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Substantially Complete Removal of Three Major Allergenic Soybean Proteins (Gly mBd 30K,Gly mBd 28K, and theα-Subunit of Conglycinin) from Soy Protein by Using a Mutant Soybean, Tohoku 124
Author(s) -
Masahiko Samoto,
Yôichi Fukuda,
Koji Takahashi,
Kohsei Tabuchi,
Miki HIEMORI,
Hideaki Tsuji,
Tadashi Ogawa,
Yukio Kawamura
Publication year - 1997
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.61.2148
Subject(s) - protein subunit , cultivar , soy protein , chemistry , monoclonal antibody , storage protein , molecular mass , antibody , food science , biochemistry , biology , genetics , horticulture , gene , enzyme
A wild-type soybean contains three major allergenic proteins, Gly m Bd 30K, the α-subunit of conglycinin, and Gly m Bd 28K. A genetically mutated soybean (Tohoku 124), which was originally developed as a cultivar lacking the α- and α'-subunits of conglycinin, was also found to lack Gly m Bd 28K from immunoblot analysis using monoclonal antibodies specific to Gly m Bd 28K. This finding indicates the possibility to prepare soy milk and soy proteins containing none of the three major allergenic soybean proteins from this cultivar. By applying the previous removal procedure [Samoto et al., Biosci. Biotech. Biochem., 60, 1911-1913 (1996)] to Tohoku 124, the substantially complete removal of the three major allergenic proteins from the soy milk was attained. The removal rates of Gly m Bd 30K, α-subunit of conglycinin, and Gly m Bd 28K were 99.8, 100, and 100%, respectively.

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