pH-metric detection of alkaline phosphatase activity as a novel biosensing platform

A detection of alkaline phosphatase (ALP, EC 3.1.3.1) activity by the monitoring of pH changes caused by the biocatalytic action of the enzyme has been experimentally examined. Enzymatically catalyzed hydrolysis of monofluorophosphate has been found to be the best basis for such measurements. Protolytic equilibria connected with the developed biosensing system were recognized and the optimal conditions for the assay have been found. Advantages and disadvantages of the developed (bio)sensing scheme have been discussed. The prototype of pH-ALP based enzyme electrode has been demonstrated. Potential utility of such substrate-enzyme-sensor system for the development of a new group of biosensors has been announced.