Lee Yoon-Mee, Kwon O-Yul, Yoon Yeo-Joon, Ryu Keungarp
School of Chemical Engineering and Bioengineering, University of Ulsan, 680-749, Ulsan, Korea.
Biotechnol Lett. 2006 Jan;28(1):39-43. doi: 10.1007/s10529-005-9685-8.
Horseradish peroxidase (HRP) was immobilized on carboxylated multi-wall carbon nanotubes in the presence of a coupling reagent, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide. The immobilized HRP maintained its oxidative activity for guaiacol over a broad range of pH values (4-9). An electrode of graphite rod, 6 mm diam. was fabricated using the immobilized HRP. Cyclic voltammetry of the enzyme electrode confirmed electron transfer between the immobilized HRP and the electrode in the presence of H2O2 but without an added mediator or a reducing substrate.
在偶联剂1-乙基-3-(3-二甲基氨基丙基)碳二亚胺存在的情况下，辣根过氧化物酶(HRP)被固定在羧基化多壁碳纳米管上。固定化的HRP在很宽的pH值范围(4-9)内保持其对愈创木酚的氧化活性。使用固定化的HRP制备了直径为6 mm的石墨棒电极。酶电极的循环伏安法证实，在存在H2O2但未添加介质或还原底物的情况下，固定化的HRP与电极之间发生了电子转移。
