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Unique transglycosylation potential of extracellular alpha-D-galactosidase from Talaromyces flavus

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F06%3A00048853" target="_blank" >RIV/61388971:_____/06:00048853 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Unique transglycosylation potential of extracellular alpha-D-galactosidase from Talaromyces flavus

  • Original language description

    The transalycosylation potential of the extracellular alpha-D-galactosidase from the filamentous fungus Talaromyces flavus CCF 2686, chosen as the best enzyme from the screening, was investigated using a series of sterically hindered alcohols (primary, secondary and tertiary) as galactosyl acceptors. Nine alkyl alpha-D-galactopyranosides derived from the following alcohols - tert-butyl alcohol, 2-methyl-2-butyl alcohol, 2-methyl-1-propyl alcohol, 2,2,2-trifluoroethyl alcohol, 2-propyn-1-ol, n-pentyl alcohol, 3,5-dihydroxybenzyl alcohol, 1-phenylethyl alcohol and 1,4-dithio-DL-threitol - were prepared on a semi-preparative scale. This demonstrates a broad synthetic potential of the T flavus alpha-D-galactosidase that has not been observed with another enzyme tested. Moreover, this enzyme exhibits good transglycosylation yields (6-34%). The enzymatic synthesis of tert-butyl alpha-D-galactopyranoside by transglycosylation was studied in detail

  • Czech name

    Jedinečný transglycosylační potenciál extracelulární alpha-D-galactosidasy z Talaromyces flavus

  • Czech description

    Byl studován transglykosylační potenciál extracelulární alpha-D-galactosidasy z Talaromyces flavus s použitím serie stericky bráněných alkoholů

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

    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-Enzymatic

  • ISSN

    1381-1177

  • e-ISSN

  • Volume of the periodical

    39

  • Issue of the periodical within the volume

    -

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

    128-134

  • UT code for WoS article

  • EID of the result in the Scopus database