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Biotransformation of nitriles by Rhodococcus equi A4 immobilized in LentiKats(R).

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F06%3A00017788" target="_blank" >RIV/60461373:22330/06:00017788 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Biotransformation of nitriles by Rhodococcus equi A4 immobilized in LentiKats(R).

  • Original language description

    Whole cells of Rhodococcus equi A4, a producer of nitrile hydratase and amidase activities, were immobilized in lens-shaped hydrogel particles, LentiKats(R). The immobilized biocatalyst was applied to the biotransformation of benzonitrile, 3-cyanopyridine, (R,S)-3-hydroxy-2-methylene-butanenitrile and (R,S)-3-hydroxy-2-methylene-3-phenyl-propanenitrile. The stability of the nitrile hydratase during the repeated use of the biocatalyst was dependent on the type of the substrate. The enzyme was the most stable during the transformation of (R,S)-3-hydroxy-2-methylene-butanenitrile. No significant loss of the amidase activity was observed within the biocatalyst operation

  • Czech name

    Biotransformace nitrilů Rhodococcus equi A4 imobilizovaných v LentiKats(R).

  • Czech description

    Rhodococcus equi A4, producent nitrilhydratasové a amidasové aktivity byl imobilizován v lentiketových hydrogelových partikulích LentiKats(R). Imobilizovaný biokatalyzátor byl aplikován v biotransformaci benzonitrilu, 3-cyanopyridinu, (R,S)-3-hydroxy-2-methylene-butanenitrilu and (R,S)-3-hydroxy-2-methylene-3-phenyl-propanenitrilu. Stabilita nitrilhydratasy během opakovaného použití biokatalyzátoru byla závislá na typu substrátu.Během použití nebyla zaznamenána výrazná aktivita amidasy.

Classification

  • Type

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

  • CEP classification

    EI - Biotechnology and bionics

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2006

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Molecular Catalysis B

  • ISSN

    1381-1177

  • e-ISSN

  • Volume of the periodical

  • Issue of the periodical within the volume

    39

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    3

  • Pages from-to

    59-61

  • UT code for WoS article

  • EID of the result in the Scopus database