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Temperature depending bioelectrocatalysis current of multicopper oxidase from a hyperthermophilic archaeon Pyrobaculum aerophilum

Abstract 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… Click to show full abstract

Abstract 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 archaeon Pyrobaculum 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.

Keywords: oxidase hyperthermophilic; multicopper oxidase; archaeon pyrobaculum; multicopper; hyperthermophilic archaeon

Journal Title: Electrochemistry Communications
Year Published: 2021

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