Recombinant pyranose dehydrogenase-A versatile enzyme possessing both mediated and direct electron transfer

Maria Yakovleva, Aniko Killyeni, Roberto Ortiz, Christopher Schulz, Domhnall MacAodha, Peter O. Conghaile, Donal Leech, Ionel Catalin Popescu, Christoph Gonaus, Clemens K. Peterbauer, Lo Gorton

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

Sammanfattning

The catalytical properties of glycosylated pyranose dehydrogenase (gPDH) and deglycosylated PDH (dgPDH) from Agaricus meleagris recombinantly expressed in Pichia pastoris were studied. Both gPDH and dgPDH were "wired" to an osmium redox polymer on graphite electrodes mounted in a flow-injection system. The current from oxidation of glucose by immobilised gPDH and dgPDH was compared using flow injection amperometry and cyclic voltammetry. An increase in the current density was observed for dgPDH (190 mu A cm(-2)) compared with that for gPDH (90 mu A cm(-2)) due to the improved electron transfer between the active site and the electrode. Additionally, the ability of dgPDH for direct electron transfer (DET) was discovered, which is rather unique among FAD-containing enzymes. The ability to oxidise a variety of sugars at a rather low potential makes dgPDH attractive for construction of biofuel cells with high power output. (C) 2012 Elsevier B.V. All rights reserved.
Originalspråkengelska
Sidor (från-till)120-122
TidskriftElectrochemistry Communications
Volym24
DOI
StatusPublished - 2012

Ämnesklassifikation (UKÄ)

  • Biologiska vetenskaper

Fingeravtryck

Utforska forskningsämnen för ”Recombinant pyranose dehydrogenase-A versatile enzyme possessing both mediated and direct electron transfer”. Tillsammans bildar de ett unikt fingeravtryck.

Citera det här