Direct electrochemistry of cellobiose dehydrogenase for applications in the third-generation biosensor and biofuel cell
|Hirotoshi Matsumura 1,2, Kiyohiko Igarashi 2, Nobuhumi Nakamura 3, Hiroyuki Ohno 3, Masahiro Samejima 2, Lo Gorton 1|
1. Lund University, Department of Analytical Chemistry, Lund SE-221 00, Sweden
Constructing biofuel cells and third-generation biosensors requires direct electron-transfer (DET) reactions, in which the electron transfer occurs directly between enzymes and electrodes. However, DET has been generally proven for a restricted number of redox enzymes which contain a catalytic domain and additionally a redox domain carrying metallocenters such as heme. One of these multidomain enzymes is cellobiose dehydrogenase (CDH). CDH is an extracellular hemoflavoenzyme, which is secreted by various cellulolytic fungi in the course of cellulose degradation. The CDH carries a flavin and a b-type heme in two separate domains. The flavin domain of basidiomycete CDH (class I) oxidizes the reducing-end group of cellobiose and higher cellooligosaccharides to their corresponding δ-lactones. The electrons are loaded from the flavin domain to some electrodes via the heme domain. In this study, DET-type bioelectrocatalytic oxidation of CDH from the basidiomycete Phanerochaete chrysosporium using carbon nanoparticles is reported. CDH was adsorbed onto carbon electrodes with carbon black (CB) (PRINTEX®30, Degussa). CB powder was mixed with DMF (80 : 20, w/w) to prepare a CB slurry. The slurry was applied to a carbon electrode and dried in a drying oven at 60 °C. A CDH solution was then cast on the CB-modified electrode. We have also investigated the optimal conditions of this CDH electrode. The CDH electrode was employed in the third-generation biosensor based and biofuel cell.
Presentation: Poster at SMCBS'2009 International Workshop, by Hirotoshi Matsumura
See On-line Journal of SMCBS'2009 International Workshop
Submitted: 2009-08-31 14:44 Revised: 2009-08-31 15:11
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