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

Abstract

The effects of longan seed polyphenols (LSPs) on postprandial glycemic response in mice were investigated, enzyme inhibition kinetics of LSPs against α-amylase were studied using an inhibition assay in vitro, and the underlying mechanisms were discussed by analyzing the impacts of LSPs on the structure of α-amylase using multispectral approaches. The results showed LSPs significantly suppressed blood glucose response in a dose-dependent manner. Enzyme inhibition analysis demonstrated LSPs inhibited α-amylase activity in a mixed type (IC₅₀ 3.02 mg mL⁻¹). 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.