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 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

• Blue multicopper oxidase
• Thermostable
• Oxygen reduction
• Single-walled carbon nanotube (SWCNT)
• Hyperthermophilic archaeon
• Structural transition