• The Korean Journal of Food And Nutrition
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• v.9 no.4
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• pp.404-408
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• 1996

One of the major objectives of the food industry is the enrichment of the functional properties and nutritional value of soybean protein. To attain this goal, an expression system of cDNA encoding native and protein-engineered soybean proteins in a microorganism must be developed and the function then ability of self-assembly and the functionalities of the expressed proteins should be evaluated before the modified genes are transfered to soybean plants. The pro-$\beta$-conglycinin synthesized in E. coli BL21(DE3) comprised approximately 20% of the total bacterial proteins and the expressed protein are formed soluble and trimer such as native protein in E. coli cells. The highly expressed protein was purified to homogeneity by salt precipitation with 20~40$ Ammonium sulfate ion-exchange chromatography with Q-Sepharose and hydrophobic column chromatography with Butyltoyopearl. Therefore, we concluded that the high-level expression system of $\beta$-conglycinin cDNA was established and a relatively simple and rapid method for purifying pro-$\beta$-conglicinin was also developed.