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The separation and identification of the residual antigenic fragments in soy protein hydrolysates

Journal of Food Biochemistry (Article in Press)Guanhao Bu, Ting Huang, Tanghao Li

Abstract: Soybean is one of the major food allergens. In this study, soy protein isolate was hydrolyzed by Neutrase and Flavourzyme. The hydrolysates were separated by ultrafiltration and ionexchange chromatography. The antigenicity of proteins was determined by indirect competitive ELISA. The molecular weight distribution was characterized by SDSPAGE. The amino acid sequence of chromatography fractions was analyzed by LCMS. The results showed that proteins with >50kDa in hydrolysates had the highest antigenicity and were further separated into F1F5 fragments by ionexchange chromatography. Fragment F4, which was the most antigenic, was analyzed by LCMS. The results of mass spectrometry showed that most of the peptides that contained antigen epitopes in chromatography fraction F4 belonged to glycinin subunits. The antigenicity of soy protein was reduced by enzymatic hydrolysis, but glycinin showed resistance to enzymatic hydrolysis.

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