Sucrose as an electron source for cofactor regeneration in recombinant Escherichia coli expressing invertase and a Baeyer Villiger monooxygenase.
E. coli
Synechocystis sp.
Baeyer–Villiger monooxygenase
Cyanobacteria
Oxidation
Sucrose
Whole-cell biotransformation
Journal
Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812
Informations de publication
Date de publication:
12 Aug 2024
12 Aug 2024
Historique:
received:
08
03
2024
accepted:
08
07
2024
medline:
13
8
2024
pubmed:
13
8
2024
entrez:
12
8
2024
Statut:
epublish
Résumé
The large-scale biocatalytic application of oxidoreductases requires systems for a cost-effective and efficient regeneration of redox cofactors. These represent the major bottleneck for industrial bioproduction and an important cost factor. In this work, co-expression of the genes of invertase and a Baeyer-Villiger monooxygenase from Burkholderia xenovorans to E. coli W ΔcscR and E. coli BL21 (DE3) enabled efficient biotransformation of cyclohexanone to the polymer precursor, ε-caprolactone using sucrose as electron source for regeneration of redox cofactors, at rates comparable to glucose. E. coli W ΔcscR has a native csc regulon enabling sucrose utilization and is deregulated via deletion of the repressor gene (cscR), thus enabling sucrose uptake even at concentrations below 6 mM (2 g L Herein, we show a proof of concept where the co-expression of invertase for both E. coli hosts was sufficient for efficient sucrose utilization to sustain cofactor regeneration in the Baeyer-Villiger oxidation of cyclohexanone. Using E. coli W ΔcscR, a specific activity of 37 U g Results show that sucrose can be an alternative electron source to drive whole-cell biotransformations in recombinant E. coli strains opening novel strategies for sustainable chemical production.
Sections du résumé
BACKGROUND
BACKGROUND
The large-scale biocatalytic application of oxidoreductases requires systems for a cost-effective and efficient regeneration of redox cofactors. These represent the major bottleneck for industrial bioproduction and an important cost factor. In this work, co-expression of the genes of invertase and a Baeyer-Villiger monooxygenase from Burkholderia xenovorans to E. coli W ΔcscR and E. coli BL21 (DE3) enabled efficient biotransformation of cyclohexanone to the polymer precursor, ε-caprolactone using sucrose as electron source for regeneration of redox cofactors, at rates comparable to glucose. E. coli W ΔcscR has a native csc regulon enabling sucrose utilization and is deregulated via deletion of the repressor gene (cscR), thus enabling sucrose uptake even at concentrations below 6 mM (2 g L
RESULTS
RESULTS
Herein, we show a proof of concept where the co-expression of invertase for both E. coli hosts was sufficient for efficient sucrose utilization to sustain cofactor regeneration in the Baeyer-Villiger oxidation of cyclohexanone. Using E. coli W ΔcscR, a specific activity of 37 U g
CONCLUSIONS
CONCLUSIONS
Results show that sucrose can be an alternative electron source to drive whole-cell biotransformations in recombinant E. coli strains opening novel strategies for sustainable chemical production.
Identifiants
pubmed: 39135032
doi: 10.1186/s12934-024-02474-2
pii: 10.1186/s12934-024-02474-2
doi:
Substances chimiques
beta-Fructofuranosidase
EC 3.2.1.26
Sucrose
57-50-1
Mixed Function Oxygenases
EC 1.-
Cyclohexanones
0
cyclohexanone
5QOR3YM052
Recombinant Proteins
0
caprolactone
56RE988L1R
Caproates
0
Lactones
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
227Subventions
Organisme : European Union, FET Open
ID : 899576
Organisme : European Union, FET Open
ID : 899576
Organisme : European Union, FET Open
ID : 899576
Organisme : European Union, FET Open
ID : 899576
Organisme : European Union, FET Open
ID : 899576
Organisme : European Union, FET Open
ID : 899576
Organisme : Novo Nordisk Foundation
ID : NNF20OC0064371
Informations de copyright
© 2024. The Author(s).
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