| Project/Area Number |
18510099
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Nanomaterials/Nanobioscience
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| Research Institution | Kumamoto University |
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Principal Investigator |
TOMINAGA Masato Kumamoto University, Graduate School of Science and Technology, Assistant Professor (70264207)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥4,120,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥420,000)
Fiscal Year 2007: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2006: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | nanomaterial / nanotube / catalys is / self-assembly / biomaterial / enzyme / sensor / electrode / 自分組織化 / フェリチン / タンパク質 / ナノ粒子 / カーボンナノチューブ / 触媒 |
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| Research Abstract |
Carbon nanotubes(CNTs)was synthesized on a platinum plate(99.98 %, 20×20×1 mm)by the chemical vapor deposition(CVD)method using iron nanoparticles derived from ferritin molecules. The synthesized CNTs were characterized by Raman spectroscopy and TEM. Two Raman shift peaks corresponding to G-(ca. 1580 cm^<-1>)and D-bands(ca. 1350 cm^<-1>)were observed on the platinum electrode surface after the synthesis of the CNTs, which indicated that CNTs were present on the electrode surface. The diameters of individual CNTs were evaluated to be ca. 5 to 10 nm, which could be classified as multi-walled CNTs(MWCNTs).
The MWCNTs synthesized on the Pt plate (MWCNTs/Pt)electrode were immediately immersed into solutions of glucose oxidase (GOX)to immobilize these enzymes onto the MWCNTs/Pt electrode surfaces. After the GOX was immobilized onto the MWCNTs/Pt electrode, a well-defined catalytic oxidation current was increased from ca. -0.45 V (vs. Ag/AgCl/sat'd KCl), which was close to the redox potential of flavin adenine dinucleotide (FAD)as a prosthetic group of GOX under physiological pH values. Also, fructose dehydrogenase (FDH)immobilized MWCNTs/Pt electrode showed a well-defined catalytic oxidation current based on FDH was observed from ca. -0.15 V (vs. Ag/AgCl/sat'd KCl), which was close to the redox potential of heme c as a prosthetic group of FDH. From an analysis of a plot of the catalytic current vs. substrate, the calibration range for the fructose concentration was up to ca. 40μmol dm^<-3>, and the apparent Michaelis-Menten constant was evaluated to be 11 (±)mmol dm^<-3>
Further investigations concerning both the interactions between enzymes and MWCNTs and direct heterogeneous electron transfer reactions are underway to develop sensor applications and glucose-oxygen biofuel cells.
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