Jung Soo-Keun Chae, YR Yoon, JM Cho, BW Ryu, KG 2024-01-21T05:12:02Z 2024-01-21T05:12:02Z 2021-09-03 2005-04 1017-7825 https://pubs.kist.re.kr/handle/201004/136619 Glucose oxidase was immobilized on the carboxylated multi-wall carbon nanotubes (MWNT-COOHs) in the presence of a coulping reagent, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide. Significant amounts of glucose oxidase were also immobilized on MWNT-COOHs without the coupling reagent. Various conditions for the immobilization of glucose oxidase were optimized. Optimal pH for the maximal activity of the immobilized glucose oxidase shifted to 7 from the optimal pH of 6 for the maximal activity of free enzyme due to the carboxyl groups on the surface of MWNT-COOHs. An electrode of graphite rod with a diameter of 6 mm was fabricated using the immobilized glucose oxidase. The cyclic voltammetry study of the enzyme electrode revealed that the oxidation of glucose and subsequent transfer of electrons from the oxidation of glucose to the electrode were possible by the immobilized glucose oxidase without a mediator, implying that the enzyme electrode can be utilized for the development of biofuel cells. English KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY CATHODE CATALYSTS PEROXIDE PROTEINS Immobilization of glucose oxidase on multi-wall carbon nanotubes for biofuel cell applications Article 1 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.15, no.2, pp.234 - 238 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY 15 2 234 238 scie scopus kci ART001100418 000228813800002 2-s2.0-18144370851 Biotechnology & Applied Microbiology Microbiology Biotechnology & Applied Microbiology Microbiology Article CATHODE CATALYSTS PEROXIDE PROTEINS carbon nanotubes glucose oxidase immobilization