Abstract:The dry Maillard reaction method was used to glycosylate rice bran globulin.On this basis，the noncovalent binding of glycosylated rice bran globulin with two polyphenols was studied. The interaction mechanism between them was characterized and analyzed by fluorescence spectroscopy，infrared spectroscopy，differential scanning calorimetry，etc. The results showed that the micromorphology of rice bran globulin was changed after glycosylation，and the anti-digestibility and antioxidant properties were improved. Quercetin and resveratrol could both cause fluorescence quenching of glycosylated proteins，and resveratrol caused a red shift in the emission peak of glycosylated proteins. In this non-covalent binding，hydrogen bonding/van der Waals forces played a major role.Fluorescence fitting data showed that glycosylated proteins could bind both resveratrol and quercetin simultaneously，with binding sites and constants of 0.014 7 and 0.002 23，respectively. The binding ability was lower than that of binding resveratrol or quercetin molecules separately. The particle sizes of glycosylated proteins and glycosylated protein-polyphenol non-covalent complexes were higher than that of rice bran globulin，and the maximum particle size occurred when glycosylated proteins were bound to two polyphenols simultaneously. In addition，the non-covalent binding of glycosylated proteins with two polyphenols could significantly improve the protein’s thermal stability and antioxidant capacity，and this improvement was situated between the glycosylated proteins binding to resveratrol and quercetin molecules alone.