Laboratory evolution of an epoxide hydrolase - Towards an enantioconvergent biocatalyst

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F11%3A00366238" target="_blank" >RIV/61388971:_____/11:00366238 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.jbiotec.2011.08.003" target="_blank" >http://dx.doi.org/10.1016/j.jbiotec.2011.08.003</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jbiotec.2011.08.003" target="_blank" >10.1016/j.jbiotec.2011.08.003</a>

Result language
angličtina
Original language name
Laboratory evolution of an epoxide hydrolase - Towards an enantioconvergent biocatalyst
Original language description
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 accumulatedin 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
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Project
<a href="/en/project/GAP207%2F10%2F0135" target="_blank" >GAP207/10/0135: Investigations into regioselectivity of evolved epoxide hydrolases</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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