Production of a recombinant membrane protein in an Escherichia coli strain for the whole cell biosynthesis of phenylacetic acids

[Display omitted] The styrene oxide isomerase (SOI) represents a membrane-bound enzyme of the microbial styrene degradation pathway and has been discussed as promising biocatalyst. It catalyzes the isomerization of styrene oxide to phenylacetaldehyde. In this study a styC gene, which encodes the SOI...

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Published in:Biotechnology reports (Amsterdam, Netherlands) Vol. 7; no. C; pp. 38 - 43
Main Authors: Oelschlägel, Michel, Heiland, Claudia, Schlömann, Michael, Tischler, Dirk
Format: Journal Article
Language:English
Published: Netherlands Elsevier B.V 01.09.2015
Elsevier
Subjects:
biocatalysts
biomass
biosynthesis
Epoxide isomerase
Escherichia coli
genes
isomerization
membrane proteins
oxides
phenylacetaldehyde
phenylacetic acid
recombinant proteins
Rhodococcus
Rhodococcus opacus
styrene
Styrene oxide isomerase
Styrene oxide isomerase
Rhodococcus
Epoxide isomerase
ISSN:2215-017X, 2215-017X
Online Access:Get full text
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Summary:[Display omitted] The styrene oxide isomerase (SOI) represents a membrane-bound enzyme of the microbial styrene degradation pathway and has been discussed as promising biocatalyst. It catalyzes the isomerization of styrene oxide to phenylacetaldehyde. In this study a styC gene, which encodes the SOI of Rhodococcus opacus 1CP, was optimized for optimal expression in Escherichia coli BL21(DE3) pLysS. The expression of this synthetic styC was investigated and subsequently optimized. Highly active biomass was obtained yielding an SOI activity of 44.5±8.7Umg−1 after 10h. This represents the highest SOI activity reported for crude cell extracts of SOI-containing bacterial strains. Remarkably, this biomass can be applied as whole cell biocatalyst for the production of phenylacetic acids from styrene oxides. In the case of non-substituted styrene oxide, nearly 730mgl−1 phenylacetic acid (∼85% yield) was formed over a period of 20 days.
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ISSN:2215-017X
2215-017X
DOI:10.1016/j.btre.2015.05.002