All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

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

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

  • Czech description

Classification

  • Type

    D - Article in proceedings

  • CEP classification

  • 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

  • e-ISSN

  • 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