Abstract: Soybean protein has high nutritional value and has been widely used in many fields.However,Soybean protein may cause harm to the human body because of the allergic reactions.The combination of high pressure homogenization and enzymatic hydrolysis treatment is an effective modification method.In this work,soy protein isolates were treated with different high-pressure homogenization conditions and then enzymatic digested with alkaline protease and neutral protease.The results showed that the combination of high-pressure homogenization and enzymatic hydrolysis could significantly reduce the antigenicity of soybean major antigen proteins.The results of ELISA showed that the antigen inhibition rate of β-conglycinin and glycinin were reduced by 44.38% and 19.93% respectively after high-pressure homogeneous and enzymatic treatment.Fourier infrared results showed that the content of α-helix of the treated samples decreased while the irregular curl increased.The surface hydrophobicity results indicated that the spatial structure of soybean protein was changed,and the tertiary and quarternary structure of protein was destroyed.It was concluded that changes in the amino acid sequence and spatial structure of proteins would affect the antigenicity of antigen due to the hiding or masking of antigenic epitopes.