Regensburg 2007 – scientific programme

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HL: Fachverband Halbleiterphysik

HL 42: GaN: devices

HL 42.3: Talk

Thursday, March 29, 2007, 14:30–14:45, H13

Characterization of AlGaN/GaN Enzyme Modified Field Effect Transistors — •Barbara Baur, John Howgate, Vedran Bandalo, Wiebke Steins, Martin Stutzmann, and Martin Eickhoff — Walter Schottky Institut, Technische Universität München, 85748 Garching, Germany

Enzyme-modified field-effect transistors (EnFETs) were prepared by immobilisation of penicillinase on AlGaN/GaN solution gate field-effect transistors. The stability of the transistor during operation in a liquid environment and the influence of the immobilisation process on enzyme functionality have been investigated by a direct comparison of covalent immobilization and physisorption. Covalent immobilization by Schiff base formation on GaN surfaces modified with an aminopropyltriethoxysilane monolayer exhibits a high reproducibility with respect to the enzyme/substrate affinity. The stability of the enzyme layer is shown to be significantly increased by reductive amination of the Schiff base bonds to secondary amines.