Allergenic proteins of pacific oyster (Crassostrea gigas) were separated and the change of protein molecular weight and antigenicity after proteases treatment were studied.MethodsOyster allergenic protein was isolated by ammonium sulfate precipitation and Sephadex G-75. The oyster allergenic protein was hydrolyzed by animal protein hydrolysis enzyme, papain, and neutrase protease, respectively. The degrees of hydrolysis were assessed by OPA and SDS-PAGE methods. The change of allergenic protein antigenicity were detected by indirect competitive ELISA. ResultsOyster allergenic protein of 40 and 98 kD was separated and the 40 kD protein was used for further studies. The highest hydrolysis degree of (31.87±0.309)% was achieved by papain and the oyster allergy protein band was disappeared in SDS-PAGE analysis. While by animal protein hydrolysis enzyme and neutral protease, the proteolytic degree of oyster allergies were (24.13±0.153)% and (12.43±0.115)%, respectively. The indirect competitive ELISA analysis also showed that the antigenicity of protein were obviously decreased by hydrolysis with these three proteases.ConclusionAntigenicity of oyster allergenic protein could be effectively reduced by papain hydrolysis.