Sulfoxidation reactions catalysed by the Baeyer-Villiger monooxygenase OTEMO from Pseudomonas putida ATCC 17453

The Baeyer-Villiger monooxygenase OTEMO from Pseudomonas putida ATCC 17453 has been employed as biocatalyst in the asymmetric synthesis of a set of optically active sulfoxides. Several alkyl aryl sulfides are oxidised by this biocatalyst leading to the (S)-sulfoxides. Especially for those substrates...

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Detalles Bibliográficos
Autores: Gonzalo Calvo, Gonzalo de, Loncar, Nikola, Fraaije, Marco W.
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2022
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:dnet:idus________::66dd6028e5b5654d65b10fa37f79f7b3
Acceso en línea:https://hdl.handle.net/11441/185524
https://doi.org/10.1080/10242422.2022.2113519
Access Level:acceso abierto
Palabra clave:Biocatalysis
Baeyer-Villiger monooxygenases
Sulfoxidations
Kinetic resolution
Descripción
Sumario:The Baeyer-Villiger monooxygenase OTEMO from Pseudomonas putida ATCC 17453 has been employed as biocatalyst in the asymmetric synthesis of a set of optically active sulfoxides. Several alkyl aryl sulfides are oxidised by this biocatalyst leading to the (S)-sulfoxides. Especially for those substrates containing electron-donating groups in the aromatic ring or in the alkyl moiety, good to high enantiopurities can be obtained. OTEMO is also able to perform the kinetic resolution of racemic sulfoxides, but with low enantioselectivities. Finally, parameters that can affect its biocatalytic properties, such as pH, temperature, organic cosolvents and substrate concentration, have been tested to get a better insight into the biocatalytic potential of this hitherto poorly explored oxidative biocatalyst.