The transglutaminase (TGase) and D-galactosamine were modified improve the solubility in water of corn glutelin. The effect of the glycosylation modification on structural properties and antioxidant activities of original corn glutelin were evaluated. The result of Fourier transform infrared spectroscopy indicated that D-galactosamine was covalently conjugated to corn glutelin under the catalysis of transglutaminase. The free amino groups and the denaturation temperature, as well as the enthalpy of thermal denaturation of the glycosylated corn glutelin, decreased by 158 mmol/kg protein and 9.03 ℃ and 68.74 J/g compared with the original corn glutelin, respectively. These indicated that the structure of corn glutelin became disordered and loose, and the thermal stability of corn glutelin was significantly decreased by glycosylation modification. Meanwhile, three radical scavenging activities (including DPPH, superoxide, hydroxyl), Fe²⁺-chelating capacity, and the reducing power of the glycosylated corn glutelin were increased, and its EC₅₀ value for Fe²⁺-chelating capacity was decreased by 1.27 mg/mL. The results suggested that enzymatic glycosylation would be an effective method for the modification of corn gluten.