 66 ppm). It indicates a high affinity of dihydroquercetin to enzyme. The effect of dihydroquercetin as starch hydrolysis inhibitor was confirmed in
Saccharomyces cerevisiae
biological model. Molecular docking analysis demonstrated binding of DHQ through hydrogen bonding with Tyr 193, Trp 263, and His 327 of the alpha-amylase. These interactions cause the competitive enzyme inhibition. DHQ constitutes a promise in the development of new drugs for the control of diabetes mellitus.