Šetrná hydrolýza nitrilů imobilizovanou nitrilasou z Aspergillus niger K10

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216208:11310/06:10580

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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)

Název v anglickém jazyce

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

Popis výsledku anglicky

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)

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2006

Kód důvěrnosti údajů

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

Název periodika

Journal of Molecular Catalysis B-Enzymatic

ISSN

1381-1177

e-ISSN

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Svazek periodika

39

Číslo periodika v rámci svazku

-

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

4

Strana od-do

55-58

Kód UT WoS článku

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EID výsledku v databázi Scopus

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