Direct bioelectrocatalysis at carbon electrodes modified with quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33

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A newly isolated, purified, and characterized PQQ-dependent alcohol dehydrogenase (a bacterial membrane-bound protein) was recently found to display a surprisingly large linear range and high selectivity towards ethanol when integrated into a conducting polymer network on a platinum electrode. These findings motivated us to study the enzyme when simply immobilized onto carbonaceous surfaces in order to establish its characteristics and suitability for sensor development, the sensor design being based on a direct-electron transfer pathway. Graphite rods and screen-printed electrodes were modified in two different ways, and were operated both in FIA and batch mode. The obtained biosensor characteristics were highly dependent on the sensor architecture, the highest sensitivity (179 mA M-1 cm(-2)) and lowest detection limit (1 muM) being obtained for screen-printed electrodes used in a batch mode. A mechanism of the observed direct electron transfer between the enzyme's active center and the electrode is proposed.


  • J Razumiene
  • M Niculescu
  • A Ramanavicius
  • V Laurinavicius
  • Elisabeth Csöregi
Enheter & grupper

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Kemi


Sidor (från-till)43-49
Utgåva nummer1
StatusPublished - 2002
Peer review utfördJa