The effects of thermal treatments on the antigenicity and structural properties of soybean glycinin

The effects of thermal treatments on the antigenicity and structural properties of soybean glycinin were investigated. An indirect enzyme-linked immunosorbent assay (iELISA) result indicated that the antigenicity of the soybean glycinin decreased to the lowest level when the heat treatment time was 50 min and the temperature was set at 110°C. The reducing sodium dodecyl sulfate-Gel electrophoresis results showed that the heat treatment had promoted the formation of small molecular weight protein subunits and concentrated protein. The free sulfhydryl (-SH) group of glycinin had increased significantly (p < .05) under the conditions of temperature between 90 and 120°C and 40 to 50 min heat treatments. The maximum fluorescence wavelength of the intrinsic fluorescence also changed significantly when compared with the control. The circular dichroism showed that the number of disordered structures had also increased significantly. These results provided evidence that the heat-induced structural modifications of glycinin will alter the antigenicity of soybean glycinin. PRACTICAL APPLICATIONS: The relationship between antigenicity and structural properties of heat-treated soybean globulin was studied by different protein structural research methods. The results showed that the antigenicity of the protein was minimized at 110°C 50 min, which could be used in food safety production. This study chose to analyze the changes in the antigenicity and structural characteristics of soybean glycinin, both prior to and after heat treatments, for the purpose of promoting the development of low allergenic food products.