Longan seed polyphenols inhibit α-amylase activity and reduce postprandial glycemic response in mice

Abstract

). UV-vis absorption spectroscopy and fluorescence quenching spectroscopy suggest LSPs tend to bind with α-amylase through static interaction at one binding site, mainly through hydrogen bonding and van der Waals forces. The secondary structure of α-amylase was changed by LSPs as reviewed by circular dichroism, showing a more compact skeleton and more flexible loop of α-amylase. This hinders the substrate from reaching the binding site of the enzyme, resulting in reduced enzyme activity. These suggest the potential application of LSPs as a hypoglycemic agent in functional foods.

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