Electroanalytical determination of peroxidases and laccases on carbon paste electrodes

Electrocatalytical reduction of hydrogen peroxide and oxygen was performed by horseradish peroxidase, recombinant Coprinus cinereus peroxidase, Polyporus pinsitus laccase and Botrytis cinerea laccase on carbon paste electrodes containing a paraffin soluble mediator. The electrocatalytical process pr...

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Veröffentlicht in:Electroanalysis (New York, N.Y.) N.Y.), 1997-02, Vol.9 (3), p.213-218
Hauptverfasser: Kulys, Juozas, Drungiliene, Alma, Wollenberger, Ulla, Krikstopaitis, Kastis, Scheller, Frieder
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container_end_page 218
container_issue 3
container_start_page 213
container_title Electroanalysis (New York, N.Y.)
container_volume 9
creator Kulys, Juozas
Drungiliene, Alma
Wollenberger, Ulla
Krikstopaitis, Kastis
Scheller, Frieder
description Electrocatalytical reduction of hydrogen peroxide and oxygen was performed by horseradish peroxidase, recombinant Coprinus cinereus peroxidase, Polyporus pinsitus laccase and Botrytis cinerea laccase on carbon paste electrodes containing a paraffin soluble mediator. The electrocatalytical process proceeded at 0.0V (vs Ag/AgCl; in situ electrode). The electrode responses had maximum values at pH 6.4 and 5.5 for the horseradish peroxidase and laccases catalyzed reactions, respectively. The sensitivity for horseradish peroxidase and recombinant Coprinus cinereus peroxidase was 23.4 and 5.4 μC nM−1 cm−2, respectively. A detection limit of 7.5 fmol horseradish peroxidase could thus be achieved. Systems based on laccases showed lower sensitivity. The model of electrocatalytical reduction of hydrogen peroxide and oxygen included a permanent liberation of mediator from the carbon paste and it's biocatalytical conversion in the diffusion layer. The model was analyzed by comparing kinetic data in homogeneous solution with the electrode response. Mass transport effects were studied by using rotating carbon paste electrodes.
doi_str_mv 10.1002/elan.1140090305
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The electrocatalytical process proceeded at 0.0V (vs Ag/AgCl; in situ electrode). The electrode responses had maximum values at pH 6.4 and 5.5 for the horseradish peroxidase and laccases catalyzed reactions, respectively. The sensitivity for horseradish peroxidase and recombinant Coprinus cinereus peroxidase was 23.4 and 5.4 μC nM−1 cm−2, respectively. A detection limit of 7.5 fmol horseradish peroxidase could thus be achieved. Systems based on laccases showed lower sensitivity. The model of electrocatalytical reduction of hydrogen peroxide and oxygen included a permanent liberation of mediator from the carbon paste and it's biocatalytical conversion in the diffusion layer. The model was analyzed by comparing kinetic data in homogeneous solution with the electrode response. 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The electrocatalytical process proceeded at 0.0V (vs Ag/AgCl; in situ electrode). The electrode responses had maximum values at pH 6.4 and 5.5 for the horseradish peroxidase and laccases catalyzed reactions, respectively. The sensitivity for horseradish peroxidase and recombinant Coprinus cinereus peroxidase was 23.4 and 5.4 μC nM−1 cm−2, respectively. A detection limit of 7.5 fmol horseradish peroxidase could thus be achieved. Systems based on laccases showed lower sensitivity. The model of electrocatalytical reduction of hydrogen peroxide and oxygen included a permanent liberation of mediator from the carbon paste and it's biocatalytical conversion in the diffusion layer. The model was analyzed by comparing kinetic data in homogeneous solution with the electrode response. 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subjects 1-(N
1‐(N,N‐dimethylamine)‐4‐(4‐morpholine)benzene
Botrytis cinerea laccase
Carbon paste electrode
Chemically modified electrode
Coprinus cinereus peroxidase
Graphite
Horseradish peroxidase
N-dimethylamine)-4-(4-morpholine)benzene
Polyporus pinsitus laccase
title Electroanalytical determination of peroxidases and laccases on carbon paste electrodes
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