Cyanide hydratase from Aspergillus niger K10: Overproduction in Escherichia coli, purification, characterization and use in continuous cyanide degradation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10289017" target="_blank" >RIV/00216208:11310/14:10289017 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/14:00428318

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.procbio.2013.12.008" target="_blank" >http://dx.doi.org/10.1016/j.procbio.2013.12.008</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.procbio.2013.12.008" target="_blank" >10.1016/j.procbio.2013.12.008</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Cyanide hydratase from Aspergillus niger K10: Overproduction in Escherichia coli, purification, characterization and use in continuous cyanide degradation

Popis výsledku v původním jazyce

A cyanide hydratase from Aspergillus niger K10 was expressed in Escherichia coli and purified. Apart from HCN, it transformed some nitriles, preferentially 2-cyanopyridine and fumaronitrile. V-max and K-m for HCN were ca. 6.8mmol min(-1) mg(-1) protein and 109mM, respectively. V-max for fumaronitrite and 2-cyanopyridine was two to three orders of magnitude lower than for HCN (ca. 18.8 and 10.3 mu.,mol min(-1) mg(-1), respectively) but K-m was also lower (ca. 14.7 and 3.7 mM, respectively). Both cyanidehydratase and nitrilase activities were abolished in truncated enzyme variants missing 18-34 C-terminal aa residues. The enzyme exhibited the highest activity at 45 degrees C and pH 8-9; it was unstable at over 35 degrees C and at below pH 5.5. The operational stability of the whole-cell catalyst was examined in continuous stirred membrane reactors with 70-mL working volume. The catalyst exhibited a half-life of 5.6 h at 28 degrees C. A reactor loaded with an excess of the catalyst was u

Název v anglickém jazyce

Cyanide hydratase from Aspergillus niger K10: Overproduction in Escherichia coli, purification, characterization and use in continuous cyanide degradation

Popis výsledku anglicky

A cyanide hydratase from Aspergillus niger K10 was expressed in Escherichia coli and purified. Apart from HCN, it transformed some nitriles, preferentially 2-cyanopyridine and fumaronitrile. V-max and K-m for HCN were ca. 6.8mmol min(-1) mg(-1) protein and 109mM, respectively. V-max for fumaronitrite and 2-cyanopyridine was two to three orders of magnitude lower than for HCN (ca. 18.8 and 10.3 mu.,mol min(-1) mg(-1), respectively) but K-m was also lower (ca. 14.7 and 3.7 mM, respectively). Both cyanidehydratase and nitrilase activities were abolished in truncated enzyme variants missing 18-34 C-terminal aa residues. The enzyme exhibited the highest activity at 45 degrees C and pH 8-9; it was unstable at over 35 degrees C and at below pH 5.5. The operational stability of the whole-cell catalyst was examined in continuous stirred membrane reactors with 70-mL working volume. The catalyst exhibited a half-life of 5.6 h at 28 degrees C. A reactor loaded with an excess of the catalyst was u

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Process Biochemistry

ISSN

1359-5113

e-ISSN

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Svazek periodika

49

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

6

Strana od-do

445-450

Kód UT WoS článku

000334482300013

EID výsledku v databázi Scopus

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