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Engineering of pyranose dehydrogenase for application to enzymatic anodes in biofuel cells.

Yakovleva, Maria LU ; Gonaus, Christoph; Schropp, Katharina; ÓConghaile, Peter; Leech, Dónal; Peterbauer, Clemens K and Gorton, Lo LU (2015) In Physical Chemistry Chemical Physics 17(14). p.9074-9081
Abstract
In the search for improved glucose oxidising enzymes for biofuel cells, a number of Agaricus meleagris (Am) pyranose dehydrogenase mutants (mPDHs) exhibiting different degrees of glycosylation were produced using site-directed mutagenesis and electrochemically characterised. The response of electrodes modified with different mPDHs is compared in a mediated electron transfer mode, where the electrodes are modified with each of the mutants covalently attached to redox polymers based on polyvinylimidazole-bound osmium complexes using a cross-linking agent. Coating of each of the enzymes onto the graphite electrode surface is also used to screen for their capacity for direct electron transfer. The double mutant PDH exhibits the highest... (More)
In the search for improved glucose oxidising enzymes for biofuel cells, a number of Agaricus meleagris (Am) pyranose dehydrogenase mutants (mPDHs) exhibiting different degrees of glycosylation were produced using site-directed mutagenesis and electrochemically characterised. The response of electrodes modified with different mPDHs is compared in a mediated electron transfer mode, where the electrodes are modified with each of the mutants covalently attached to redox polymers based on polyvinylimidazole-bound osmium complexes using a cross-linking agent. Coating of each of the enzymes onto the graphite electrode surface is also used to screen for their capacity for direct electron transfer. The double mutant PDH exhibits the highest response to glucose at physiological pH in both direct and mediated electron transfer modes, producing a Jmax of ≈800 μA cm(-2) at room temperature and when "wired" to the Os-polymer having the highest formal potential. From the results obtained the double mPDH is proposed as the most suitable candidate for application to bioanode fabrication. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
in
Physical Chemistry Chemical Physics
volume
17
issue
14
pages
9074 - 9081
publisher
Royal Society of Chemistry
external identifiers
  • pmid:25752794
  • wos:000351933600061
  • scopus:84961288356
ISSN
1463-9084
DOI
10.1039/c5cp00430f
language
English
LU publication?
yes
id
ffa5a7cc-e557-4f2a-85f1-094bd2ea9998 (old id 5264991)
date added to LUP
2015-04-16 13:52:44
date last changed
2017-10-22 03:16:01
@article{ffa5a7cc-e557-4f2a-85f1-094bd2ea9998,
  abstract     = {In the search for improved glucose oxidising enzymes for biofuel cells, a number of Agaricus meleagris (Am) pyranose dehydrogenase mutants (mPDHs) exhibiting different degrees of glycosylation were produced using site-directed mutagenesis and electrochemically characterised. The response of electrodes modified with different mPDHs is compared in a mediated electron transfer mode, where the electrodes are modified with each of the mutants covalently attached to redox polymers based on polyvinylimidazole-bound osmium complexes using a cross-linking agent. Coating of each of the enzymes onto the graphite electrode surface is also used to screen for their capacity for direct electron transfer. The double mutant PDH exhibits the highest response to glucose at physiological pH in both direct and mediated electron transfer modes, producing a Jmax of ≈800 μA cm(-2) at room temperature and when "wired" to the Os-polymer having the highest formal potential. From the results obtained the double mPDH is proposed as the most suitable candidate for application to bioanode fabrication.},
  author       = {Yakovleva, Maria and Gonaus, Christoph and Schropp, Katharina and ÓConghaile, Peter and Leech, Dónal and Peterbauer, Clemens K and Gorton, Lo},
  issn         = {1463-9084},
  language     = {eng},
  number       = {14},
  pages        = {9074--9081},
  publisher    = {Royal Society of Chemistry},
  series       = {Physical Chemistry Chemical Physics},
  title        = {Engineering of pyranose dehydrogenase for application to enzymatic anodes in biofuel cells.},
  url          = {http://dx.doi.org/10.1039/c5cp00430f},
  volume       = {17},
  year         = {2015},
}