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Molecular cloning, expression, and characterization of acyltransferase from Pseudomonas protegens.

ABSTRACT: The formation of C-C bonds by using CoA independent acyltransferases may have significant impact for novel methods for biotechnology. We report the identification of Pseudomonas strains with CoA-independent acyltransferase activity as well as the heterologous expression of the enzyme in E. coli. The cloning strategies and selected expression studies are discussed. The recombinant acyltransferases were characterized with regard to thermal and storage stability, pH,- and co-solvent tolerance. Moreover, the impact of bivalent metals, inhibitors, and other additives was tested. Careful selection of expression and working conditions led to obtain recombinant acyltransferase form Pseudomonas protegens with up to 11 U mL-1 activity.

SUBMITTER: Schmidt NG

PROVIDER: S-EPMC6013524 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

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Molecular cloning, expression, and characterization of acyltransferase from Pseudomonas protegens.

Schmidt Nina G NG Żądło-Dobrowolska Anna A Ruppert Valerie V Höflehner Christian C Wiltschi Birgit B Kroutil Wolfgang W

Applied microbiology and biotechnology 20180512 14

The formation of C-C bonds by using CoA independent acyltransferases may have significant impact for novel methods for biotechnology. We report the identification of Pseudomonas strains with CoA-independent acyltransferase activity as well as the heterologous expression of the enzyme in E. coli. The cloning strategies and selected expression studies are discussed. The recombinant acyltransferases were characterized with regard to thermal and storage stability, pH,- and co-solvent tolerance. More ...[more]

PMID: 29754162

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