Direct electrochemistry and electrocatalysis of myoglobin covalently immobilized in mesopores cellular foams

Myoglobin (Mb) was firstly covalently immobilized into mesopores cellular foams (MCFs) to fabricate the protein electrode (Mb–MCFs/GC electrode) and study the direct electrochemistry of redox protein. The results of UV–vis and FTIR spectra illustrated that the covalently immobilized Mb well retained its native structure and presented good stability. Cyclic voltammetry of Mb–MCFs/GC electrode showed nearly reversible cyclic voltammetric peaks, indicating the direct electron transfer of Mb–FeIII/FeII. In addition, Mb–MCFs/GC electrode exhibited favorable electrocatalytic reduction to H2O2 with high sensitivity, good thermal and long-time stability. Such an avenue, which integrated mesopores cellular foams and redox protein via a simple covalent method, may provide a novel and efficient platform for the fabrication of the third generation biosensor.