Impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by Klebsiella pneumoniae
1,3-Propanediol (1,3-PDO) is an important compound that is mainly used in industry for polymer production. Fermentation of 1,3-PDO from glycerol by Klebsiella pneumoniae is accompanied by formation of 2,3-butanediol (2,3-BDO) as one of the main byproduct. The first step in the formation of 2,3-BDO f...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6481767/ https://www.ncbi.nlm.nih.gov/pubmed/31017890 http://dx.doi.org/10.1371/journal.pone.0200978 |
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author | Zhou, Sheng Huang, Youhua Mao, Xinliang Li, Lili Guo, Chuanyu Gao, Yongli Qin, Qiwei |
author_facet | Zhou, Sheng Huang, Youhua Mao, Xinliang Li, Lili Guo, Chuanyu Gao, Yongli Qin, Qiwei |
author_sort | Zhou, Sheng |
collection | PubMed |
description | 1,3-Propanediol (1,3-PDO) is an important compound that is mainly used in industry for polymer production. Fermentation of 1,3-PDO from glycerol by Klebsiella pneumoniae is accompanied by formation of 2,3-butanediol (2,3-BDO) as one of the main byproduct. The first step in the formation of 2,3-BDO from pyruvate is catalyzed by acetolactate synthase (ALS), an enzyme that competes with 1,3-PDO oxidoreductase for the cofactor NADH. This study aimed to analyze the impact of engineering the 2,3-BDO formation pathway via inactivation of ALS on 1,3-PDO fermentation by K. pneumoniae HSL4. An ALS mutant was generated using Red recombinase assisted gene replacement. The ALS specific activities of K. pneumoniae ΔALS were notably lower than that of the wild-type strain. Fed-batch fermentation of the mutant strain resulted in a 1,3-PDO concentration, productivity and conversion of 72.04 g L(–1), 2.25 g L(–1) h(–1), and 0.41 g g(–1), increase by 4.71%, 4.65% and 1.99% compared with the parent strain. Moreover, inactivation of ALS decreased meso-2,3-BDO formation to trace amounts, significantly increased 2S,3S-BDO and lactate production, and a pronounced redistribution of intracellular metabolic flux was apparent. |
format | Online Article Text |
id | pubmed-6481767 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-64817672019-05-07 Impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by Klebsiella pneumoniae Zhou, Sheng Huang, Youhua Mao, Xinliang Li, Lili Guo, Chuanyu Gao, Yongli Qin, Qiwei PLoS One Research Article 1,3-Propanediol (1,3-PDO) is an important compound that is mainly used in industry for polymer production. Fermentation of 1,3-PDO from glycerol by Klebsiella pneumoniae is accompanied by formation of 2,3-butanediol (2,3-BDO) as one of the main byproduct. The first step in the formation of 2,3-BDO from pyruvate is catalyzed by acetolactate synthase (ALS), an enzyme that competes with 1,3-PDO oxidoreductase for the cofactor NADH. This study aimed to analyze the impact of engineering the 2,3-BDO formation pathway via inactivation of ALS on 1,3-PDO fermentation by K. pneumoniae HSL4. An ALS mutant was generated using Red recombinase assisted gene replacement. The ALS specific activities of K. pneumoniae ΔALS were notably lower than that of the wild-type strain. Fed-batch fermentation of the mutant strain resulted in a 1,3-PDO concentration, productivity and conversion of 72.04 g L(–1), 2.25 g L(–1) h(–1), and 0.41 g g(–1), increase by 4.71%, 4.65% and 1.99% compared with the parent strain. Moreover, inactivation of ALS decreased meso-2,3-BDO formation to trace amounts, significantly increased 2S,3S-BDO and lactate production, and a pronounced redistribution of intracellular metabolic flux was apparent. Public Library of Science 2019-04-24 /pmc/articles/PMC6481767/ /pubmed/31017890 http://dx.doi.org/10.1371/journal.pone.0200978 Text en © 2019 Zhou et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Zhou, Sheng Huang, Youhua Mao, Xinliang Li, Lili Guo, Chuanyu Gao, Yongli Qin, Qiwei Impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by Klebsiella pneumoniae |
title | Impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by Klebsiella pneumoniae |
title_full | Impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by Klebsiella pneumoniae |
title_fullStr | Impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by Klebsiella pneumoniae |
title_full_unstemmed | Impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by Klebsiella pneumoniae |
title_short | Impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by Klebsiella pneumoniae |
title_sort | impact of acetolactate synthase inactivation on 1,3-propanediol fermentation by klebsiella pneumoniae |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6481767/ https://www.ncbi.nlm.nih.gov/pubmed/31017890 http://dx.doi.org/10.1371/journal.pone.0200978 |
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