Biotransformation of nitriles to amides using soluble and immobilized nitrile hydratase from Rhodococcus erythropolis A4
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F08%3A00320846" target="_blank" >RIV/61388971:_____/08:00320846 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Biotransformation of nitriles to amides using soluble and immobilized nitrile hydratase from Rhodococcus erythropolis A4
Original language description
A semi-purified nitrile hydratase from Rhodococcus erythropolis A4 was applied to biotransformations of various alkyl- and acyl-nitriles into amides. Enzyme preparates with nitrile hydratase and amidase activities were prepared and used for nitrile hydration in presence of ammonium sulfate, which selectively inhibited amidase activity. The genes nha1 and nha2 coding for alpha and beta subunits of nitrile hydratase were cloned and sequenced
Czech name
Biotransformace nitrilů na amidy s použitím rozpustné a imobilizované nitrilhydratasy z Rhodococcus erythropolis A4
Czech description
Částečně purifikovaná nitrilhydratasa z Rhodococcus erythropolis A4 byla použita pro biotransformace různých alkyl- a acyl-nitrilů na amidy. Enzymové preparáty s nitrilhydratasovou a amidasovou aktivitou byly připraveny a použity pro hydrataci nitrilů vpřítomnosti síranu amonného, který selektivně inhibuje amidasovou aktivitu. Geny nha1 a nha2 kódující alfa a beta podjednotky nitrilhydratasy byly klonovány a sekvenovány
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
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
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2008
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Catalysis B-Enzymatic
ISSN
1381-1177
e-ISSN
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Volume of the periodical
50
Issue of the periodical within the volume
2-4
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
7
Pages from-to
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UT code for WoS article
000252487300010
EID of the result in the Scopus database
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