Heterologous expression, purification and characterization of arylacetonitrilases from Nectria haematococca and Arthroderma benhamiae
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10192015" target="_blank" >RIV/00216208:11310/13:10192015 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/13:00395703
Result on the web
<a href="http://dx.doi.org/10.3109/10242422.2012.758117" target="_blank" >http://dx.doi.org/10.3109/10242422.2012.758117</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3109/10242422.2012.758117" target="_blank" >10.3109/10242422.2012.758117</a>
Alternative languages
Result language
angličtina
Original language name
Heterologous expression, purification and characterization of arylacetonitrilases from Nectria haematococca and Arthroderma benhamiae
Original language description
Two novel arylacetonitrilases were purified from Escherichia coli BL21-Gold (DE3) expressing nit genes from Nectria haematococca mpVI 77-13-4 (EEU45207; NitNh) and Arthroderma benhamiae CBS 112371 (EFE30690; NitAb). The nitrilases formed holoenzymes of 360 and 336 kDa through gel filtration, while their apparent subunit size in SDS-PAGE was approximately 36 and 37 kDa, respectively. The preferred substrates of the purified enzymes were phenylacetonitrile, (R, S)-mandelonitrile, and 3-indolylacetonitrile. Both enzymes hydrolyzed (R)-mandelonitrile preferentially but with different degrees of selectivity, the e.e.s of the product (R)-mandelic acid being 63 and 89% in NitAb and NitNh, respectively, at pH 8.0. NitAb exhibited a higher temperature and pH stability than NitNh. Significant amounts of amide (> 5% of total product) were produced only by NitNh (from 2-cyanopyridine, (R, S)-mandelonitrile and phenylacetonitrile).
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
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
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
Biocatalysis and Biotransformation
ISSN
1024-2422
e-ISSN
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Volume of the periodical
31
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
8
Pages from-to
49-56
UT code for WoS article
000316220800006
EID of the result in the Scopus database
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