日本語フィールド
著者：Masato Tominaga, Aiko Sasaki, Makoto Togami題名：Bioelectrocatalytic Oxygen Reaction and Chloride Inhibition Resistance of Laccase Immobilized on Single-walled Carbon Nanotube and Carbon Paper Electrodes発表情報： 巻: 84 号: 5 ページ: 315-31キーワード：概要：The rate of heterogeneous direct electron transfer of laccase immobilized on single-walled carbon nanotube
(SWCNT) and carbon paper electrodes was evaluated by cyclic voltammetry and background-current-corrected
steady-state linear voltammetry. These rates indicated that the molecular orientation of laccase immobilized on the
SWCNT electrode was more favorable for direct electron transfer, than that of laccase immobilized on the carbon
paper electrode. The inhibition of the bioelectrocatalytic O2 reduction current of the two electrodes by chloride
and fluoride were tested. The results indicated differing inhibition mechanisms by these two halides. Laccase
immobilized on the SWCNT electrode exhibited high stability and high resistance to chloride inhibition.抄録：英語フィールド
Author：Masato Tominaga, Aiko Sasaki, Makoto TogamiTitle：Bioelectrocatalytic Oxygen Reaction and Chloride Inhibition Resistance of Laccase Immobilized on Single-walled Carbon Nanotube and Carbon Paper ElectrodesAnnouncement information: Vol: 84 Issue: 5 Page: 315-31An abstract：The rate of heterogeneous direct electron transfer of laccase immobilized on single-walled carbon nanotube
(SWCNT) and carbon paper electrodes was evaluated by cyclic voltammetry and background-current-corrected
steady-state linear voltammetry. These rates indicated that the molecular orientation of laccase immobilized on the
SWCNT electrode was more favorable for direct electron transfer, than that of laccase immobilized on the carbon
paper electrode. The inhibition of the bioelectrocatalytic O2 reduction current of the two electrodes by chloride
and fluoride were tested. The results indicated differing inhibition mechanisms by these two halides. Laccase
immobilized on the SWCNT electrode exhibited high stability and high resistance to chloride inhibition.