Biotransformation of nitriles by Rhodococcus equi A4 immobilized in LentiKats

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F06%3A00039333" target="_blank" >RIV/61388971:_____/06:00039333 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Biotransformation of nitriles by Rhodococcus equi A4 immobilized in LentiKats

Original language description

Whole cells of Rhodococcus equi A4, a producer of nitrile hydratase and amidase activities, were immobilized in lens-shaped hydrogel particles. LentiKats (R). The immobilized biocatalyst was applied to the biotransformation of benzonitrile, 3-cyanopyridine, (R,S)-3-hydroxy-2-methylenebutanenitrile and (R,S)-3-hydroxy-2-methylene-3-phenylpropanenitrile. The stability of the nitrile hydratase during the repeated use of the biocatalyst was dependent on the type of the substrate. The enzyme was most stableduring the transformation of (R,S)-3-hydroxy-2-methylenebutanenitrile. No significant loss of the amidase activity was observed within the course of the biocatalytic reaction

Czech name

Biotransformace nitrilů pomocí baktérie Rhodococcus equi A4 imobilizované v LentiKats

Czech description

Celé buňky baktérie Rhodococcus equi A4, producenta nitrilhydratasy a amidasy, byly imobilizovány v čočkovitých částicích hydrogelu, LentiKats (R). Imobilizovaný biokatalyzátor byl použit pro biotransformaci benzonitrilu, 3-kyanopyridinu, (R,S)-3-hydroxy-2-methylenebutanenitrilu and (R,S)-3-hydroxy-2-methylene-3-phenylpropanenitrilu. Stabilita nitrilhydratasy během opakovaného použití biokatalyzátoru závisela na typu substrátu. Enzym byl stabilní během transformace (R,S)-3-hydroxy-2-methylenebutanenitrilu. Během reakce nebyla pozorována výraznější ztráta aktivity amidasy

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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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>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2006

Confidentiality

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

Name of the periodical

Journal of Molecular Catalysis B-Enzymatic

ISSN

1381-1177

e-ISSN

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Volume of the periodical

39

Issue of the periodical within the volume

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Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

3

Pages from-to

59-61

UT code for WoS article

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EID of the result in the Scopus database

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