Engineering cascade biocatalysis in whole cells for syringic acid bioproduction.


Journal

Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812

Informations de publication

Date de publication:
01 Jun 2024
Historique:
received: 29 03 2024
accepted: 25 05 2024
medline: 2 6 2024
pubmed: 2 6 2024
entrez: 2 6 2024
Statut: epublish

Résumé

Syringic acid (SA) is a high-value natural compound with diverse biological activities and wide applications, commonly found in fruits, vegetables, and herbs. SA is primarily produced through chemical synthesis, nonetheless, these chemical methods have many drawbacks, such as considerable equipment requirements, harsh reaction conditions, expensive catalysts, and numerous by-products. Therefore, in this study, a novel biotransformation route for SA production was designed and developed by using engineered whole cells. An O-methyltransferase from Desulfuromonas acetoxidans (DesAOMT), which preferentially catalyzes a methyl transfer reaction on the meta-hydroxyl group of catechol analogues, was identified. The whole cells expressing DesAOMT can transform gallic acid (GA) into SA when S-adenosyl methionine (SAM) is used as a methyl donor. We constructed a multi-enzyme cascade reaction in Escherichia coli, containing an endogenous shikimate kinase (AroL) and a chorismate lyase (UbiC), along with a p-hydroxybenzoate hydroxylase mutant (PobA Overall, we designed a multi-enzyme cascade in E. coli for SA biosynthesis by using resting or growing whole cells. This work identified an O-methyltransferase (DesAOMT), which can catalyze the methylation of GA to produce SA. The multi-enzyme cascade containing four enzymes expressed in an engineered E. coli for synthesizing of SA from SHA. The metabolic system of the strain and biotransformation conditions influenced catalytic efficiency. This study provides a new green route for SA biosynthesis.

Sections du résumé

BACKGROUND BACKGROUND
Syringic acid (SA) is a high-value natural compound with diverse biological activities and wide applications, commonly found in fruits, vegetables, and herbs. SA is primarily produced through chemical synthesis, nonetheless, these chemical methods have many drawbacks, such as considerable equipment requirements, harsh reaction conditions, expensive catalysts, and numerous by-products. Therefore, in this study, a novel biotransformation route for SA production was designed and developed by using engineered whole cells.
RESULTS RESULTS
An O-methyltransferase from Desulfuromonas acetoxidans (DesAOMT), which preferentially catalyzes a methyl transfer reaction on the meta-hydroxyl group of catechol analogues, was identified. The whole cells expressing DesAOMT can transform gallic acid (GA) into SA when S-adenosyl methionine (SAM) is used as a methyl donor. We constructed a multi-enzyme cascade reaction in Escherichia coli, containing an endogenous shikimate kinase (AroL) and a chorismate lyase (UbiC), along with a p-hydroxybenzoate hydroxylase mutant (PobA
CONCLUSION CONCLUSIONS
Overall, we designed a multi-enzyme cascade in E. coli for SA biosynthesis by using resting or growing whole cells. This work identified an O-methyltransferase (DesAOMT), which can catalyze the methylation of GA to produce SA. The multi-enzyme cascade containing four enzymes expressed in an engineered E. coli for synthesizing of SA from SHA. The metabolic system of the strain and biotransformation conditions influenced catalytic efficiency. This study provides a new green route for SA biosynthesis.

Identifiants

pubmed: 38824548
doi: 10.1186/s12934-024-02441-x
pii: 10.1186/s12934-024-02441-x
doi:

Substances chimiques

Gallic Acid 632XD903SP
syringic acid E390O181H5
Methyltransferases EC 2.1.1.-
Shikimic Acid 29MS2WI2NU

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

162

Informations de copyright

© 2024. The Author(s).

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Auteurs

Xin Liu (X)

School of Life Science, Beijing Institute of Technology, No 5 Zhongguancun South Street, Haidian District, Beijing, 100081, China.

Yi An (Y)

School of Life Science, Beijing Institute of Technology, No 5 Zhongguancun South Street, Haidian District, Beijing, 100081, China.

Haijun Gao (H)

School of Life Science, Beijing Institute of Technology, No 5 Zhongguancun South Street, Haidian District, Beijing, 100081, China. hj_gao@bit.edu.cn.

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Classifications MeSH