Recombinant alpha-L-rhamnosidase of Aspergillus terreus immobilization in polyvinylalcohol hydrogel and its application in rutin derhamnosylation

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F13%3A00422606" target="_blank" >RIV/61388971:_____/13:00422606 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.3109/10242422.2013.858711" target="_blank" >http://dx.doi.org/10.3109/10242422.2013.858711</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3109/10242422.2013.858711" target="_blank" >10.3109/10242422.2013.858711</a>

Result language
angličtina
Original language name
Recombinant alpha-L-rhamnosidase of Aspergillus terreus immobilization in polyvinylalcohol hydrogel and its application in rutin derhamnosylation
Original language description
Recombinant alpha-L-rhamnosidase from Aspergillus terreus expressed in Pichia pastoris was immobilized in LentiKats (R) lens-shaped polyvinylalcohol (PVA) capsules with an activity of 7 U g(-1), which was 21% of its original activity. Immobilization didnot significantly affect the pH and temperature profile of alpha-L-rhamnosidase, K-M increased by a factor of 3.4 whereas V-max decreased more than 10-fold. No decrease in activity was observed after 27 repeated batch runs of rutin derhamnosylation. Theenzyme proved to have an excellent storage stability (136 days) in 60 g L-1 ethanol with no change in its activity
Czech name
—
Czech description
—

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—

Project
<a href="/en/project/7E11010" target="_blank" >7E11010: Developing the Next Generation of Biocatalysts for Industrial Chemical Synthesis</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)