Abstract: The compounds resulting from the Maillard reaction between bioactive peptides derived from food and carbohydrates possess unique molecular structures, excellent nutritional functionality, and exceptional biocompatibility. These compounds exert significant influence on the processing quality, functional characteristics, and nutritional health benefits of food. The complexes formed by proteolytic products and sugars have smaller molecular weight, higher covalent efficiency, better functional nutritional properties, and easier digestion and decomposition of biological activity compared to the covalent complexes formed by protein-sugars. Therefore, in order to better modify and utilize gluten protein,in this study, gluten was modified by enzymatic hydrolysis combined with Maillard reaction, and its physicochemical, structural, and processing properties were studied. Due to the influence of enzymatic hydrolysis and reaction temperature, the properties and structures of Maillard reaction products of gluten protein (MG) and its enzymatic hydrolysates (MEG) had significant differences. The results showed that compared with gluten protein, when the reaction temperature was 100 ℃, the maximum foaming capacity of MEG was 19.17%, the solubility and grafting degree were increased to (40.27±0.32)% and (24.75±1.47)%, respectively. The emulsifying activity increased by 1.2 times, and the free sulfhydryl content was 0.86μmol/g, indicating that enzymatic hydrolysis can effectively reduce the formation of disulfide bonds. In addition, with the increase in reaction temperature, the fluorescence intensity of Maillard reaction products (MRPs) decreased, which enhanced the fluorescence quenching of tryptophan and tyrosine residues, while the content of fluorescent intermediates increased. Meanwhile, enzymatic hydrolysis promoted the occurrence of the Maillard reaction and the formation of advanced glycation end products (AGEs). Therefore, the objective of this study was to evaluate the applicability of enzymatic hydrolysis and Maillard reaction in improving gluten processability. The physicochemical properties and structural characteristics, the functional properties and the effect of modification on AGEs generation were investigated. The results provided a feasible method for modifying the structure of gluten protein and improved its processing performance.