Mild hydrolysis of nitriles by the immobilized nitrilase from Aspergillus niger K10

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F06%3A00039334" target="_blank" >RIV/61388971:_____/06:00039334 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/06:10580

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Mild hydrolysis of nitriles by the immobilized nitrilase from Aspergillus niger K10

Original language description

The cell free extract front the nitrile-hydrolyzing strain Aspergillus niger K10 (0.25 mg of protein) was adsorped onto a 1 mL HiTrap Butyl Sepharose column. The benzonitrile-hydrolyzing activity of the immobilized enzyme (about 1.6 U/mg of protein) wasstable at pH 8 and 35 degrees C within the examined period (4 h). The enzyme load on the above column was increased 18 times in order to achieve high nitrile conversion. This enzyme preparation was used for the conversion of 3-cyanopyridine and 4-cyanopyridine under the above conditions. The initial substrate conversion was nearly quantitative. The activity was fairly stable; the conversion of 3-cyanopyridine decreased to 70% after 15 h, while the conversion of 4-cyanopyridine was 60% of the initial value after 39 It. The former substrate was converted into nicotinic acid and nicotinamide (molar ratio approximately 16: 1) and the latter one into isonicotinic acid and isonicotinamide (molar ratio approximately 3: 1)

Czech name

Šetrná hydrolýza nitrilů imobilizovanou nitrilasou z Aspergillus niger K10

Czech description

Buněčný extrakt z kmene Aspergillus niger K10 hydrolyzujícího nitrily (0.25 mg proteinu) byl adsorbován na 1 ml koloně HiTrap Butyl Sepharose. Hydrolytická aktivita imobilizovaného enzymů vůči benzonitrilu (asi 1.6 U/mg proteinu) byla stabilní při pH 8 and 35 °C během 4 h. Množství vázaného enzymu bylo zvýšené 18a s cílem dosáhnout vysoké konverze nitrilu. Enzymový preparát byl použit pro konverzi 3-kyanopyridinu a 4-kyanopyridinu. Počáteční konverze substrátu byla téměř kvantitativní. Stabilita aktivity byla uspokojivá; konverze 3-kyanopyridinu se snížila na 70% po 15 h, zatímco konverze 4-kyanopyridinu byla 60% původní hodnoty po 39 h. 3-Kyanopyridin byl transformován na kyselinu nikotinovou a nikotinamid (16:1) a 4-kyanopyridin na kyselinu isonikotinovou a isonikotinamid (3:1)

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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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)

Publication year

2006

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Molecular Catalysis B-Enzymatic

ISSN

1381-1177

e-ISSN

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Volume of the periodical

39

Issue of the periodical within the volume

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Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

4

Pages from-to

55-58

UT code for WoS article

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EID of the result in the Scopus database

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