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An amperometric biosensor based on catalase enzyme was developed for the investigation of the effect of calcium ions on the activity of the enzyme. Calcium plays an activator role for the catalase enzyme that catalysis the degradation of hydrogen peroxide to O2 and H2O. Determination method of the effect of calcium ion on the activity of the enzyme was based on the assay of the differences on the responses of the biosensor in the absence and the presence of calcium in the reaction medium. The biosensor had a linear relation to calcium concentrations and good measurement correlation between 0.05 and 15 mM with 3 min response time. PPB-HCl buffer (pH 6.8; 20 mM) and 37oC were obtained as the optimum working conditions. In the application studies, the biosensor was used determination of calcium level of real samples such as cow milk, Aavin (green) and MD water. In the characterization studies of the biosensor some parameters such as reproducibility, substrate specificity, operational and storage stability were carried out. Finally, by using the biosensor developed and enzymatic-spectrophotometric method alcohol concentrations of some alcoholic drinks were determined and results were compared.

iosr journal of pharmacy and biological sciences

Biosensor application of extracellular catalase from Ganoderma lucidum AVK-1 and Acinetobacter calcoaceticus AV-6 and Comparative study of commercial catalase from Bovine liver catalase