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Glycerol conversion to 1, 3-Propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in Lactobacillus reuteri
In this work, Lactobacillus reuteri has been metabolically engineered for improving 1, 3-propanediol (1, 3-PD) production by the expression of an Escherichia coli alcohol dehydrogenase, yqhD, that is known to efficiently convert the precursor 3-hydroxypropionaldehyde (3-HPA) to 1, 3-PD. The engineer...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Springer
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3256104/ https://www.ncbi.nlm.nih.gov/pubmed/22053913 http://dx.doi.org/10.1186/2191-0855-1-37 |
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author | Vaidyanathan, Hema Kandasamy, Vijayalakshmi Gopal Ramakrishnan, Gopi Ramachandran, KB Jayaraman, Guhan Ramalingam, Subramanian |
author_facet | Vaidyanathan, Hema Kandasamy, Vijayalakshmi Gopal Ramakrishnan, Gopi Ramachandran, KB Jayaraman, Guhan Ramalingam, Subramanian |
author_sort | Vaidyanathan, Hema |
collection | PubMed |
description | In this work, Lactobacillus reuteri has been metabolically engineered for improving 1, 3-propanediol (1, 3-PD) production by the expression of an Escherichia coli alcohol dehydrogenase, yqhD, that is known to efficiently convert the precursor 3-hydroxypropionaldehyde (3-HPA) to 1, 3-PD. The engineered strain exhibited significantly altered formation rates for the product and other metabolites during the fermentation. An increase in the 1, 3-PD specific productivity of 34% and molar yield by 13% was achieved in the clone, relative to the native strain. A concomitant decrease in the levels of toxic intermediate, 3-HPA, was observed, with the specific productivity levels being 25% lesser than that of the native strain. Interestingly, the recombinant strain exhibited elevated rates of lactate and ethanol formation as well as reduced rate of acetate production, compared to the native strain. The preferential utilization of NADPH by YqhD with a possible decrease in the native 1, 3-PD oxidoreductase (NADH-dependent) activity, could have resulted in the diversion of surplus NADH towards increased lactate and ethanol productivities. |
format | Online Article Text |
id | pubmed-3256104 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Springer |
record_format | MEDLINE/PubMed |
spelling | pubmed-32561042012-01-18 Glycerol conversion to 1, 3-Propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in Lactobacillus reuteri Vaidyanathan, Hema Kandasamy, Vijayalakshmi Gopal Ramakrishnan, Gopi Ramachandran, KB Jayaraman, Guhan Ramalingam, Subramanian AMB Express Original In this work, Lactobacillus reuteri has been metabolically engineered for improving 1, 3-propanediol (1, 3-PD) production by the expression of an Escherichia coli alcohol dehydrogenase, yqhD, that is known to efficiently convert the precursor 3-hydroxypropionaldehyde (3-HPA) to 1, 3-PD. The engineered strain exhibited significantly altered formation rates for the product and other metabolites during the fermentation. An increase in the 1, 3-PD specific productivity of 34% and molar yield by 13% was achieved in the clone, relative to the native strain. A concomitant decrease in the levels of toxic intermediate, 3-HPA, was observed, with the specific productivity levels being 25% lesser than that of the native strain. Interestingly, the recombinant strain exhibited elevated rates of lactate and ethanol formation as well as reduced rate of acetate production, compared to the native strain. The preferential utilization of NADPH by YqhD with a possible decrease in the native 1, 3-PD oxidoreductase (NADH-dependent) activity, could have resulted in the diversion of surplus NADH towards increased lactate and ethanol productivities. Springer 2011-11-04 /pmc/articles/PMC3256104/ /pubmed/22053913 http://dx.doi.org/10.1186/2191-0855-1-37 Text en Copyright ©2011 Vaidyanathan et al; licensee Springer. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Vaidyanathan, Hema Kandasamy, Vijayalakshmi Gopal Ramakrishnan, Gopi Ramachandran, KB Jayaraman, Guhan Ramalingam, Subramanian Glycerol conversion to 1, 3-Propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in Lactobacillus reuteri |
title | Glycerol conversion to 1, 3-Propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in Lactobacillus reuteri |
title_full | Glycerol conversion to 1, 3-Propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in Lactobacillus reuteri |
title_fullStr | Glycerol conversion to 1, 3-Propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in Lactobacillus reuteri |
title_full_unstemmed | Glycerol conversion to 1, 3-Propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in Lactobacillus reuteri |
title_short | Glycerol conversion to 1, 3-Propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in Lactobacillus reuteri |
title_sort | glycerol conversion to 1, 3-propanediol is enhanced by the expression of a heterologous alcohol dehydrogenase gene in lactobacillus reuteri |
topic | Original |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3256104/ https://www.ncbi.nlm.nih.gov/pubmed/22053913 http://dx.doi.org/10.1186/2191-0855-1-37 |
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