Electrochemical Characterization of Myoglobin-Polylysine Films at a Temperature Range of 6-80 degree C
This work demonstrated for the first time that myoglobin cross-linked in polylysine films is electrochemically active at 6 degree C. At 6 degree C, these protein films exhibited reversible reduction/oxidation peaks which are characteristic of FeIII/FeII redox couple. The estimated current function d...
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Veröffentlicht in: | Electroanalysis (New York, N.Y.) N.Y.), 2010-06, Vol.22 (11), p.1186-1190 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | This work demonstrated for the first time that myoglobin cross-linked in polylysine films is electrochemically active at 6 degree C. At 6 degree C, these protein films exhibited reversible reduction/oxidation peaks which are characteristic of FeIII/FeII redox couple. The estimated current function densities (J=1.6X10-4 C/V cm2), surface concentrations (T=0.10 nmol/cm2) and standard electron transfer constant (ks=13.86 s-1) at 6 degree C for the data taken at a scan rate of 0.1 V/s were similar to those which were obtained at 10, 15 and 23 degree C. Basically, this study shows a possible electrocatalytic application of these myoglobin/polylysine films, for example in low temperature sensing applications. |
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ISSN: | 1040-0397 |
DOI: | 10.1002/elan.200900463 |