A Comparative Study of Nitrilases Identified by Genome Mining
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191997" target="_blank" >RIV/00216208:11310/13:10191997 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/13:00395407
Result on the web
<a href="http://dx.doi.org/10.1007/s12033-013-9656-6" target="_blank" >http://dx.doi.org/10.1007/s12033-013-9656-6</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s12033-013-9656-6" target="_blank" >10.1007/s12033-013-9656-6</a>
Alternative languages
Result language
angličtina
Original language name
A Comparative Study of Nitrilases Identified by Genome Mining
Original language description
Escherichia coli strains expressing different nitrilases transformed nitriles or KCN. Six nitrilases (from Aspergillus niger (2), A. oryzae, Neurospora crassa, Arthroderma benhamiae, and Nectria haematococca) were arylacetonitrilases, two enzymes (from A. niger and Penicillium chrysogenum) were cyanide hydratases and the others (from P. chrysogenum, P. marneffei, Gibberella moniliformis, Meyerozyma guilliermondi, Rhodococcus rhodochrous, and R. ruber) preferred (hetero)aromatic nitriles as substrates. Promising nitrilases for the transformation of industrially important substrates were found: the nitrilase from R. ruber for 3-cyanopyridine, 4-cyanopyridine and bromoxynil, the nitrilases from N. crassa and A. niger for (R,S)-mandelonitrile, and the cyanide hydratase from A. niger for KCN and 2-cyanopyridine.
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Applied Biochemistry and Biotechnology - Part B Molecular Biotechnology
ISSN
1073-6085
e-ISSN
—
Volume of the periodical
54
Issue of the periodical within the volume
3
Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
996-1003
UT code for WoS article
000318513200027
EID of the result in the Scopus database
—