Application of a thermostable Baeyer-Villiger monooxygenase for the synthesis of branched polyester precursors.

Background: It is widely accepted that the poor thermostability of Baeyer-Villiger monooxygenases limits their use as biocatalysts for applied biocatalysis in industrial applications. The goal of this study was to investigate the biocatalytic oxidation of 3,3,5-trimethylcyclohexanone using a thermostable cyclohexanone monooxygenase from Thermocrispum municipale (TmCHMO) for the synthesis of branched ϵ-caprolactone derivatives as building blocks for tuned polymeric backbones. In this multi-enzymatic reaction, the thermostable cyclohexanone monooxygenase was fused to a phosphite dehydrogenase (PTDH) in order to ensure co-factor regeneration.