Exploring the Potential of Fungal Arylacetonitrilases in Mandelic Acid Synthesis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10296584" target="_blank" >RIV/00216208:11310/15:10296584 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/15:00444847
Result on the web
<a href="http://dx.doi.org/10.1007/s12033-015-9840-y" target="_blank" >http://dx.doi.org/10.1007/s12033-015-9840-y</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s12033-015-9840-y" target="_blank" >10.1007/s12033-015-9840-y</a>
Alternative languages
Result language
angličtina
Original language name
Exploring the Potential of Fungal Arylacetonitrilases in Mandelic Acid Synthesis
Original language description
The application of arylacetonitrilases from filamentous fungi to the hydrolysis of high concentrations of (R, S)-mandelonitrile (100-500 mM) was demonstrated for the first time. Escherichia coli strains expressing the corresponding genes were used as whole-cell catalysts. Nitrilases from Aspergillus niger, Neurospora crassa, Nectria haematococca, and Arthroderma benhamiae (enzymes NitAn, NitNc, NitNh, and NitAb, respectively) exhibited different degrees of enantio-and chemoselectivity (amide formation).Their enantio-and chemoselectivity was increased by increasing pH (from 8 to 9-10) and adding 4-10 % (v/v) toluene as the cosolvent. NitAn and NitNc were able to convert an up to 500 mM substrate in batch mode. NitAn formed a very low amount of the by-product, amide (<1% of the total product). This enzyme produced up to >70 g/L of (R)-mandelic acid (e.e. 94.5-95.6 %) in batch or fed-batch mode. Its volumetric productivities were the highest in batch mode [571 +/- 32 g/(L d)] and its cat
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
<a href="/en/project/GAP504%2F11%2F0394" target="_blank" >GAP504/11/0394: Interspecies comparison of nitrilases by using recombinant enzymes obtained by database-mining: their environmental impact and potential application</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
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
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Volume of the periodical
57
Issue of the periodical within the volume
5
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
466-474
UT code for WoS article
000353147700009
EID of the result in the Scopus database
2-s2.0-84928310446