@article {Wang:2014:0954-0105:301,
title = "Reduction of the allergenic protein in soybean meal by enzymatic hydrolysis",
journal = "Food and Agricultural Immunology",
parent_itemid = "infobike://tandf/cfai",
publishercode ="tandf",
year = "2014",
volume = "25",
number = "3",
publication date ="2014-07-03T00:00:00",
pages = "301-310",
itemtype = "ARTICLE",
issn = "0954-0105",
eissn = "1465-3443",
url = "https://www.ingentaconnect.com/content/tandf/cfai/2014/00000025/00000003/art00001",
doi = "doi:10.1080/09540105.2013.782268",
keyword = "ELISA, soybean meal, proteolysis, soy allergenic protein, protein subunit",
author = "Wang and Li and Yuan and Zhao and Cui and Hu and Wang",
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 , and
-subunits of -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 , subunits
of -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 , subunits of -conglycinin and acidic subunit of glycinin
decreased significantly, that by trypsin did not. The content of immune-reactive -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.",
}