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Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli

Poly(3-hydroxypropionate) (P3HP) is a thermoplastic with great compostability and biocompatibility, and can be produced through several biosynthetic pathways, in which the glycerol pathway achieved the highest P3HP production. However, exogenous supply of vitamin B(12) was required to maintain the a...

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Autores principales: Lacmata, Stephen Tamekou, Kuiate, Jules-Roger, Ding, Yamei, Xian, Mo, Liu, Huizhou, Boudjeko, Thaddée, Feng, Xinjun, Zhao, Guang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5333900/
https://www.ncbi.nlm.nih.gov/pubmed/28253372
http://dx.doi.org/10.1371/journal.pone.0173150
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author Lacmata, Stephen Tamekou
Kuiate, Jules-Roger
Ding, Yamei
Xian, Mo
Liu, Huizhou
Boudjeko, Thaddée
Feng, Xinjun
Zhao, Guang
author_facet Lacmata, Stephen Tamekou
Kuiate, Jules-Roger
Ding, Yamei
Xian, Mo
Liu, Huizhou
Boudjeko, Thaddée
Feng, Xinjun
Zhao, Guang
author_sort Lacmata, Stephen Tamekou
collection PubMed
description Poly(3-hydroxypropionate) (P3HP) is a thermoplastic with great compostability and biocompatibility, and can be produced through several biosynthetic pathways, in which the glycerol pathway achieved the highest P3HP production. However, exogenous supply of vitamin B(12) was required to maintain the activity of glycerol dehydratase, resulting in high production cost. To avoid the addition of VB(12), we have previously constructed a P3HP biosynthetic route with β-alanine as intermediate, and the present study aimed to improve the P3HP production of this pathway. L-aspartate decarboxylase PanD was found to be the rate-limiting enzyme in the β-alanine pathway firstly. To improve the pathway efficiency, PanD was screened from four different sources (Escherichia coli, Bacillus subtilis, Pseudomonas fluorescens, and Corynebacterium glutamicum). And PanD from C. glutamicum was found to have the highest activity, the P3HP production was improved in flask cultivation with this enzyme. To further improve the production, the host strain was screened and the culture condition was optimized. Under optimal conditions, production and content of P3HP reached to 10.2 g/L and 39.1% (wt/wt [cell dry weight]) in an aerobic fed-batch fermentation. To date, this is the highest P3HP production without VB(12).
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spelling pubmed-53339002017-03-10 Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli Lacmata, Stephen Tamekou Kuiate, Jules-Roger Ding, Yamei Xian, Mo Liu, Huizhou Boudjeko, Thaddée Feng, Xinjun Zhao, Guang PLoS One Research Article Poly(3-hydroxypropionate) (P3HP) is a thermoplastic with great compostability and biocompatibility, and can be produced through several biosynthetic pathways, in which the glycerol pathway achieved the highest P3HP production. However, exogenous supply of vitamin B(12) was required to maintain the activity of glycerol dehydratase, resulting in high production cost. To avoid the addition of VB(12), we have previously constructed a P3HP biosynthetic route with β-alanine as intermediate, and the present study aimed to improve the P3HP production of this pathway. L-aspartate decarboxylase PanD was found to be the rate-limiting enzyme in the β-alanine pathway firstly. To improve the pathway efficiency, PanD was screened from four different sources (Escherichia coli, Bacillus subtilis, Pseudomonas fluorescens, and Corynebacterium glutamicum). And PanD from C. glutamicum was found to have the highest activity, the P3HP production was improved in flask cultivation with this enzyme. To further improve the production, the host strain was screened and the culture condition was optimized. Under optimal conditions, production and content of P3HP reached to 10.2 g/L and 39.1% (wt/wt [cell dry weight]) in an aerobic fed-batch fermentation. To date, this is the highest P3HP production without VB(12). Public Library of Science 2017-03-02 /pmc/articles/PMC5333900/ /pubmed/28253372 http://dx.doi.org/10.1371/journal.pone.0173150 Text en © 2017 Lacmata 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
Lacmata, Stephen Tamekou
Kuiate, Jules-Roger
Ding, Yamei
Xian, Mo
Liu, Huizhou
Boudjeko, Thaddée
Feng, Xinjun
Zhao, Guang
Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli
title Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli
title_full Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli
title_fullStr Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli
title_full_unstemmed Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli
title_short Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli
title_sort enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant escherichia coli
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5333900/
https://www.ncbi.nlm.nih.gov/pubmed/28253372
http://dx.doi.org/10.1371/journal.pone.0173150
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