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

Result code in 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>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

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

Original language description

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

Czech name

Nitrile hydratase CLEAs: Imobilizace a stabilizace průmyslově důležitého enzymu

Czech description

Je popsána úspěšná imobilizace a stabilizace enzymu nitril hydratasy ve formě cross-linkovaných enzymových agregátů (CLEA). CLEA byly připraveny agregací proteinu síranem amonným a následným cross-linkingem glutaraldehydem. Byl zkoumán vliv různé koncentrace glutaraldehydu na výslednou aktivitu agregátů a uvolňování enzymu z agregátů. Přestože výsledná aktivita CLEA agregátů byla pouze 21%, skladovací stabilita byla oproti použití hrubého extraktu nebo celých buněk značně navýšena, stejně jako reakční stabilita, kdy byly agregáty vystaveny vysokým koncentracím acrylamidu a acrylonitrilu

Type

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

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/OC%20D25.002" target="_blank" >OC D25.002: New Enzymes and Selective Methods for Glycosidase-Catalysed Synthesis of Bioactive Glycosides and Glycomimetics</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2008

Confidentiality

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

Name of the periodical

Green Chemistry

ISSN

1463-9262

e-ISSN

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Volume of the periodical

10

Issue of the periodical within the volume

4

Country of publishing house

GB - UNITED KINGDOM

Number of pages

6

Pages from-to

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UT code for WoS article

000254443000006

EID of the result in the Scopus database

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