Improvement in Electron Transfer Efficiency Between Multicopper Oxidase and Electrode by Immobilization of Directly Oriented Enzyme Molecules
Source abstract
Abstract
We investigated the effects of the distance between redox site of multicopper oxidase from Pyrobaculum aerophilum (McoP) and the electrode surface on efficient electron transfer to optimize biodevice performance. The O2 reduction peak current densities of the electrode on which McoP was directly immobilized using C-terminus His-tagged and Cys residue introduced McoP, and the electrode on which McoP was immobilized using C-terminus His-tagged McoP and self-assembled monolayer (SAM) were 203.6 µA/cm2 and 167.4 µA/cm2, respectively. The O2 reduction current per unit enzyme activity of McoP was 88.9 mA/units in the electrode on which McoP was directly immobilized using C-terminus His-tagged and Cys residue introduced McoP, and 68.4 mA/units in the electrode on which McoP was immobilized using C-terminus Histagged McoP and SAM. McoP was directly immobilized onto Au electrode while controlling McoP orientation using cysteine residue on the C-terminus of McoP. As a result, O2 reduction current was increased. Improving the electron transfer efficiency between redox site of McoP and electrode surface was achieved by reducing the distance between them.
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Research context
OpenAlex topics: Electrochemical sensors and biosensors · Electrochemical Analysis and Applications · Advanced Nanomaterials in Catalysis
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Affiliations
Department of Advanced Interdisciplinary Science and Technology, Graduate School of Engineering, University of Fukui
Department of Frontier Fiber Technology and Science, Graduate School of Engineering, University of Fukui
Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui
Department of Applied Biological Science, Faculty of Agriculture, Kagawa University
Department of Biomedical Engineering, Faculty of Engineering, Osaka Institute of Technology
References (21)
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