Recombinant alpha-L-rhamnosidase from Aspergillus terreus in selective trimming of rutin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10123297" target="_blank" >RIV/00216208:11310/12:10123297 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/12:00382285

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.procbio.2012.02.014" target="_blank" >http://dx.doi.org/10.1016/j.procbio.2012.02.014</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.procbio.2012.02.014" target="_blank" >10.1016/j.procbio.2012.02.014</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Recombinant alpha-L-rhamnosidase from Aspergillus terreus in selective trimming of rutin

Popis výsledku v původním jazyce

alpha-L-Rhamnosidase (EC 3.2.1.40) is a biotechnologically important enzyme used for derhamnosylation of many natural compounds. The extracellular alpha-L-rhamnosidase was purified from the culture of Aspergillus terreus grown on L-rhamnose-rich medium.This enzyme was found to be thermo- and alkali-tolerant, able to operate at 70 degrees C and pH 8.0. The alpha-L-rhamnosidase cDNA was cloned from A. terreus, sequenced, and expressed in the yeast Pichia pastoris as a fully functional protein. The recombinant protein was purified to apparent homogeneity and biochemically characterized. Both the native and the recombinant alpha-L-rhamnosidases catalyzed the conversion of rutin into quercetin-3-glucopyranoside (isoquercitrin), a pharmacologically significant flavonoid usable in nutraceutics. This procedure has high volumetric productivity (up to 300 g/L) and yields the product void of unwanted quercetin. The significant advantage of our expression system consists in shorter production tim

Název v anglickém jazyce

Recombinant alpha-L-rhamnosidase from Aspergillus terreus in selective trimming of rutin

Popis výsledku anglicky

alpha-L-Rhamnosidase (EC 3.2.1.40) is a biotechnologically important enzyme used for derhamnosylation of many natural compounds. The extracellular alpha-L-rhamnosidase was purified from the culture of Aspergillus terreus grown on L-rhamnose-rich medium.This enzyme was found to be thermo- and alkali-tolerant, able to operate at 70 degrees C and pH 8.0. The alpha-L-rhamnosidase cDNA was cloned from A. terreus, sequenced, and expressed in the yeast Pichia pastoris as a fully functional protein. The recombinant protein was purified to apparent homogeneity and biochemically characterized. Both the native and the recombinant alpha-L-rhamnosidases catalyzed the conversion of rutin into quercetin-3-glucopyranoside (isoquercitrin), a pharmacologically significant flavonoid usable in nutraceutics. This procedure has high volumetric productivity (up to 300 g/L) and yields the product void of unwanted quercetin. The significant advantage of our expression system consists in shorter production tim

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

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

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Process Biochemistry

ISSN

1359-5113

e-ISSN

—

Svazek periodika

47

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

828-835

Kód UT WoS článku

000303622400020

EID výsledku v databázi Scopus

—