Development of glutaric acid production consortium system with α-ketoglutaric acid regeneration by glutamate oxidase in Escherichia coli.
Catalase
Glutamate oxidase
Glutaric acid
Optimization
α-Ketoglutaric acid
Journal
Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761
Informations de publication
Date de publication:
Feb 2020
Feb 2020
Historique:
received:
08
08
2019
revised:
10
09
2019
accepted:
07
10
2019
entrez:
26
12
2019
pubmed:
26
12
2019
medline:
1
5
2020
Statut:
ppublish
Résumé
Glutaric acid is a C5 dicarboxylic acid that can be used as a building block for bioplastics. Although high concentrations of glutaric acid can be produced by fermentation or bioconversion, a large amount of α-ketoglutaric acid (α-KG) is necessary to accept the amine group from 5-aminovaleric acid. To decrease the demand for α-KG, we introduced l-glutamate oxidase (GOX) from Streptomyces mobaraensis in our previous system for cofactor regeneration in combination with a glutaric acid production system from 5-aminovaleric acid. To enhance glutaric acid production, critical factors were optimized such as the expression vector, pH, temperature, and cell ratio. As a result, the demand for α-KG was decreased by more than 6-fold under optimized conditions. Additionally, the effect of catalase was also demonstrated by blocking the degradation of α-KG to succinic acid because of the hydrogen peroxide. Finally, 468.5 mM glutaric acid was produced from 800 mM 5-aminovaleric acid using only 120 mM α-KG. Moreover, this system containing davBA, gabTD-nox, and gox can be applied to produce glutaric acid from L-lysine by reusing α-KG with GOX. This improved cofactor regeneration system has a potential to apply much larger production of glutaric acid.
Identifiants
pubmed: 31874692
pii: S0141-0229(19)30184-X
doi: 10.1016/j.enzmictec.2019.109446
pii:
doi:
Substances chimiques
Glutarates
0
Ketoglutaric Acids
0
Catalase
EC 1.11.1.6
Amino Acid Oxidoreductases
EC 1.4.-
L-glutamate oxidase
EC 1.4.3.11
glutaric acid
H849F7N00B
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
109446Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.