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 ion-exchange chromatography. The antigenicity of proteins was determined by indirect competitive ELISA. The molecular weight distribution was characterized by SDS-PAGE. The amino acid sequence of chromatography fractions was analyzed by LC-MS. The results showed that proteins with >50kDa in hydrolysates had the highest antigenicity and were further separated into F1 -F5 fragments by ion-exchange chromatography. Fragment F4 , which was the most antigenic, was analyzed by LC-MS. 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. PRACTICAL APPLICATIONS: The identification of residual antigenicity in soy protein hydrolysates by LC-MS provides important information on the resistance mechanism of enzymatic hydrolysis of soybean protein allergens. In addition, the efficient separation of soy protein hydrolysates could be beneficial for developing low-allergenic soybean products.
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