Influence of point mutations near the active site on the catalytic properties of fungal arylacetonitrilases from Aspergillus niger and Neurospora crassa
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00378903" target="_blank" >RIV/61388971:_____/12:00378903 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.molcatb.2012.01.005" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2012.01.005</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.molcatb.2012.01.005" target="_blank" >10.1016/j.molcatb.2012.01.005</a>
Alternative languages
Result language
angličtina
Original language name
Influence of point mutations near the active site on the catalytic properties of fungal arylacetonitrilases from Aspergillus niger and Neurospora crassa
Original language description
Arylacetonitrilases from Aspergillus niger CBS 513.88 and Neurospora crassa OR74A (NitAn and NicNc, respectively) were expressed in recombinant Escherichia coil JM109. The respective whole-cell catalysts preferentially hydrolyzed (R)-enantiomers of (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile. NitNc also formed significant amounts of mandelamide from (R,S)-mandelonitrile (40% of total product), mainly found as the (S)-enantiomer. At pH 4.5 and 5.0, the cells retained more than 40 and 60% of their nitrilase activity at pH 7, respectively
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
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2012
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
—
Volume of the periodical
77
Issue of the periodical within the volume
MAY 2012
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
7
Pages from-to
74-80
UT code for WoS article
000302106400011
EID of the result in the Scopus database
—