Recombinant alpha-L-rhamnosidase from Aspergillus terreus in selective trimming of rutin
The result's identifiers
Result code in 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>
Alternative codes found
RIV/61388971:_____/12:00382285
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Recombinant alpha-L-rhamnosidase from Aspergillus terreus in selective trimming of rutin
Original language description
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
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
CE - Biochemistry
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
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
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Process Biochemistry
ISSN
1359-5113
e-ISSN
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Volume of the periodical
47
Issue of the periodical within the volume
5
Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
828-835
UT code for WoS article
000303622400020
EID of the result in the Scopus database
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