Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 15, Issue 46, Pages 9824-9829Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7ob02692g
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Funding
- Max-Planck-Society
- LOEWE Research Cluster SynBioChem
- European Union (EU) project ROBOX under EU's Horizon Programme Research and Innovation actions [635734]
- FWF [P28477-B21]
- COST-Action [CM1303]
- TU Wien ABC-Top Anschubfinanzierung
- Max Planck Society
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Baeyer-Villiger monooxygenases (BVMOs) and evolved mutants have been shown to be excellent biocatalysts in many stereoselective Baeyer-Villiger transformations, but industrial applications are rare which is partly due to the insufficient thermostability of BVMOs under operating conditions. In the present study, the substrate scope of the recently discovered thermally stable BVMO, TmCHMO from Thermocrispum municipale, was studied. This revealed that the wild-type (WT) enzyme catalyzes the oxidation of a variety of structurally different ketones with notable activity and enantioselectivity, including the desymmetrization of 4-methylcyclohexanone (99% ee, S). In order to induce the reversal of enantioselectivity of this reaction as well as the transformations of other substrates, directed evolution based on iterative saturation mutagenesis (ISM) was applied, leading to (R)-selectivity (94% ee) without affecting the thermostability of the biocatalyst.
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