Nitrile hydratase CLEAs: Imobilizace a stabilizace průmyslově důležitého enzymu

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F08%3A00311256" target="_blank" >RIV/61388971:_____/08:00311256 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Nitrile Hydratase CLEAs: The immobilization and stabilization of an industrially important enzyme

Popis výsledku v původním jazyce

The successful immobilization and stabilization of nitrile hydratase in the form of a cross-linked enzyme aggregate (CLEA) is described. CLEAs were prepared by using ammonium sulfate as an aggregation agent followed by cross-linking with glutaraldehyde.The effect of different glutaraldehyde concentration on the recovery of enzyme activity in the CLEA and enzyme leakage from the CLEA matrix was investigated. Although activity recovery was low (21%) the CLEA facilitates easy separation and recycling of the nitrile hydratase. It was also found that the nitrile hydratase CLEA had substantially increased storage stability as well as increased operational stability during exposure to high concentration of acrylamide and acrylonitrile compared to that of thenitrile hydratase in the crude cell-free extract and whole cell formulation

Název v anglickém jazyce

Nitrile Hydratase CLEAs: The immobilization and stabilization of an industrially important enzyme

Popis výsledku anglicky

The successful immobilization and stabilization of nitrile hydratase in the form of a cross-linked enzyme aggregate (CLEA) is described. CLEAs were prepared by using ammonium sulfate as an aggregation agent followed by cross-linking with glutaraldehyde.The effect of different glutaraldehyde concentration on the recovery of enzyme activity in the CLEA and enzyme leakage from the CLEA matrix was investigated. Although activity recovery was low (21%) the CLEA facilitates easy separation and recycling of the nitrile hydratase. It was also found that the nitrile hydratase CLEA had substantially increased storage stability as well as increased operational stability during exposure to high concentration of acrylamide and acrylonitrile compared to that of thenitrile hydratase in the crude cell-free extract and whole cell formulation

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/OC%20D25.002" target="_blank" >OC D25.002: Nové, vysoce výtěžné a regioselektivní metody enzymové syntézy bioaktivních glykosidů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

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

Název periodika

Green Chemistry

ISSN

1463-9262

e-ISSN

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Svazek periodika

10

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

6

Strana od-do

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Kód UT WoS článku

000254443000006

EID výsledku v databázi Scopus

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