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Laboratory evolution of an epoxide hydrolase - Towards an enantioconvergent biocatalyst
- 1.0366238 - MBÚ 2012 RIV NL eng J - Journal Article
Kotík, Michael - Archelas, A. - Faměrová, Veronika - Oubrechtová, Pavla - Křen, Vladimír
Laboratory evolution of an epoxide hydrolase - Towards an enantioconvergent biocatalyst.
Journal of Biotechnology. Roč. 156, č. 1 (2011), s. 1-10. ISSN 0168-1656. E-ISSN 1873-4863
R&D Projects: GA ČR GAP207/10/0135
Institutional research plan: CEZ:AV0Z50200510
Keywords : Directed evolution * Regioselectivity * Enantioconvergence
Subject RIV: EE - Microbiology, Virology
Impact factor: 3.045, year: 2011
We performed a laboratory evolution study with the epoxide hydrolase from Aspergillus niger M200. This enzyme exhibits no enantioconvergence with the substrates styrene oxide or para-chlorostyrene oxide, i.e. racemic vicinal diols are produced from the racemic substrates. After saturation mutagenesis, screening by chiral gas chromatography revealed enzyme variants with improved enantioconvergence as manifested by an increased enantiomeric excess of the diol product. Nine amino acid exchanges accumulated in the active site and the substrate access tunnel over the course of 5 productive rounds of iterative saturation mutagenesis, resulting in an enantioconvergent epoxide hydrolase variant
Permanent Link: http://hdl.handle.net/11104/0201293
Number of the records: 1