Structural and Electrochemical Properties of Self-organized HFBI Membranes on Different Types of Substrates
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- YAMASAKI Ryota
- Division of Functional Interface Engineering, Department of Biological Functions Engineering, Kyushu Institute of Technology Research center for Eco-fitting Technology, Kyushu Institute of Technology Advanced Catalytic Transformation program for Carbon utilization (ACT-C), Japan Science and Technology Agency (JST)
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- ASAKAWA Hitoshi
- Advanced Catalytic Transformation program for Carbon utilization (ACT-C), Japan Science and Technology Agency (JST) Division of Electrical Engineering and Computer Science, Kanazawa University Bio-AFM Frontier Research Center, Kanazawa University
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- FUKUMA Takeshi
- Advanced Catalytic Transformation program for Carbon utilization (ACT-C), Japan Science and Technology Agency (JST) Division of Electrical Engineering and Computer Science, Kanazawa University Bio-AFM Frontier Research Center, Kanazawa University
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- HARUYAMA Tetsuya
- Division of Functional Interface Engineering, Department of Biological Functions Engineering, Kyushu Institute of Technology Research center for Eco-fitting Technology, Kyushu Institute of Technology Advanced Catalytic Transformation program for Carbon utilization (ACT-C), Japan Science and Technology Agency (JST)
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The HFBI protein, a type of hydrophobin, from Trichoderma reesei self-organizes in an orderly manner at either air/water or water/solid interfaces. The structural and electrochemical properties of self-organized membranes on different types of solid substrates (electrode materials) were investigated. Two types of substrates, highly oriented pyrolytic graphite (HOPG) and single crystal Au(111), were used for this study. Atomic force microscopy (AFM) showed that the self-organized HFBI membranes (prepared at the air/water interface) exhibited different structures on the two types of electrodes. In terms of the electrochemical results, both HFBI/HOPG and HFBI/Au(111) electrodes performed electrochemical reactions. Self-organized HFBI membranes did not provide insulation from electron transfer. Our findings that HFBI can be tagged with functional proteins, such as enzymes, by genetic fusion and utilized as a molecular carrier to fabricate molecular interfaces on an electrode.
収録刊行物
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- Electrochemistry
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Electrochemistry 83 (11), 969-973, 2015
公益社団法人 電気化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681476903936
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- NII論文ID
- 130005107651
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- NII書誌ID
- AN00151637
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- ISSN
- 21862451
- 13443542
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- NDL書誌ID
- 026839562
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用可