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dc.contributor.authorYakovleva, Maria E.
dc.contributor.authorGonaus, Christoph
dc.contributor.authorSchropp, Katharina
dc.contributor.authorÓConghaile, Peter
dc.contributor.authorLeech, Dónal
dc.contributor.authorPeterbauer, Clemens K.
dc.contributor.authorGorton, Lo
dc.date.accessioned2018-09-20T16:28:43Z
dc.date.available2018-09-20T16:28:43Z
dc.date.issued2015-01-01
dc.identifier.citationYakovleva, Maria E. Gonaus, Christoph; Schropp, Katharina; ÓConghaile, Peter; Leech, Dónal; Peterbauer, Clemens K.; Gorton, Lo (2015). Engineering of pyranose dehydrogenase for application to enzymatic anodes in biofuel cells. Phys. Chem. Chem. Phys. 17 (14), 9074-9081
dc.identifier.issn1463-9076,1463-9084
dc.identifier.urihttp://hdl.handle.net/10379/14473
dc.description.abstractIn 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 J(max) of approximate to 800 mu A 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.
dc.publisherRoyal Society of Chemistry (RSC)
dc.relation.ispartofPhys. Chem. Chem. Phys.
dc.subjectdirect electron-transfer
dc.subjectagaricus-meleagris
dc.subjectcellobiose dehydrogenase
dc.subjectcoulombic efficiency
dc.subjectredox polymer
dc.subjectfuel-cells
dc.subjecthorseradish-peroxidase
dc.subjectphysiological buffer
dc.subjectrecombinant forms
dc.subjectglucose-oxidation
dc.titleEngineering of pyranose dehydrogenase for application to enzymatic anodes in biofuel cells
dc.typeArticle
dc.identifier.doi10.1039/c5cp00430f
dc.local.publishedsourcehttp://pubs.rsc.org/en/content/articlepdf/2015/cp/c5cp00430f
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