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
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CC - Organic chemistry
OECD FORD branch
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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
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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
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