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• W2898833981 abstract "Baeyer-Villiger monooxygenases (BVMOs) convert ketones into lactones that have important applications in polymer synthesis. Here we report on expanding the substrate scope of a thermostable phenylacetone monooxygenase (PAMO) to cyclohexanone by using site-directed mutagenesis. Several new mutants were found to be active with cyclohexanone for which wild-type PAMO shows no activity. The best mutants could convert 10 mM cyclohexanone completely within 12 h, and their catalytic properties were characterized subsequently. In addition to cyclohexanone, several other cyclic ketones were also identified as substrate for the new evolved mutants. These results expand the biocatalytic toolbox for further feasible applications." @default.
• W2898833981 created "2018-11-09" @default.
• W2898833981 creator A5013682689 @default.
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• W2898833981 date "2019-01-01" @default.
• W2898833981 modified "2023-10-14" @default.
• W2898833981 title "Expanding the substrate scope of phenylacetone monooxygenase from Thermobifida fusca towards cyclohexanone by protein engineering" @default.
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• W2898833981 doi "https://doi.org/10.1016/j.catcom.2018.10.022" @default.
• W2898833981 hasPublicationYear "2019" @default.
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