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Expanding the set of rhodococcal Baeyer-Villiger monooxygenases by high-throughput cloning, expression and substrate screening

Riebel, A., Dudek, H. M., de Gonzalo, G., Stepniak, P., Rychlewski, L. & Fraaije, M. W., Sep-2012, In : Applied Microbiology and Biotechnology. 95, 6, p. 1479-1489 11 p.

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DOI

  • A. Riebel
  • H. M. Dudek
  • G. de Gonzalo
  • P. Stepniak
  • L. Rychlewski
  • M. W. Fraaije

To expand the available set of Baeyer-Villiger monooxygenases (BVMOs), we have created expression constructs for producing 22 Type I BVMOs that are present in the genome of Rhodococcus jostii RHA1. Each BVMO has been probed with a large panel of potential substrates. Except for testing their substrate acceptance, also the enantioselectivity of some selected BVMOs was studied. The results provide insight into the biocatalytic potential of this collection of BVMOs and expand the biocatalytic repertoire known for BVMOs. This study also sheds light on the catalytic capacity of this large set of BVMOs that is present in this specific actinomycete. Furthermore, a comparative sequence analysis revealed a new BVMO-typifying sequence motif. This motif represents a useful tool for effective future genome mining efforts.

Original languageEnglish
Pages (from-to)1479-1489
Number of pages11
JournalApplied Microbiology and Biotechnology
Volume95
Issue number6
Publication statusPublished - Sep-2012

    Keywords

  • Biocatalysis, Baeyer-Villiger monooxygenase, Sulfoxidation, Enantioselectivity, PHENYLACETONE MONOOXYGENASE, CYCLOHEXANONE MONOOXYGENASE, THERMOBIFIDA-FUSCA, JOSTII RHA1, OXIDATIONS, IDENTIFICATION, BIOCATALYSTS, SPECIFICITY, PEROXIDASE, INSIGHTS

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