A comparative study of covalent glucose oxidase and laccase immobilization techniques at powdered supports for biosensors fabrication
The result's identifiers
Result code in 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>
Alternative codes found
RIV/00216208:11310/20:10420315
Result on the web
<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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Alternative languages
Result language
angličtina
Original language name
A comparative study of covalent glucose oxidase and laccase immobilization techniques at powdered supports for biosensors fabrication
Original language description
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.
Czech name
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Czech description
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Classification
Type
D - Article in proceedings
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/GA20-07350S" target="_blank" >GA20-07350S: Electrochemical and analytical aspects of the transport of addictive and psychotropic drugs across the model biological barriers</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Article name in the collection
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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Number of pages
6
Pages from-to
25-30
Publisher name
Charles University
Place of publication
Prague
Event location
Prague
Event date
Sep 17, 2020
Type of event by nationality
WRD - Celosvětová akce
UT code for WoS article
000623101400005