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Biotransformation of nitriles to amides using soluble and immobilized nitrile hydratase from Rhodococcus erythropolis A4

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F08%3A00320846" target="_blank" >RIV/61388971:_____/08:00320846 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Biotransformation of nitriles to amides using soluble and immobilized nitrile hydratase from Rhodococcus erythropolis A4

  • Original language description

    A semi-purified nitrile hydratase from Rhodococcus erythropolis A4 was applied to biotransformations of various alkyl- and acyl-nitriles into amides. Enzyme preparates with nitrile hydratase and amidase activities were prepared and used for nitrile hydration in presence of ammonium sulfate, which selectively inhibited amidase activity. The genes nha1 and nha2 coding for alpha and beta subunits of nitrile hydratase were cloned and sequenced

  • Czech name

    Biotransformace nitrilů na amidy s použitím rozpustné a imobilizované nitrilhydratasy z Rhodococcus erythropolis A4

  • Czech description

    Částečně purifikovaná nitrilhydratasa z Rhodococcus erythropolis A4 byla použita pro biotransformace různých alkyl- a acyl-nitrilů na amidy. Enzymové preparáty s nitrilhydratasovou a amidasovou aktivitou byly připraveny a použity pro hydrataci nitrilů vpřítomnosti síranu amonného, který selektivně inhibuje amidasovou aktivitu. Geny nha1 a nha2 kódující alfa a beta podjednotky nitrilhydratasy byly klonovány a sekvenovány

Classification

  • Type

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

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2008

  • 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-Enzymatic

  • ISSN

    1381-1177

  • e-ISSN

  • Volume of the periodical

    50

  • Issue of the periodical within the volume

    2-4

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

  • UT code for WoS article

    000252487300010

  • EID of the result in the Scopus database