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In Vivo Analysis of fadB Homologous Enzymes Involved in Biosynthesis of Polyhydroxyalkanoates in Recombinant Escherichia coli  

최종일 (한국과학기술원 생명화학공학과, 생물공정연구센터 및 대사공학 국가지정연구실)
박시재 (한국과학기술원 생명화학공학과, 생물공정연구센터 및 대사공학 국가지정연구실)
이상엽 (한국과학기술원 바이오시스템학과)
Publication Information
KSBB Journal / v.19, no.4, 2004 , pp. 331-334 More about this Journal
Abstract
In vivo characterization of FadB homologous enzymes including PaaG, YdbU and YgfG for medium-chain-length (MCL) polyhydroxyalkanoate (PHA) biosynthesis was carried out in fadB mutant Escherichia coli. Previously, it was reported that amplification of FadB homologous enzymes such as PaaG and YdbU in fadB mutant E. coli resulted in enhanced biosynthesis of MCL-PHA by greater than two fold compared with control strain. In this study, we constructed paaG fadB double mutant E. coli WB114 and ydbU fadB double mutant E. coli WB115 to investigate the roles of PaaG and YdbU in biosynthesis of MCL-PHA. Inactivation of paaG and ydbU genes in fadB mutant E. coli harboring Pseudomonas sp. 61-3 phaC2 gene reduced the MCL-PHA production to 0.16 and 0.16 PHA g/L, respectively from 2 g/L of sodium decanoate, which are much lower than 0.43 PHA g/L obtained with fadB mutant E. coli WB101 harboring the phaC2 gene. Also, we identified new FadB homologous enzyme YgfG, and examined its roles by overexpression of ygfG and construction of ygfG fadB double mutant E. coli WB113.
Keywords
paaG; ydbU; ygfG; fadB; recombinant E. coli; PHA;
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Times Cited By KSCI : 1  (Citation Analysis)
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