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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CC - Organická chemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Advanced Synthesis & Catalysis

ISSN

1615-4150

e-ISSN

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Svazek periodika

357

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

11

Strana od-do

107-117

Kód UT WoS článku

000347705400015

EID výsledku v databázi Scopus

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