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Title 

Identification and utilization of a 1,3-propanediol oxidoreductase isoenzyme for production of 1,3-propanediol from glycerol in Klebsiella pneumoniae

 

크렙시엘라 뉴모니아 유래 신규 1,3-프로판디올 옥시더리덕타제 효소

Authors 

Jeong Woo SeoM Y SeoBaek Rock OhSun Yeon HeoJin Oh BaekD RairakhwadaL H LuoWon Kyung HongChul Ho Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

2010

Citation 

Applied Microbiology and Biotechnology, vol. 85, no. 3, pp. 659-666

Keywords 

1,3-Propanediol1,3-Propanediol oxidoreductase isoenzymeGlycerol metabolismKlebsiella pneumoniae

Abstract 

In a previous study, we showed that 1,3-propanediol (1,3-PD) was still produced from glycerol by the Klebsiella pneumoniae mutant strain defective in 1,3-PD oxidoreductase (DhaT), although the production level was lower compared to the parent strain. As a potential candidate for another putative 1,3-PD oxidoreductase, we identified and characterized a homolog of Escherichia coli yqhD (88% homology in amino acid sequence), which encodes an alcohol dehydrogenase and is well known to replace the function of DhaT in E. coli. Introduction of multiple copies of the yqhD homolog restored 1,3-PD production in the mutant K. pneumoniae strain defective in DhaT. In addition, by-product formation was still eliminated in the recombinant strain due to the elimination of the glycerol oxidative pathway. An increase in NADP-dependent 1,3-PD oxidoreductase activity was observed in the recombinant strain harboring multiple copies of the yqhD homolog. The level of 1,3-PD production during batch fermentation in the recombinant strain was comparable to that of the parent strain; further engineering can generate an industrial strain producing 1,3-propanediol.

ISSN 

0175-7598

Link 

http://dx.doi.org/10.1007/s00253-009-2123-4

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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