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%2F00216208%3A11310%2F20%3A10420315" target="_blank" >RIV/00216208:11310/20:10420315 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388955:_____/20:00566826

  • 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 functionalized groups introduced at support surfaces (-NH2 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 -NH2 groups through glutaraldehyde to -NH2 functionalized supports, in particular SBA15-NH2 and cellulose-NH2 for glucose oxidase, MCM41-NH2 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

    10406 - Analytical chemistry

Result continuities

  • Project

  • Continuities

    S - Specificky vyzkum na vysokych skolach<br>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 &quot;Modern Analytical Chemistry&quot;

  • ISBN

    978-80-7444-079-3

  • ISSN

  • e-ISSN

  • Number of pages

    6

  • Pages from-to

    25-30

  • Publisher name

    Univerzita Karlova, Přírodovědecká fakulta

  • Place of publication

    Praha

  • Event location

    Prague

  • Event date

    Sep 17, 2020

  • Type of event by nationality

    EUR - Evropská akce

  • UT code for WoS article

    000623101400005