Improved Technologies to Produce Heterologous Proteins in Recombinant Escherichia coli.

재조합 대장균에서 외래단백질 발현을 위한 기술개발

  • 박용철 (서울대학교 협동과정 생물화학공학 전공) ;
  • 권대혁 (서울대학교 식품공학과) ;
  • 이대희 (서울대학교 식품공학과) ;
  • 서진호 (서울대학교 식품공학과)
  • Published : 2001.02.01

Abstract

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.

Keywords

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