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Original title:
A comparative study of covalent glucose oxidase and laccase immobilization techniques at powdered supports for biosensors fabrication
Authors: Tvorynska, Sofiia ; Barek, J. ; Josypčuk, Bohdan ; Nesměrák, K.
Document type: Papers
Conference/Event: International Students Conference “Modern Analytical Chemistry” /16./, Prague (CZ), 20200917
Year: 2020
Language: eng
Abstract: 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\ngroups introduced at support surfaces (−NH and −COOH), and the methods of activation (glutaraldehyde and carbodiimide). Amino and carboxyl functionalized mesoporous silica and cellulose powders\nwere 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.
Keywords: biosensors; covalent immobilization; enzymatic reactor
Project no.: GA20-07350S (CEP)
Funding provider: GA ČR
Host item entry: Proceedings of the 16th International Students Conference “Modern Analytical Chemistry”, ISBN 978-80-7444-079-3
Institution: J. Heyrovsky Institute of Physical Chemistry AS ČR (web)
Document availability information: Fulltext is available at external website.
External URL: http://web.natur.cuni.cz/analchem/isc/isc16.pdf
Original record: https://hdl.handle.net/11104/0338103
Permalink: http://www.nusl.cz/ntk/nusl-519843
The record appears in these collections:
Research > Institutes ASCR > J. Heyrovsky Institute of Physical Chemistry
Conference materials > Papers
Authors: Tvorynska, Sofiia ; Barek, J. ; Josypčuk, Bohdan ; Nesměrák, K.
Document type: Papers
Conference/Event: International Students Conference “Modern Analytical Chemistry” /16./, Prague (CZ), 20200917
Year: 2020
Language: eng
Abstract: 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\ngroups introduced at support surfaces (−NH and −COOH), and the methods of activation (glutaraldehyde and carbodiimide). Amino and carboxyl functionalized mesoporous silica and cellulose powders\nwere 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.
Keywords: biosensors; covalent immobilization; enzymatic reactor
Project no.: GA20-07350S (CEP)
Funding provider: GA ČR
Host item entry: Proceedings of the 16th International Students Conference “Modern Analytical Chemistry”, ISBN 978-80-7444-079-3
Institution: J. Heyrovsky Institute of Physical Chemistry AS ČR (web)
Document availability information: Fulltext is available at external website.
External URL: http://web.natur.cuni.cz/analchem/isc/isc16.pdf
Original record: https://hdl.handle.net/11104/0338103
Permalink: http://www.nusl.cz/ntk/nusl-519843
The record appears in these collections:
Research > Institutes ASCR > J. Heyrovsky Institute of Physical Chemistry
Conference materials > Papers
Record created 2023-01-15, last modified 2023-12-06