Dataset Information

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

ABSTRACT:

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.

Results

Using reaction engineering, the reaction rate and product formation of the regio-isomeric branched lactones were improved and the use of co-solvents and the initial substrate load were investigated. Substrate inhibition and poor product solubility were overcome using continuous substrate feeding regimes, as well as a biphasic reaction system with toluene as water-immiscible organic solvent. A maximum volumetric productivity, or space-time-yield, of 1.20 g L^-1 h^-1 was achieved with continuous feeding of substrate using methanol as co-solvent, while a maximum product concentration of 11.6 g L^-1 was achieved with toluene acting as a second phase and substrate reservoir.

Conclusion

These improvements in key process metrics therefore demonstrate progress towards the up-scaled Baeyer-Villiger monooxygenase-biocatalyzed synthesis of the target building blocks for polymer application. © 2018 The Authors. Journal of Chemical Technology & Biotechnology published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

SUBMITTER: Delgove MA

PROVIDER: S-EPMC6055809 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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Publications

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

Delgove Marie Af MA Elford Matthew T MT Bernaerts Katrien V KV De Wildeman Stefaan Ma SM

Journal of chemical technology and biotechnology (Oxford, Oxfordshire : 1986) 20180416 8

<h4>Background</h4>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 ...[more]

PMID: 30069077

Similar Datasets

Project description:Baeyer-Villiger monooxygenases (BVMOs) are an emerging class of promising biocatalysts for the oxidation of ketones to prepare corresponding esters or lactones. Although many BVMOs have been reported, the development of highly efficient enzymes for use in industrial applications is desirable. In this work, we identified a BVMO from Rhodococcus pyridinivorans (BVMORp) with a high affinity toward aliphatic methyl ketones (Km < 3.0 μM). The enzyme was highly soluble and relatively stable, with a half-life of 23 h at 30°C and pH 7.5. The most effective substrate discovered so far is 2-hexanone (kcat = 2.1 s-1; Km = 1.5 μM). Furthermore, BVMORp exhibited excellent regioselectivity toward most aliphatic ketones, preferentially forming typical (i.e., normal) products. Using the newly identified BVMORp as the catalyst, a high concentration (26.0 g/liter; 200 mM) of methyl levulinate was completely converted to methyl 3-acetoxypropionate after 4 h, with a space-time yield of 5.4 g liter-1 h-1 Thus, BVMORp is a promising biocatalyst for the synthesis of 3-hydroxypropionate from readily available biobased levulinate to replace the conventional fermentation.IMPORTANCE BVMOs are emerging as a green alternative to traditional oxidants in the BV oxidation of ketones. Although many BVMOs are discovered and used in organic synthesis, few are really applied in industry, especially in the case of aliphatic ketones. Herein, a highly soluble and relatively stable monooxygenase from Rhodococcus pyridinivorans (BVMORp) was identified with high activity and excellent regioselectivity toward most aliphatic ketones. BVMORp possesses unusually high substrate loading during the catalysis of the oxidation of biobased methyl levulinate to 3-hydroxypropionic acid derivatives. This study indicates that the synthesis of 3-hydroxypropionate from readily available biobased levulinate by BVMORp-catalyzed oxidation holds great promise to replace traditional fermentation.

Dataset Information

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

Background

Results

Conclusion

Publications

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

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