In this experiment, the peptides were obtained by enzymatic digestion of wheat germ proteins from river sets using neutral protease, trypsin and pepsin. In vitro antioxidant capacity of samples was determined and their polypeptides distribution was determined using polyacrylamide gel electrophoresis (SDS-PAGE). The results showed that germ protein and polypeptides concentrations were positively correlated with antioxidant capacity.The antioxidant capacity of the peptides obtained by enzymatic digestion of neutral protease at different concentrations was significantly higher than that obtained by enzymatic digestion of pepsin and trypsin (P<0.05), and their reducing capacity, 2,2-biazo-bis(3-ethyl-benzothiazole- 6-sulfonic acid) diammonium salt (ABTS+), 1,1-diphenyl-2-picrylhydrazyl (DPPH) clearance was up to (1.17±0.004) 1.0 mg/mL, (84.82%±0.87%) 1.5 mg/mL and (55.01%±0.01%) 1.0 mg/mL, respectivety, and their ABTS+ and DPPH radical scavenging rates were significantly higher than those of germ proteins (p<0.05). In addition, for the hydrolysis capacity of different proteases differs, pepsin had the greatest hydrolysis capacity while neutral protease had the least. The antioxidant capacity of germ protein polypeptides correlated with their molecular weight, but it is not necessarily the case that the smaller the molecular weight of a protein peptide had the better antioxidant effect. The results of these experiments provide a theoretical basis for further research on the antioxidant polypeptides of wheat germ in the Hetao.