Earticle

초록

영어

The purpose of this research is to develop new strains for producing more fatty acids by improving fatty acid biosynthesis mechanism in Escherichia coli. β-Ketoacyl acyl carrier protein synthase III (fabH) is the enzyme that catalyze the first step in the synthesis of fatty acids with acetyl-CoA carboxylase (accABC) and malonyl-CoA: acyl carrier protein (fabD) acyltransferase in Escherichia coli MG1655. fabH, accABC and fabD genes were cloned and characterized. The enzyme of fabH gene leads to increase short-chain-length fatty acids and shows strong preference for acetyl-CoA, and produces only straight chain fatty acids (SCFAs). β-Ketoacyl acyl carrier protein synthase III (fabH) is also thought to play a major role in determining fatty acids type and compositions. The fabH, accABC and fabD genes were identified as homologous gene of E. coli MG1655 through a metabolic pathway. The recombinant E. coli MG1655 containing the fabH or accABC::fabD or accABC::fabD::fabH gene-inserted expression vector (pTrc99A) was constructed. To analyze the effects of genes overexpression, analysis of intermediate products and fatty acids was performed. As a result, recombinant strains produced more acetic acid, malonic acid and fatty acids than its wild type E. coli did.

키워드

저자

• Sunhee LEE [ Department of Chemical and Biomolecular Engineering, Sogang University, Seoul 121-742. ]
• Eunyoung JEON [ Department of Chemical and Biomolecular Engineering, Sogang University, Seoul 121-742. ]
• Jinwon LEE [ Department of Chemical and Biomolecular Engineering, Sogang University, Seoul 121-742. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576