Identification and utilization of a 1,3-propanediol oxidoreductase isoenzyme for production of 1,3-propanediol from glycerol in Klebsiella pneumoniae |
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Authors: | Jeong-Woo Seo Mi-Young Seo Baek-Rock Oh Sun-Yeon Heo Jin-Oh Baek Dina Rairakhwada Lian Hua Luo Won-Kyung Hong Chul Ho Kim |
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Institution: | (1) Molecular Bioprocess Research Center, Jeonbuk Branch Institute, KRIBB, Jeongeup, Jeonbuk, 580-185, South Korea;(2) School of Life Sciences and Biotechnology, Korea University, Seoul, 136-701, South Korea;(3) School of Biological Sciences and Technology, Chonnam National University, Gwangju, 500-757, South Korea;(4) Institute for Molecular Biology and Genetics, Research Center of Bioactive Materials, Chonbuk National University, Jeonju, Chonbuk, 561-756, South Korea; |
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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. |
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