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Enzymatic oxidative dimerization of silymarin flavonolignans

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F14%3A00435748" target="_blank" >RIV/61388971:_____/14:00435748 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.molcatb.2014.07.012" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2014.07.012</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.molcatb.2014.07.012" target="_blank" >10.1016/j.molcatb.2014.07.012</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Enzymatic oxidative dimerization of silymarin flavonolignans

  • Original language description

    Dimerization of phenolic compounds can potentially enhance their biological (antioxidant) activity. We present here the selective oxidative dimerization of several flavonolignans from Silybum marianum seed extract, namely, silybin A (1a), silybin B (1b),silychristin (3), and silydianin (4) catalyzed by a laccase from Trametes versicolor. Selective benzylation of C-7 OH group of both silybins ensured the priority of the dimerization reaction, avoiding thus polymerization. C-C homodimers connected via E-rings of silybin A and B and silydianin dimers were successfully isolated after respective debenzylation. On the contrary, dimerization of 7-O-benzyl silychristin afforded a complex, inseparable mixture of the products. All isolated flavonolignan dimersexhibited significantly improved 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity compared to their monomers and, therefore, seem to be promising for further biological studies

  • 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

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2014

  • 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

    109

  • Issue of the periodical within the volume

    NOV 2014

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    6

  • Pages from-to

    24-30

  • UT code for WoS article

    000343854100004

  • EID of the result in the Scopus database