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dc.contributor.authorZafar, Muhammad Nadeem
dc.contributor.authorBeden, Najat
dc.contributor.authorLeech, Dónal
dc.contributor.authorSygmund, Christoph
dc.contributor.authorLudwig, Roland
dc.contributor.authorGorton, Lo
dc.date.accessioned2018-09-20T16:28:55Z
dc.date.available2018-09-20T16:28:55Z
dc.date.issued2012-01-06
dc.identifier.citationZafar, Muhammad Nadeem; Beden, Najat; Leech, Dónal; Sygmund, Christoph; Ludwig, Roland; Gorton, Lo (2012). Characterization of different fad-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells. Analytical and Bioanalytical Chemistry 402 (6), 2069-2077
dc.identifier.issn1618-2642,1618-2650
dc.identifier.urihttp://hdl.handle.net/10379/14507
dc.description.abstractIn this study, different flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenases (FADGDHs) were characterized electrochemically after "wiring" them with an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)(2)(PVI)(10)Cl](+) on graphite electrodes. One tested FADGDH was that recently discovered in Glomerella cingulata (GcGDH), another was the recombinant form expressed in Pichia pastoris (rGcGDH), and the third was a commercially available glycosylated enzyme from Aspergillus sp. (AspGDH). The performance of the Os-polymer "wired" GDHs on graphite electrodes was tested with glucose as the substrate. Optimal operational conditions and analytical characteristics like sensitivity, linear ranges and current density of the different FADGDHs were determined. The performance of all three types of FADGDHs was studied at physiological conditions (pH 7.4). The current densities measured at a 20 mM glucose concentration were 494 +/- 17, 370 +/- 24, and 389 +/- 19 mu A cm(-2) for GcGDH, rGcGDH, and AspGDH, respectively. The sensitivities towards glucose were 2.16, 1.90, and 1.42 mu A mM(-1) for GcGDH, rGcGDH, and AspGDH, respectively. Additionally, deglycosylated rGcGDH (dgrGcGDH) was investigated to see whether the reduced glycosylation would have an effect, e.g., a higher current density, which was indeed found. GcGDH/Os-polymer modified electrodes were also used and investigated for their selectivity for a number of different sugars.
dc.publisherSpringer Nature
dc.relation.ispartofAnalytical and Bioanalytical Chemistry
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Ireland
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/3.0/ie/
dc.subjectglucose biosensor
dc.subjectfad
dc.subjectglucose dehydrogenase
dc.subjectos-polymer
dc.subjectdeglycosylation
dc.subjectbiofuel cell
dc.subjectdirect electron-transfer
dc.subjectenzymatic fuel-cells
dc.subjectgraphite-electrodes
dc.subjectcellobiose dehydrogenase
dc.subjectamperometric biosensors
dc.subjectadenine-dinucleotide
dc.subjectcatalytic-oxidation
dc.subjectcarbon electrodes
dc.subjectredox polymers
dc.subjectoxidase
dc.titleCharacterization of different fad-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells
dc.typeArticle
dc.identifier.doi10.1007/s00216-011-5650-7
dc.local.publishedsourcehttps://link.springer.com/content/pdf/10.1007%2Fs00216-011-5650-7.pdf
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Attribution-NonCommercial-NoDerivs 3.0 Ireland
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