Influence of Carrier Area on Properties of Immobilized Cellulase Complex

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26310%2F15%3APU115377" target="_blank" >RIV/00216305:26310/15:PU115377 - 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

Influence of Carrier Area on Properties of Immobilized Cellulase Complex

Popis výsledku v původním jazyce

Commercial cellulase preparation Celluclast 1.5 L was attached to the synthetic carrier from polyethylene terephtalate (PET) of different surface area, when applying the activation with glutaraldehyde. It was found that all carriers used have always bound the entire amount of the enzyme. The highest relative activity have retained the preparation bound to the carrier with the largest particle size. During the one month storage at 4 °C this preparation showed no decrease in activity. After the immobilization no change of the pH optimum was observed, when compared to the free enzyme. Simultaneously, any change of the any change of the temperature optimum was not proved in comparison to the free enzyme. From experiments, in which the decrease of viscosityof the polymeric substrate as a function of the percentage of cleaved glycosidic linkages was observed, follow that the immobilization alone does not substantially change the mode of action of the immobilized preparation.

Název v anglickém jazyce

Influence of Carrier Area on Properties of Immobilized Cellulase Complex

Popis výsledku anglicky

Commercial cellulase preparation Celluclast 1.5 L was attached to the synthetic carrier from polyethylene terephtalate (PET) of different surface area, when applying the activation with glutaraldehyde. It was found that all carriers used have always bound the entire amount of the enzyme. The highest relative activity have retained the preparation bound to the carrier with the largest particle size. During the one month storage at 4 °C this preparation showed no decrease in activity. After the immobilization no change of the pH optimum was observed, when compared to the free enzyme. Simultaneously, any change of the any change of the temperature optimum was not proved in comparison to the free enzyme. From experiments, in which the decrease of viscosityof the polymeric substrate as a function of the percentage of cleaved glycosidic linkages was observed, follow that the immobilization alone does not substantially change the mode of action of the immobilized preparation.

Druh

O - Ostatní výsledky

CEP obor

EI - Biotechnologie a bionika

OECD FORD obor

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Projekt

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Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2015

Kód důvěrnosti údajů

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