Immobilization of horseradish peroxidase on self-assembled (3-mercaptopropyl)trimethoxysilane film: Characterization, direct electrochemistry, redox thermodynamics and biosensing
Immobilization of horseradish peroxidase on self-assembled (3-mercaptopropyl)trimethoxysilane film: Characterization, direct electrochemistry, redox thermodynamics and biosensing
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辣根过氧化物酶在自组装(3-巯基丙基)三甲氧基硅烷膜上的固定化:表征、直接电化学、氧化还原热力学和生物传感
DOI:
10.1016/j.electacta.2008.06.031
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发表时间:
2008-11
影响因子:
6.6
通讯作者:
Hu, Zhichao
中科院分区:
文献类型:
--
作者:
Wu, Fanghua;Jin, Litong;Xian, Yuezhong;Tian, Yuan;Wang, Liwei;Xu, Jingjing;Hu, Zhichao
Highly organized (3-mercaptopropyl)trimethoxysilane (3-MPT) films have been prepared via self-assembled coupled with sol–gel linking technology. Horseradish peroxidase (HRP) is successfully immobilized onto the densely packed three-dimensional (3D) 3-MPT network and the direct electrochemistry of HRP is achieved without any electron mediators or promoters. Redox thermodynamics of HRP on the 3-MPT films, which is obtained from the temperature dependence of the reduction potential, suggests that the positive shift of redox potentials of HRP at the interface of 3-MPT originates from the solvent reorganization effects and conformational change of the polypeptide chain of HRP. Based on the direct electrochemistry and electrocatalytic ability of HRP, a sensitive third-generation amperometric H2O2biosensor is developed with two linear dependence ranges of 5.0×10−7to 1.0×10−4and 1.0×10−4to 2.0×10−2molL−1.
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DOI:
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10.1002/chin.199834325
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