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%2F61388955%3A_____%2F20%3A00566826" target="_blank" >RIV/61388955:_____/20:00566826 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/20:10420315

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 functionalizedngroups introduced at support surfaces (−NH and −COOH), and the methods of activation (glutaraldehyde and carbodiimide). Amino and carboxyl functionalized mesoporous silica and cellulose powdersnwere prepared by silanization using (3-aminopropyl)triethoxysilane and carboxyethylsilanetriol, respectively. It was found that coupling of both enzymes by their –NH groups through glutaraldehyde to -NH functionalized supports, in particular SBA15−NH and cellulose−NH for glucose oxidase, MCM41−NH 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 functionalizedngroups introduced at support surfaces (−NH and −COOH), and the methods of activation (glutaraldehyde and carbodiimide). Amino and carboxyl functionalized mesoporous silica and cellulose powdersnwere prepared by silanization using (3-aminopropyl)triethoxysilane and carboxyethylsilanetriol, respectively. It was found that coupling of both enzymes by their –NH groups through glutaraldehyde to -NH functionalized supports, in particular SBA15−NH and cellulose−NH for glucose oxidase, MCM41−NH for laccase, showed the highest activity and the best stability.

Druh

D - Stať ve sborníku

CEP obor

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OECD FORD obor

10403 - Physical chemistry

Projekt

<a href="/cs/project/GA20-07350S" target="_blank" >GA20-07350S: Elektrochemické a analytické aspekty transportu návykových a psychotropních látek přes modelové biologické bariery</a><br>

Návaznosti

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 “Modern Analytical Chemistry”

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

Charles University

Místo vydání

Prague

Místo konání akce

Prague

Datum konání akce

17. 9. 2020

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

000623101400005