Inhibition mechanism of diacylated anthocyanins from purple sweet potato (Ipomoea batatas L.) against α-amylase and α-glucosidase

This study aimed to evaluate inhibitory activity of anthocyanins from purple sweet potato and blueberries against alpha-amylase and alpha-glucosidase, as well as investigate the inhibition mechanism of diacylated anthocyanins (Diacylated AF-PSP). Diacylated AF-PSP better inhibited alpha-amylase (IC50 = 0.078 mg mL-1) and alpha-glucosidase (IC50 = 1.56 mg mL-1) than other anthocyanin fractions, which was a mixed-type inhibitor. Fluorescence analysis indicated that Diacylated AF-PSP bound to the enzymes mainly through hydrogen bonds and influenced the microenvironments of proteins. Additionally, surface hydrophobicity and circular dichroism spectra results confirmed conformational changes in the enzymes induced by Diacylated AF-PSP. Molecular docking further demonstrated the interaction of Diacylated AF-PSP with enzyme active site, which might be stabilized by its acyl groups. Finally, 160 mg kg-1 Diacylated AF-PSP significantly decreased (p < 0.01) blood glucose level peak by 20.52% after starch administration in SD rats. This study provided theoretical evidences for utilization of diacylated anthocyanins in hyperglycemia-management functional foods.