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Citation: MA Guo-Xian, ZHONG Qing-Dong, LU Xiong-Gang, LU Tian-Hong. Immobilization and Direct Electrochemistry of Horseradish Peroxidase on Large Cage-Like Mesoporous Silica FDU-12[J]. Acta Physico-Chimica Sinica, ;2009, 25(10): 2061-2067. doi: 10.3866/PKU.WHXB20091037 shu

Immobilization and Direct Electrochemistry of Horseradish Peroxidase on Large Cage-Like Mesoporous Silica FDU-12

1.
School of Materials Science and Engineering, Shanghai University, Shanghai 200072, P. R. China

Received Date: 11 May 2009
Available Online: 10 September 2009

We report on a direct electron transfer and bioelectrocatalysis of horseradish peroxidase (HRP) immobilized in mesoporous silica FDU-12 with three-dimensional (3D) large cages and entrances. UV-Vis spectroscopy, Fourier transform infrared (FTIR) spectroscopy, and impedance spectroscopy were used to prove the interaction between HRP and FDU-12. Results from cyclic voltammetry show that immobilized HRP can under a direct quasi-reversible electrochemical reaction. Its formal potential, E0', is -0.325 V in a phosphate buffer solution (PBS, pH 6.9) and this is almost independent of the scan rate from 40 to 300 mV·s -1. The experimental results also demonstrate that the immobilized HRP retains its bioelectrocatalytic activity for the reduction of H2O2. Furthermore, the electrode can be stored at 4 °C for several weeks without any loss of enzyme activity. Thus, FDU-12 is a novel matrix for realizing a direct electron transfer of various proteins and enzymes and the preparation of electrodes for the third biosensors.
- Horseradish peroxidase,
- FDU-12,
- Direct electrochemisrty,
- Hydrogen peroxide,
- Biosensor
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