Ketoreductase activity for reduction of substituted-beta-tetralones utilizing aqueous-organic systems and beta-cyclodextrin derivatives
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F12%3A43893308" target="_blank" >RIV/60461373:22340/12:43893308 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.3109/10242422.2012.662960" target="_blank" >http://dx.doi.org/10.3109/10242422.2012.662960</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3109/10242422.2012.662960" target="_blank" >10.3109/10242422.2012.662960</a>
Alternative languages
Result language
angličtina
Original language name
Ketoreductase activity for reduction of substituted-beta-tetralones utilizing aqueous-organic systems and beta-cyclodextrin derivatives
Original language description
Ketoreductases (KREDs) were employed for enantioselective reduction of 7-hydroxy-2-tetralone 1a and adduct 7-methoxy-2-tetralonbisulfite 2a to their corresponding (S)-/(R)-alcohols. In addition, the effect of additives such as organic solvents and beta-cyclodextrin derivatives on the enzyme reductions was investigated. The changes in enzyme activity as a function of additives were correlated to structural alterations of the KREDs using circular dichroism and fluorescence spectrophotometric measurements.The effects of both the organic solvents and beta-cyclodextrin derivatives on substrate solubility and equilibrium binding constants (log K) of beta-cyclodextrin-substrate complexes were determined.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CB - Analytical chemistry, separation
OECD FORD branch
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Result continuities
Project
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Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biocatalysis and Biotransformation
ISSN
1024-2422
e-ISSN
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Volume of the periodical
30
Issue of the periodical within the volume
2
Country of publishing house
GB - UNITED KINGDOM
Number of pages
12
Pages from-to
226-237
UT code for WoS article
000302020800008
EID of the result in the Scopus database
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