Catalytic activity of enzymes immobilized on AlGaN/GaN solution gate field-effect transistors

被引:54
作者
Baur, B. [1 ]
Howgate, J. [1 ]
von Ribbeck, H. -G. [1 ]
Gawlina, Y. [1 ]
Bandalo, V. [1 ]
Steinhoff, G. [1 ]
Stutzmann, M. [1 ]
Eickhoff, M. [1 ]
机构
[1] Tech Univ Munich, Walter Schottky Inst, D-85748 Garching, Germany
关键词
D O I
10.1063/1.2369534
中图分类号
O59 [应用物理学];
学科分类号
摘要
Enzyme-modified field-effect transistors (EnFETs) were prepared by immobilization of penicillinase on AlGaN/GaN solution gate field-effect transistors. The influence of the immobilization process on enzyme functionality was analyzed by comparing covalent immobilization and physisorption. Covalent immobilization by Schiff base formation on GaN surfaces modified with an aminopropyltriethoxysilane monolayer exhibits high reproducibility with respect to the enzyme/substrate affinity. Reductive amination of the Schiff base bonds to secondary amines significantly increases the stability of the enzyme layer. Electronic characterization of the EnFET response to penicillin G indicates that covalent immobilization leads to the formation of an enzyme (sub)monolayer. (c) 2006 American Institute of Physics.
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页数:3
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