Effect of extrusion temperature on antigenicity and structure of soybean protein isolate
In order to provide reference for the development of desensitization technology of soybean protein,the antigenicity,SDS-PAGE,amino acid composition,solubility,UV absorption spectra,endogenous fluorescence spectra and surface hydrophobicity of the soybean protein isolate(SPI)extruded at different extrusion temperatures.The results showed that the antigenicity of SPI decreased first and then increased with the increase of extrusion temperature,and the antigenicity of SPI decreased most significantly at 145 ℃.The α,α'and βsubunits of the antigen protein β-conglycinin and the acidic and basic subunits of glycinin in SPI were significantly degraded.The amino acid composition and the ratio of essential amino acids to total amino acids of SPI had no obvious change,and the nutritional characteristics of SPI remained good.After extrusion,the solubility of SPI decreased,and hydrogen bond,disulfide bond and hydrophobic interaction were the molecular forces that maintained SPI spatial structure,in which hydrogen bond played the main role.The UV and endogenous fluorescence spectra of SPI extruded showed different degrees of redshift,the UV absorption intensity and fluorescence intensity changed,the surface hydrophobicity decreased significantly,and the tertiary structure of SPI changed.In conclusion,extrusion can reduce the antigenicity of SPI to a certain extent and affect its spatial structure.
soybean protein isolateextrusionantigenicityprotein structure
万方数据
维普
