A substantial portion of the human population has immune hypersensitivities to various food materials. Soybean is one of the most common foods involved in such hypersensitivity reactions, especially in younger children. In this study, we investigated the effect of peptic and chymotryptic hydrolysis on the allergenicity of the 11S soybean globulin, which is the primary soybean allergen. The 11S globulin is composed of both acidic and basic polypeptides, and we found that the acidic polypeptide was effectively hydrolyzed, while basic polypeptide was more resistant to hydrolysis. The 11S globulin hydrolysate was size-fractionated by gel filtration, and 9 of the fractions obtained were tested for allergenicity against sera from 6 soybean-allergenic patients. The overall allergenicity of soybean 11S globulin was reduced by peptic and chymotryptic hydrolysis, although a gel filtration fraction with a major peptide of 20 kDa was highly immunoreactive. Hydrolyzed fragments of less than about 20 kDa were not immunoreactive.

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