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Mesoporous Materials Promoting Direct Electrochemistry and Electrocatalysis of Horseradish Peroxidase
Author(s) -
Dai Zhihui,
Ju Huangxian,
Chen Hongyuan
Publication year - 2005
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.200403163
Subject(s) - horseradish peroxidase , mesoporous material , electrocatalyst , electron transfer , electrochemistry , chemistry , glassy carbon , fourier transform infrared spectroscopy , chemical engineering , inorganic chemistry , electrode , nuclear chemistry , cyclic voltammetry , catalysis , organic chemistry , engineering , enzyme
The direct electron transfer and electrocatalysis of horseradish peroxidase (HRP) immobilized on hexagonal mesoporous silicas (HMS) matrix was studied. The interaction between HRP and HMS was examined by using Fourier transform infrared spectroscopy, nitrogen adsorption isotherms and electrochemical methods. The immobilized HRP at a modified glassy carbon electrode showed a good direct electrochemical behavior, which depended on the specific properties of the HMS. Two couples of redox peaks corresponding to Fe(III) to Fe(II) conversion of the HRP intercalated in the mesopores and adsorbed on the external surface of the HMS were observed with the formal potentials of −0.315 and −0.161 V in 0.1 M pH 7.0 PBS, respectively. The amount of HRP intercalated in the mesopores of HMS proved to be related to the pore size. The HRP intercalated in the mesopores showed a surface controlled electrode process with a single proton transfer. The immobilized HRP displayed an excellent electrocatalytic response to the reduction of hydrogen peroxide (H 2 O 2 ) without the aid of an electron mediator. The HMS provided a novel matrix for protein immobilization and direct electron transfer study of the immobilized protein.

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