Effect of Deglycosylation of Cellobiose Dehydrogenases on the Enhancement of Direct Electron Transfer with Electrodes

Research output: Contribution to journalArticle

Abstract

Cellobiose dehydrogenase (CDH) is a monomeric extracellular flavocytochrome composed of a catalytic dehydrogenase domain (DHCDH) containing flavin adenine dinucleotide (FAD), a cytochrome domain (CYTCDH) containing heme b, and a linker region connecting the two domains. In this work, the effect of deglycosylation on the electrochemical properties of CDH from Phanerochaete chrysosporium (PcCDH) and Ceriporiopsis subvermispora (CsCDH) is presented. All the glycosylated and deglycosylated enzymes show direct electron transfer (DET) between the CYTCDH and the electrode. Graphite electrodes modified with deglycosylated PcCDH (dPcCDH) and CsCDH (dCsCDH) have a 40-65% higher I-max value in the presence of substrate than electrodes modified with their glycosylated counterparts. CsCDH trapped under a permselective membrane showed similar changes on gold electrodes protected by a thiol-based self-assembled monolayer (SAM), in contrast to PcCDH for which deglycosylation did not exhibit any different electrocatalytical response on SAM-modified gold electrodes. Glycosylated PcCDH was found to have a 30% bigger hydrodynamic radius than dPcCDH using dynamic light scattering. The basic bioelectrochemistry as well as the bioelectrocatalytic properties are presented.

Details

Authors
  • Roberto Ortiz
  • Hirotoshi Matsumura
  • Federico Tasca
  • Kawah Zahma
  • Masahiro Samejima
  • Kiyohiko Igarashi
  • Roland Ludwig
  • Lo Gorton
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Analytical Chemistry
Original languageEnglish
Pages (from-to)10315-10323
JournalAnalytical Chemistry
Volume84
Issue number23
Publication statusPublished - 2012
Publication categoryResearch
Peer-reviewedYes

Bibliographic note

The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004), Biochemistry and Structural Biology (S) (000006142)

Related research output

Ortiz, R., 2013, Department of Chemistry, Lund University. 262 p.

Research output: ThesisDoctoral Thesis (compilation)

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