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Direct electron transfer at cellobiose dehydrogenase modified anodes for biofuel cells

Tasca, Federico LU ; Gorton, Lo LU ; Harreither, Wolfgang; Haltrich, Dietmar; Ludwig, Roland and Nöll, Gilbert LU (2008) In Journal of Physical Chemistry C 112(26). p.9956-9961
Abstract
Cellobiose dehydrogenases (CDHs, EC 1.1.99.18) contain a larger flavin-associated (dehydrogenase) domain and a smaller heme-binding (cytochrome) domain. CDHs from basidiomycete fungi oxidize at an appreciable level cellobiose, cellodextrins, and lactose, and those from ascomycetes may additionally oxidize some monosaccharides to their corresponding lactones at the flavin domain. CDHs are able to communicate directly with an electrode via their heme domain. In this work, different types of CDHs have been adsorbed on graphite electrodes and studied with respect to their direct electron transfer (DET) properties. Electrochemical studies were performed in the presence and absence of single-walled carbon nanotubes (SWCNTs) using lactose as... (More)
Cellobiose dehydrogenases (CDHs, EC 1.1.99.18) contain a larger flavin-associated (dehydrogenase) domain and a smaller heme-binding (cytochrome) domain. CDHs from basidiomycete fungi oxidize at an appreciable level cellobiose, cellodextrins, and lactose, and those from ascomycetes may additionally oxidize some monosaccharides to their corresponding lactones at the flavin domain. CDHs are able to communicate directly with an electrode via their heme domain. In this work, different types of CDHs have been adsorbed on graphite electrodes and studied with respect to their direct electron transfer (DET) properties. Electrochemical studies were performed in the presence and absence of single-walled carbon nanotubes (SWCNTs) using lactose as substrate. In the presence of SWCNTs, the electrocatalytic current for substrate oxidation based on DET between enzyme and electrode was significantly increased. Furthermore, the onset of the electrocatalytic current was at lower potential than in the absence of SWCNTs. The highest electrocatalytic activity toward oxidation of lactose was found for CDH from the basidiomycete Phanerochaete sordida. Based on CDH from Phanerochaete sordida, an anode for biofuel cells was developed. This anode using lactose as substrate was combined with a Pt black cathode for oxygen reduction as a model for a membrane-less biofuel cell in which the processes at both electrodes occur by DET. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Physical Chemistry C
volume
112
issue
26
pages
9956 - 9961
publisher
The American Chemical Society
external identifiers
  • wos:000257155200060
  • scopus:48249108041
ISSN
1932-7447
DOI
10.1021/jp802099p
language
English
LU publication?
yes
id
d994f386-8e75-44cd-90ec-3f47df02c599 (old id 1186892)
date added to LUP
2008-09-04 09:41:35
date last changed
2017-09-10 03:35:05
@article{d994f386-8e75-44cd-90ec-3f47df02c599,
  abstract     = {Cellobiose dehydrogenases (CDHs, EC 1.1.99.18) contain a larger flavin-associated (dehydrogenase) domain and a smaller heme-binding (cytochrome) domain. CDHs from basidiomycete fungi oxidize at an appreciable level cellobiose, cellodextrins, and lactose, and those from ascomycetes may additionally oxidize some monosaccharides to their corresponding lactones at the flavin domain. CDHs are able to communicate directly with an electrode via their heme domain. In this work, different types of CDHs have been adsorbed on graphite electrodes and studied with respect to their direct electron transfer (DET) properties. Electrochemical studies were performed in the presence and absence of single-walled carbon nanotubes (SWCNTs) using lactose as substrate. In the presence of SWCNTs, the electrocatalytic current for substrate oxidation based on DET between enzyme and electrode was significantly increased. Furthermore, the onset of the electrocatalytic current was at lower potential than in the absence of SWCNTs. The highest electrocatalytic activity toward oxidation of lactose was found for CDH from the basidiomycete Phanerochaete sordida. Based on CDH from Phanerochaete sordida, an anode for biofuel cells was developed. This anode using lactose as substrate was combined with a Pt black cathode for oxygen reduction as a model for a membrane-less biofuel cell in which the processes at both electrodes occur by DET.},
  author       = {Tasca, Federico and Gorton, Lo and Harreither, Wolfgang and Haltrich, Dietmar and Ludwig, Roland and Nöll, Gilbert},
  issn         = {1932-7447},
  language     = {eng},
  number       = {26},
  pages        = {9956--9961},
  publisher    = {The American Chemical Society},
  series       = {Journal of Physical Chemistry C},
  title        = {Direct electron transfer at cellobiose dehydrogenase modified anodes for biofuel cells},
  url          = {http://dx.doi.org/10.1021/jp802099p},
  volume       = {112},
  year         = {2008},
}