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dc.contributor.authorGuto, Peterson M
dc.contributor.authorKamau, Geoffrey N
dc.date.accessioned2013-02-26T14:25:41Z
dc.date.issued2010
dc.identifier.citationElectroanalysis 2010, 22, No.11, 1186–1190en
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/11857
dc.description.abstractThis work demonstrated for the first time that myoglobin cross-linked in polylysine films is electrochemically active at 68C. At 68C, these protein films exhibited reversible reduction/oxidation peaks which are characteristic of FeIII/FeII redox couple. The estimated current function densities (J = 1.6104 C/V cm2), surface concentrations (0.10 nmol/cm2) and standard electron transfer constant (k)at68C for the data taken at a scan rate of 0.1 V/s were similar to those which were obtained at 10, 15 and 238C. Basically, this study shows a possible electrocatalytic application of these myoglobin/polylysine films, for example in low temperature sensing applications.en
dc.language.isoenen
dc.publisherWileyen
dc.subjectMyoglobinen
dc.subjectPolylysineen
dc.subjectCyclicvoltammetryen
dc.subjectSquarewavevoltammetryen
dc.subjectPyrolyticgraphiteelectrode(PGE)en
dc.subjectBiocatalysisen
dc.titleElectrochemical Characterization of Myoglobin-Polylysine Films at a Temperature Range of 6–808Cen
dc.typeArticleen
local.publisherChemistryen


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