A comparative study of covalent glucose oxidase and laccase immobilization techniques at powdered supports for biosensors fabrication

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F20%3A10420315" target="_blank" >RIV/00216208:11310/20:10420315 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388955:_____/20:00566826

Výsledek na webu

<a href="http://web.natur.cuni.cz/analchem/isc/isc16.pdf" target="_blank" >http://web.natur.cuni.cz/analchem/isc/isc16.pdf</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

A comparative study of covalent glucose oxidase and laccase immobilization techniques at powdered supports for biosensors fabrication

Popis výsledku v původním jazyce

In order to develop the optimal strategy and to deepen the knowledge in the field of enzyme immobilization, three different techniques of covalent binding for two enzymes (glucose oxidase and laccase) at powdered surfaces were compared. Immobilization protocol was optimized by changing supports (two mesoporous silica powders (SBA-15, MCM-41) and a cellulose powder), the functionalized groups introduced at support surfaces (-NH2 and -COOH), and the methods of activation (glutaraldehyde and carbodiimide). Amino and carboxyl functionalized mesoporous silica and cellulose powders were prepared by silanization using (3-aminopropyl)triethoxysilane and carboxyethylsilanetriol, respectively. It was found that coupling of both enzymes by their -NH2 groups through glutaraldehyde to -NH2 functionalized supports, in particular SBA15-NH2 and cellulose-NH2 for glucose oxidase, MCM41-NH2 for laccase, showed the highest activity and the best stability.

Název v anglickém jazyce

A comparative study of covalent glucose oxidase and laccase immobilization techniques at powdered supports for biosensors fabrication

Popis výsledku anglicky

In order to develop the optimal strategy and to deepen the knowledge in the field of enzyme immobilization, three different techniques of covalent binding for two enzymes (glucose oxidase and laccase) at powdered surfaces were compared. Immobilization protocol was optimized by changing supports (two mesoporous silica powders (SBA-15, MCM-41) and a cellulose powder), the functionalized groups introduced at support surfaces (-NH2 and -COOH), and the methods of activation (glutaraldehyde and carbodiimide). Amino and carboxyl functionalized mesoporous silica and cellulose powders were prepared by silanization using (3-aminopropyl)triethoxysilane and carboxyethylsilanetriol, respectively. It was found that coupling of both enzymes by their -NH2 groups through glutaraldehyde to -NH2 functionalized supports, in particular SBA15-NH2 and cellulose-NH2 for glucose oxidase, MCM41-NH2 for laccase, showed the highest activity and the best stability.

Druh

D - Stať ve sborníku

CEP obor

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OECD FORD obor

10406 - Analytical chemistry

Projekt

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Návaznosti

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

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název statě ve sborníku

Proceedings of the 16th International Students Conference &quot;Modern Analytical Chemistry&quot;

ISBN

978-80-7444-079-3

ISSN

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e-ISSN

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Počet stran výsledku

6

Strana od-do

25-30

Název nakladatele

Univerzita Karlova, Přírodovědecká fakulta

Místo vydání

Praha

Místo konání akce

Prague

Datum konání akce

17. 9. 2020

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

000623101400005