Temperature depending bioelectrocatalysis current of multicopper oxidase from a hyperthermophilic archaeon Pyrobaculum aerophilum
Temperature depending bioelectrocatalysis current of multicopper oxidase from a hyperthermophilic archaeon Pyrobaculum aerophilum
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DOI：
10.1016/j.elecom.2021.106982
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发表时间：
2021-02
影响因子：
5.4
通讯作者：
M. Tominaga;Shinobu Nakao;M. Takafuji;E. Takamura;S. Suye;T. Satomura
中科院分区：
文献类型：
--
作者：
M. Tominaga;Shinobu Nakao;M. Takafuji;E. Takamura;S. Suye;T. Satomura
耐热蓝色多铜氧化酶在高温下是稳定的，然而，由于这种结构稳定性，这种酶具有低活性。在这项研究中，实现了高的电化学催化活性，通过固定的热稳定性蓝色多铜氧化酶从超嗜热古菌Pyrobaculum aerophilum（McoP）到单壁碳纳米管（SWCNT）电极。电化学研究结果表明，在40 °C左右，单壁碳纳米管固定化的McoP发生了结构转变，而McoP溶液的光谱测量结果表明，在40 °C左右发生了结构转变。
The thermostable blue multicopper oxidase is stable at high temperature, however, because of this structural stability this enzyme has low activity. In this study, high electrochemical catalytic activity was achieved by immobilizing a thermostable blue multicopper oxidase from hyperthermophilic archaeonPyrobaculum aerophilum(McoP) onto a single-walled carbon nanotube (SWCNT) electrode. The both results of electrochemical investigation for the McoP immobilized the SWCNT and spectroscopic measurements for the McoP solution suggested that a structural transition occured around 40 °C.