Abstract
In this study, the inhibition and mechanism of epigallocatechin (EGC) on two key glycoside hydrolases (α-glucosidase, α-amylase) were explored from the molecular structure level. The chemical structure of EGC was characterized by X-ray diffraction, Fourier transform infrared (FTIR) spectroscopy, and proton nuclear magnetic resonance spectroscopy. EGC's inhibition on these enzymes was colorimetrically determined. The effects of EGC on the chemical structure and spatial configuration of the enzymes were explored via FTIR spectroscopy, fluorescence spectroscopy, and molecular docking techniques. The results showed that EGC exhibited the inhibition of α-glucosidase and α-amylase in a non-competitive manner, showing a continuous upward trend as EGC's concentration increased. There was a fluorescence quenching effect of EGC on α-glucosidase and α-amylase. Molecular docking confirmed that EGC can bind to amino acid residues in the enzyme through intermolecular hydrogen bonds and hydrophobic interactions, resulting in the changed chemical structure and spatial conformation of the enzymes. This decreased enzyme activity. This result suggested that EGC has the potential to inhibit two key glycoside hydrolases, and it would be beneficial to incorporate EGC into functional foods for diabetics.