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

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.

Automated summary

By immobilizing a thermostable blue multicopper oxidase from hyperthermophilic archaeon Pyrobaculum aerophilum onto a single-walled carbon nanotube electrode, high electrochemical catalytic activity was achieved. Results from electrochemical investigation and spectroscopic measurements suggested a structural transition around 40?C.