Salaj-Kosla, U,Poller, S,Schuhmann, W,Shleev, S,Magner, E

2013

January

Bioelectrochemistry

Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes

Published

()

Laccase Direct electron transfer Nanoporous gold BILIRUBIN OXIDASE ELECTROCATALYTIC REDUCTION MULTICOPPER OXIDASES OXYGEN REDUCTION FUNGAL LACCASES BIOSENSORS PROTEINS O-2 IMMOBILIZATION INHIBITION

91

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The enzyme Trametes hirsuta laccase undergoes direct electron transfer at unmodified nanoporous gold electrodes, displaying a current density of 28 mu A/cm(2). The response indicates that ThLc was immobilised at the surface of the nanopores in a manner which promoted direct electron transfer, in contrast to the absence of a response at unmodified polycrystalline gold electrodes. The bioelectrocatalytic activity of ThLc modified nanoporous gold electrodes was strongly dependent on the presence of halide ions. Fluoride completely inhibited the enzymatic response, whereas in the presence of 150 mM Cl-, the current was reduced to 50% of the response in the absence of Cl-. The current increased by 40% when the temperature was increased from 20 degrees C to 37 degrees C. The response is limited by enzymatic and/or enzyme electrode kinetics and is 30% of that observed for ThLc co-immobilised with an osmium redox polymer. (C) 2012 Elsevier B.V. All rights reserved.

10.1016/j.bioelechem.2012.11.001