Immobilization xanthine oxidase on interdigitated electrode for biosensor investigation

Abstract

Biosensors can be developed using different biological materials and immobilization technologies. Interest in immobilization techniques has increased because they allow for the improvement of some stability characteristics of enzymes. The high stability of immobilization enzymes for a substrate can make them ideal alternatives as recognition elements for sensors. Purified xanthine oxidase from milk biosensor was constructed in a very simple way. Xanthine oxidase was purified from bovine milk using ammonium sulfate precipitation and affinity chromatography on Sepharose-4B-L-tyrosine- 4-aminobenzamide dihydrochloride. Xanthine oxidase was immobilized on 3-amino propyl triethoxy silane linking with cysteine on an interdigitated electrode surface. This study will be a novel biosensor for based on measurements of pollutants in the water. The enzyme based biosensor film was tested against copper sulfate (CuSO4) as a pollutant. The measurement was performed by electrical characterization before and after the exposure of CuSO4. Interdigitated gold electrode coated glass substrates were used and I-V graphs were recorded between +/- 4V. The current change depending on the biosensor film environment gives remarkable information about the sensor study.