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Manipulating the stereoselectivity of the thermostable Baeyer–Villiger monooxygenase TmCHMO by directed evolution

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Abstract

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.

Graphical abstract: Manipulating the stereoselectivity of the thermostable Baeyer–Villiger monooxygenase TmCHMO by directed evolution

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Publication details

The article was received on 01 Nov 2017, accepted on 06 Nov 2017 and first published on 13 Nov 2017


Article type: Paper
DOI: 10.1039/C7OB02692G
Citation: Org. Biomol. Chem., 2017, Advance Article
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    Manipulating the stereoselectivity of the thermostable Baeyer–Villiger monooxygenase TmCHMO by directed evolution

    G. Li, M. J. L. J. Fürst, H. R. Mansouri, A. K. Ressmann, A. Ilie, F. Rudroff, M. D. Mihovilovic, M. W. Fraaije and M. T. Reetz, Org. Biomol. Chem., 2017, Advance Article , DOI: 10.1039/C7OB02692G

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