Abstract
Biosensors are analytical devices which incorporate a biologically active component, often an enzyme covalently attached to an electrode surface, and are normally used for the measurement of a single analyte at a given time. Attempts were therefore made to develop a flexible biosensor which enables the measurement of different substrates. In this article we describe a new immobilization system where enzymes like glucose oxidase, invertase and peroxidase were bound to chelating sepharose through different metal ions and the lectin concanavalin A in a way which permits elution and reloading of these enzymes in the conditions irrespective of each other. The thermal stability of the glucose oxidase preparation obtained by immobilization on different metal ions was also studied. After the performance of an experiment, the gels can easily be regenerated and reloaded with the same or different metal ions for an ensuing experiment. Thus this technique with selective removal and new immobilization of the enzymes can also be a useful tool in the field of biosensors.