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Semi-quantitative Purification and Assessment of Purity of Three Soybean Proteins-Glycinin, beta-Conglycinin and alpha-Conglycinin - by SDS-PAGE Electrophoresis, Densitometry and Immunoblotting


Semi-quantitative Purification and Assessment of Purity of Three Soybean Proteins-Glycinin, beta-Conglycinin and alpha-Conglycinin - by SDS-PAGE Electrophoresis, Densitometry and Immunoblotting



Journal of Food Science and Technology (Mysore) 31(6): 489-493



ISSN/ISBN: 0022-1155

Semi-quantitative purification of the three most antigenic proteins of soybean seeds. e.g., glycinin, beta-conglycinin and alpha-conglycinin, was studied. In first step, fractions were pre-purified by successive precipitations of respective proteins at an appropriate isoelectric point and/or ionic strength. Then, glycinin, beta-conglycinin and alpha-conglycinin fractions were isolated by gel filtration. The procedure was carried out on a semi-preparative scale, and used to purify about 2g glycinin and 1 g each of beta-conglycinin and alpha-conglycinin, from 1 kg of defatted soybean flour. Purity of glycinin. beta-conglycinin and alpha-conglycinin fractions was checked by sodium dodecylsulphate polyacrylamide gel electrophoresis and immunoblots. Contaminants detected in both glycinin (9%) and alpha-conglycinin (4%) fractions, but the beta-conglycinin obtained was pure.

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Accession: 009395085

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