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Discovery and Characterization of a Baeyer-Villiger Monooxygenase Using Sequence Similarity Network Analysis
- 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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| Author: | Thaleia Sakoleva, Harry P. Austin, Chrysoula Tzima, Mark Dörr, Uwe T. BornscheuerORCiD |
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| URN: | urn:nbn:de:gbv:9-opus-109127 |
| DOI: | https://doi.org/10.1002/cbic.202200746 |
| ISSN: | 1439-7633 |
| Parent Title (English): | ChemBioChem |
| Publisher: | Wiley |
| Place of publication: | Hoboken, NJ |
| Document Type: | Article |
| Language: | English |
| Date of Publication (online): | 2023/03/15 |
| Date of first Publication: | 2023/05/16 |
| Release Date: | 2024/03/25 |
| Tag: | Baeyer-Villiger monooxygenase; aliphatic ketones; biocatalysis |
| Volume: | 24 |
| Issue: | 10 |
| Article Number: | e202200746 |
| Page Number: | 5 |
| Faculties: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie |
| Collections: | weitere DFG-förderfähige Artikel |
| Licence (German): |  Creative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 4.0 International |