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Influence of point mutations near the active site on the catalytic properties of fungal arylacetonitrilases from Aspergillus niger and Neurospora crassa

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00378903" target="_blank" >RIV/61388971:_____/12:00378903 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.molcatb.2012.01.005" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2012.01.005</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.molcatb.2012.01.005" target="_blank" >10.1016/j.molcatb.2012.01.005</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Influence of point mutations near the active site on the catalytic properties of fungal arylacetonitrilases from Aspergillus niger and Neurospora crassa

  • Original language description

    Arylacetonitrilases from Aspergillus niger CBS 513.88 and Neurospora crassa OR74A (NitAn and NicNc, respectively) were expressed in recombinant Escherichia coil JM109. The respective whole-cell catalysts preferentially hydrolyzed (R)-enantiomers of (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile. NitNc also formed significant amounts of mandelamide from (R,S)-mandelonitrile (40% of total product), mainly found as the (S)-enantiomer. At pH 4.5 and 5.0, the cells retained more than 40 and 60% of their nitrilase activity at pH 7, respectively

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

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

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

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

    Journal of Molecular Catalysis B-Enzymatic

  • ISSN

    1381-1177

  • e-ISSN

  • Volume of the periodical

    77

  • Issue of the periodical within the volume

    MAY 2012

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

    74-80

  • UT code for WoS article

    000302106400011

  • EID of the result in the Scopus database