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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

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CB - Analytical chemistry, separation

  • OECD FORD branch

Result continuities

  • Project

  • 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

  • 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