Abstract
An amperometric biosensor for the determination of hydrazine compounds, based on their inhibitory effect on the activity of immobilized tyrosinase, has been developed. The hydrazine-tyrosinase interaction can be modeled as a reversible competitive inhibition. Kinetic parameters (K{sub i} and I{sub 0.5}) have been determined for various hydrazine compounds. The tyrosinase-based carbon paste electrode offers sensitive measurements to the low-micromolar level and good precision. The trend in sensitivity, methylhydrazine > hydrazine >dimethylhydrazine, reflects the degree of inhibition. The applicability to assays of unaltered river and drinking water samples is illustrated. Analogous measurements at disposable thick-film sensors are also reported. These inhibitor biosensors hold great promise for field-based monitoring of various hydrazines. 13 refs., 5 figs.
Published Version
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