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alpha-L-Rhamnosyl-beta-D-glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F15%3A00444488" target="_blank" >RIV/61388971:_____/15:00444488 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1002/adsc.201400566" target="_blank" >http://dx.doi.org/10.1002/adsc.201400566</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/adsc.201400566" target="_blank" >10.1002/adsc.201400566</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    alpha-L-Rhamnosyl-beta-D-glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

  • Original language description

    We report the first heterologous production of a fungal rutinosidase (6-O-alpha-L-rhamnopyranosyl-beta-d-glucopyranosidase) in Pichia pastoris. The recombinant rutinosidase was purified from the culture medium to apparent homogeneity and biochemically characterized. The enzyme reacts with rutin and cleaves the glycosidic linkage between the disaccharide rutinose and the aglycone. Furthermore, it exhibits high transglycosylation activity, transferring rutinose from rutin as a glycosyl donor onto variousalcohols and phenols. The utility of the recombinant rutinosidase was demonstrated by its use for the synthesis of a broad spectrum of rutinosides of primary (saturated and unsaturated), secondary, acyclic and phenolic alcohols as well as for the preparation of free rutinose. Moreover, the alpha-L-rhamnosidase-catalyzed synthesis of a chromogenic substrate for a rutinosidase assay - para-nitrophenyl beta-rutinoside - is described.

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    CC - Organic chemistry

  • 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

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Advanced Synthesis & Catalysis

  • ISSN

    1615-4150

  • e-ISSN

  • Volume of the periodical

    357

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    11

  • Pages from-to

    107-117

  • UT code for WoS article

    000347705400015

  • EID of the result in the Scopus database