Improved technologies to produce heterologous proteins in recombinant Escherichia coli.
Yong-Cheol Park, Dae-Hyuk Kweon, Dae-Hee Lee and Jin-Ho Seo*
Korean Journal of Biotechnology and Bioengineering 16(1): 1-10. 2001.2.28.
Escherichia coli has been used as an expression work horse for foreign genes. This article summarized recent development in genetic engineering techniques for overproduction of medical proteins and industrial enzymes. Special emphasis was placed upon research activities concerning folding and refolding of inclusion bodies at genetic and fermentation levels. Plasmid and mRNA stabilization, development of strong inducible promoters, modification of translational elements and reduction of rpoteolytic degradation were carried out to elevate an expression level of a target protein. Optimization of culture conditions, improvement of denaturation and renaturation steps and coexpression of molecular chaperones or foldase were accomplished to produce active proteins in soluble form. Fusion protein systems with selective separation and surface display technology were also performed in an effort to make the E. coli expression system more effective and versatile.
Contact Us
Science Building Room No. 204-205, Kookmin University 861-1 Jeongrung-dong, Sungbuk-gu, Seoul 136-702 Tel: +82-2-910-5596(5462), Fax: +82-2-910-5739 E-mail: ycpark@kookmin.ac.kr