Peer-Reviewed Journal Details
Mandatory Fields
Yakovleva, ME,Gonaus, C,Schropp, K,OConghaile, P,Leech, D,Peterbauer, CK,Gorton, L
2015
July
Physical Chemistry Chemical Physics
Engineering of pyranose dehydrogenase for application to enzymatic anodes in biofuel cells
Published
WOS: 10 ()
Optional Fields
DIRECT ELECTRON-TRANSFER AGARICUS-MELEAGRIS CELLOBIOSE DEHYDROGENASE COULOMBIC EFFICIENCY REDOX POLYMER FUEL-CELLS HORSERADISH-PEROXIDASE PHYSIOLOGICAL BUFFER RECOMBINANT FORMS GLUCOSE-OXIDATION
17
9074
9081
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 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.
10.1039/c5cp00430f
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