Overexpression of Dioxygenase Encoding Gene Accelerates the Phenolic Aldehyde Conversion and Ethanol Fermentability of Zymomonas mobilis.


Journal

Applied biochemistry and biotechnology
ISSN: 1559-0291
Titre abrégé: Appl Biochem Biotechnol
Pays: United States
ID NLM: 8208561

Informations de publication

Date de publication:
Sep 2021
Historique:
received: 25 01 2021
accepted: 22 03 2021
pubmed: 8 4 2021
medline: 30 9 2021
entrez: 7 4 2021
Statut: ppublish

Résumé

NADH-dependent reductase enzyme catalyzes the phenolic aldehyde conversion and correspondingly improves the ethanol fermentability of the ethanologenic Zymomonas mobilis. This study constructed the transcriptional landscape of mono/dioxygenase genes in Z. mobilis ZM4 under the stress of the toxic phenolic aldehyde inhibitors of 4-hydroxybenzaldehyde, syringaldehyde, and vanillin. One specific dioxygenase encoding gene ZMO1721 was differentially expressed by 3.07-folds under the stress of 4-hydroxybenzaldehyde among the eleven mono/dioxygenase genes. The purified ZMO1721 shared 99.9% confidence and 48.0% identity with the oxidoreductase in Rhodoferax ferrireducens T118 was assayed and the NADH-dependent reduction activity was confirmed for phenolic aldehyde vanillin conversion. The ZMO1721 gene was then overexpressed in Z. mobilis ZM4 and the 4-hydroxybenzaldehyde conversion rate was accelerated. The cell growth, glucose consumption, and ethanol productivity of Z. mobilis ZM4 were also improved by ZMO1721 overexpression. The genes identified on improving phenolic aldehyde tolerance and ethanol fermentability in this study could be used as the synthetic biology tools for modification of ethanologenic strains.

Identifiants

pubmed: 33826067
doi: 10.1007/s12010-021-03551-7
pii: 10.1007/s12010-021-03551-7
doi:

Substances chimiques

Aldehydes 0
Bacterial Proteins 0
Ethanol 3K9958V90M
Dioxygenases EC 1.13.11.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

3017-3027

Subventions

Organisme : Natural Science Foundation of Jiangxi
ID : 20192BAB204002
Organisme : Doctor Science Research Foundation of Jiujiang University
ID : 8879524

Informations de copyright

© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

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Auteurs

Xia Yi (X)

Jiangxi Provincial Key Laboratory of Systems Biomedicine, Jiujiang University, 17 Lufeng Road, Jiujiang, 332000, China. yixia@mail.ecust.edu.cn.

Jun Mei (J)

Jiangxi Provincial Key Laboratory of Systems Biomedicine, Jiujiang University, 17 Lufeng Road, Jiujiang, 332000, China.

Ling Lin (L)

Jiangxi Provincial Key Laboratory of Systems Biomedicine, Jiujiang University, 17 Lufeng Road, Jiujiang, 332000, China.

Wei Wang (W)

State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.

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