Immobilization of Arylmalonate Decarboxylase

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F18%3A73591822" target="_blank" >RIV/61989592:15310/18:73591822 - isvavai.cz</a>

Result on the web

<a href="https://www.mdpi.com/2073-4344/8/12/603/htm" target="_blank" >https://www.mdpi.com/2073-4344/8/12/603/htm</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/catal8120603" target="_blank" >10.3390/catal8120603</a>

Result language

angličtina

Original language name

Immobilization of Arylmalonate Decarboxylase

Original language description

Arylmalonate decarboxylase (AMD) is a monomeric enzyme of only 26 kDa. A recombinant AMDase from Bordetella bronchiseptica was expressed in Escherichia coli and the enzyme was immobilized using different techniques: entrapment in polyvinyl alcohol (PVA) gel (LentiKats®), covalent binding onto magnetic microparticles (MMP, PERLOZA s.r.o., Lovosice, Czech Republic) and double-immobilization (MMP-LentiKats®) using the previous two methods. The double-immobilized AMDase was stable in 8 repeated biocatalytic reactions. This combined immobilization technique has the potential to be applied to different small proteins.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

30401 - Health-related biotechnology

Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2018

Confidentiality

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

Name of the periodical

Catalysts

ISSN

2073-4344

e-ISSN

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Volume of the periodical

8

Issue of the periodical within the volume

12

Country of publishing house

CH - SWITZERLAND

Number of pages

11

Pages from-to

"603-1"-"603-11"

UT code for WoS article

000454711500035

EID of the result in the Scopus database

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