Download | - View accepted manuscript: Cyclohexylamine oxidase as useful biocatalyst for the kinetic resolution and dereacemization of amines (PDF, 587 KiB)
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DOI | Resolve DOI: https://doi.org/10.1139/V11-086 |
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Author | Search for: Leisch, Hannes1; Search for: Grosse, Stephan1; Search for: Iwaki, Hiroaki; Search for: Hasegawa, Yoshie; Search for: Lau, Peter C. K.1 |
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Affiliation | - National Research Council of Canada. NRC Biotechnology Research Institute
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Format | Text, Article |
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Subject | biocatalysis; cyclohexylamine oxidase; chiral amines; kinetic resolution; deracemization; biocatalyseur; oxydase de la cyclohexylamine; amines chirales; résolution cinétique; déracémisation |
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Abstract | The biocatalytic performance of a cloned cyclohexylamine oxidase derived from Brevibacterium oxydans IH-35A towards structurally different amines was investigated. Cycloalkyl primary amines, alkyl aryl amines, and ?-carbon-substituted aliphatic amines were identified as suitable substrates for the biocatalyst based on an activity assay. Kinetic resolutions of several amines by either recombinant whole cells or crude enzyme extracts prepared therefrom gave enantiomerically pure (R)-amines besides the corresponding ketones. When cyclohexylamine oxidase in combination with a borane-ammonia complex as reducing agent was applied to the deracemization of several substrates, excellent enantiomeric ratios (>99:1) and good isolated yields (62%-75%) of the corresponding (R)-amines were obtained. |
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Publication date | 2011-10-19 |
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In | |
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Language | English |
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Peer reviewed | Yes |
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NRC number | NRCC 53377 |
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NPARC number | 19304695 |
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Export citation | Export as RIS |
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Report a correction | Report a correction (opens in a new tab) |
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Record identifier | ddb28c81-104c-406a-84e7-418332bfeb72 |
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Record created | 2012-03-06 |
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Record modified | 2020-04-21 |
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