Abstract
The inhibition of glycosidase activity is regarded as an effective treatment for diabetes mellitus. Bilberry (Vaccinium myrtillus L.) fruit has a high content of anthocyanins with various biological activities. The objective of this study was to investigate the inhibitory activity of anthocyanin-rich bilberry extract (BE) on α-glucosidase and α-amylase and their interaction mechanisms in vitro. The IC50 values of BE with regard to α-glucosidase and α-amylase inhibition were 0.31 ± 0.02 and 4.06 ± 0.12 mg/mL, respectively. The enzyme kinetics revealed that BE acts as a mixed-type inhibitor against α-glucosidase and α-amylase. Moreover, the fluorescence of two glucosidases showed significant quenching by BE. FTIR spectra and differential scanning calorimetry (DSC) indicated that BE changed the enzyme structure and decreased its stability. A morphological observation of starch granules found that BE inhibited the activity of α-amylase to postpone the hydrolysis of starch. Furthermore, the in vivo study further showed that BE had a hypoglycaemic effect. The most suitable conformation (main anthocyanidins of BE) and optimal binding site (α-glucosidase, α-amylase) were assayed by molecular docking. In conclusion, this study revealed that BE could be a potential glycosidase inhibitor.
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