Cyclohexylamine oxidase as a useful biocatalyst for the kinetic resolution and dereacemization of amines | Zendy

Hannes Leisch | Zendy; Stephan Große | Zendy; Hiroaki Iwaki | Zendy; Yoshie Hasegawa | Zendy; Peter C. K. Lau | Zendy

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Cyclohexylamine oxidase as a useful biocatalyst for the kinetic resolution and dereacemization of amines

Author(s) -

Hannes Leisch,

Stephan Große,

Hiroaki Iwaki,

Yoshie Hasegawa,

Peter C. K. Lau

Publication year - 2011

Publication title -

canadian journal of chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.323

H-Index - 68

eISSN - 1480-3291

pISSN - 0008-4042

DOI - 10.1139/v11-086

Subject(s) - cyclohexylamine , chemistry , biocatalysis , kinetic resolution , enantiomeric excess , alkyl , organic chemistry , enantiomer , amine gas treating , aryl , formate dehydrogenase , enzyme , catalysis , enantioselective synthesis , ionic liquid , cofactor

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.Peer reviewed: YesNRC publication: Ye

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