Discovery and Characterization of a Baeyer-Villiger Monooxygenase Using Sequence Similarity Network Analysis |
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Authors: | Thaleia Sakoleva Dr. Harry P. Austin Chrysoula Tzima Dr. Mark Dörr Prof. Dr. Uwe T. Bornscheuer |
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Affiliation: | Department of Biotechnology and Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Straße 4, 17487 Greifswald, Germany |
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Abstract: | Baeyer-Villiger monooxygenases (BVMOs) are important flavin-dependent enzymes which perform oxygen insertion reactions leading to valuable products. As reported in many studies, BVMOs are usually unstable during application, preventing a wider usage in biocatalysis. Here, we discovered a novel NADPH-dependent BVMO which originates from Halopolyspora algeriensis using sequence similarity networks (SSNs). The enzyme is stable at temperatures between 10 °C to 30 °C up to five days after the purification, and yields the normal ester product. In this study, the substrate scope was investigated for a broad range of aliphatic ketones and the enzyme was biochemically characterized to identify optimum reaction conditions. The best substrate (86 % conversion) was 2-dodecanone using purified enzyme. This novel BVMO could potentially be applied as part of an enzymatic cascade or in bioprocesses which utilize aliphatic alkanes as feedstock. |
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Keywords: | aliphatic ketones Baeyer-Villiger monooxygenase biocatalysis |
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