Earticle

초록

영어

Although the propanediol utilization: CoA dependent propionaldehyde dehydrogenase (PduP) has been suggested to be involved in the de novo biosynthetic mechanism of 3-hydroxypropionic acid (3-HP) in glycerol- fermenting process, it is still poorly understood. Thus in here, we disrupted the pduP gene on the chromosomal DNA of K. pneumoniae for investigating the enzyme effect on 3-HP production. The mutant strain still produce 3-HP but accumulates 3-hydroxypropionaldehyde (3-HPA) after consumed glycerol completely that resulted in cell death as well as decreased final titer of 3-HP production. To analyze the enzyme properties, pduP was cloned and expressed in E. coli. Recombinant K. pneumoniae PduP exhibited broad substrate specificity including 3-HPA and utilized both NAD+ and NADP+ as cofactors. Among various aldehyde substrates tested, the specific activity was highest for propionaldehyde (PA), at pH 8.0 and 37°C. The Km and Vmax values for PA in the presence of NAD+ were 0.22 mM and 0.09 U mg-1, respectively. When pduP was overexpressed in K. pneumoniae, 3-HP production remarkably increased from 1.0g L-1 to 1.8 g L-1. The presentation demonstrated firstly in the role of PduP in cellular biosynthesis of 3-HP from glycerol.

키워드

저자

• Lian Hua LUO [ Microbe-based Fusion Technology Research Center, Jeonbuk Branch Institute, KRIBB, Jeonbuk 580-185. ]
• Jeong-Woo Seo SEO [ Microbe-based Fusion Technology Research Center, Jeonbuk Branch Institute, KRIBB, Jeonbuk 580-185. ]
• Dae-Hyuk Kim KIM [ Institute for Molecular Biology and Genetics, Research Center of Bioactive Materials, Chonbuk National University, Chonbuk 561-756. ]
• Chul Ho Kim KIM [ Microbe-based Fusion Technology Research Center, Jeonbuk Branch Institute, KRIBB, Jeonbuk 580-185. ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576