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Abstract
The use of covalently bound mushroom polyphenol oxidase (tyrosinase, EC 1.10.3.1) for the determination of μg/mL and ng/mL concentrations of phenol in water samples with use of continuous-flow sample/reagent processing is described. Immobilization on controlled-pore glass, CPG, was accomplished via diazo coupling. Detection was effected with hexacyanoferrate(II) as a redox mediator and was either spectrophotometric or amperometric. the immobilized enzyme preparation was part of an open tubular reactor (CPG thermally embedded on Tygon tubing). the redox mediator was used either in solution or as part of a thin-layer cell and immobilized on poly(4-vinylpyridine) incorporated in a carbon paste electrode. Different spectrophotometric and amperometric strategies are compared and the method is applied to the determination of phenol in water samples and quality control standards.
