Abstract
The effects of Alcalase and Trypsin hydrolysis on the allergenic protein and its solubility of soybean meal (SBM) were investigated by SDS-PAGE and ELISA. After 10 min of hydrolysis with Alcalase, the solubility of the protein was 87.19%, the α′, α and β-subunits of β-conglycinin disappeared and the acidic and basic subunits of glycinin decreased obviously by SDS-PAGE pattern. However, with Trypsin for 10 min, the solubility of the protein was 72.74%. The contents of α′, α subunits of β-conglycinin decreased slightly in SDS-PAGE, and the acidic and basic subunits of glycinin were almost not affected. For the insoluble hydrolysates prepared by Alcalase, the α′, α subunits of β-conglycinin and acidic subunit of glycinin decreased significantly, that by trypsin did not. The content of immune-reactive β-conglycinin obtained by ELISA was consistent with them. These results confirmed that the allergenic proteins of SBM were more sensitive to Alcalase than to Trypsin.
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