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

0566826 - ÚFCH JH 2023 RIV CZ eng C - Konferenční příspěvek (zahraniční konf.)
Tvorynska, Sofiia - Barek, J. - Josypčuk, Bohdan - Nesměrák, K.
A comparative study of covalent glucose oxidase and laccase immobilization techniques at powdered supports for biosensors fabrication.
Proceedings of the 16th International Students Conference “Modern Analytical Chemistry”. Prague: Charles University, 2020 - (Nesměrák, K.), s. 25-30. ISBN 978-80-7444-079-3.
[International Students Conference “Modern Analytical Chemistry” /16./. Prague (CZ), 17.09.2020-18.09.2020]
Grant CEP: GA ČR(CZ) GA20-07350S
Institucionální podpora: RVO:61388955
Klíčová slova: biosensors * covalent immobilization * enzymatic reactor
Obor OECD: Physical chemistry
http://web.natur.cuni.cz/analchem/isc/isc16.pdf

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 (−NH 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 –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.
Trvalý link: https://hdl.handle.net/11104/0338103