Výhody předimobilizace enyzmů na porézním nosiči pro jejich zachycení v sol-gelu

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Advantages of the Pre-Immobilization of Enzymes on Porous Supports for Their Entrapment in Sol-Gels

Popis výsledku v původním jazyce

In this work, we have compared the entrapment of free or immobilized on a porous support (Sepabeads using glutaraldehyde technique) glucose oxidase using a sol-gel technique. The previous immobilization of the enzyme permitted to keep the enzyme activityafter sol-gel formation (only 10% of the enzyme activity was lost whereas the soluble enzyme lost 60% of its initial activity) and to avoid enzyme leakage from the sol-gel matrix, which was relatively high when entrapping the soluble enzyme (39 % of theenzyme activity was released after 16 hr of incubation in a buffered solution). Moreover, the immobilized enzyme, inside the porous support, cannot be in contact with the sol-gel and maintained the stability achieved by multipoint covalent attachment onthe Sepabeads, giving much better stability than the one achieved by trapping the soluble enzyme.

Název v anglickém jazyce

Advantages of the Pre-Immobilization of Enzymes on Porous Supports for Their Entrapment in Sol-Gels

Popis výsledku anglicky

In this work, we have compared the entrapment of free or immobilized on a porous support (Sepabeads using glutaraldehyde technique) glucose oxidase using a sol-gel technique. The previous immobilization of the enzyme permitted to keep the enzyme activityafter sol-gel formation (only 10% of the enzyme activity was lost whereas the soluble enzyme lost 60% of its initial activity) and to avoid enzyme leakage from the sol-gel matrix, which was relatively high when entrapping the soluble enzyme (39 % of theenzyme activity was released after 16 hr of incubation in a buffered solution). Moreover, the immobilized enzyme, inside the porous support, cannot be in contact with the sol-gel and maintained the stability achieved by multipoint covalent attachment onthe Sepabeads, giving much better stability than the one achieved by trapping the soluble enzyme.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název periodika

Biomacromolecules

ISSN

1525-7797

e-ISSN

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Svazek periodika

6

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

4

Strana od-do

1027-1030

Kód UT WoS článku

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EID výsledku v databázi Scopus

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