The pH is one of the most important parameters for char-acterizing the chemical properties of an aqueous solution. The glass eiectrode is by far the most commonly used pH sensor. The determination of pH in special situations, e.g., in vivo applications where the fragility of the glass electrode is a draw-back, requires pH sensors that can easily be miniaturized and built into physically rugged sleeves. Also, for other applications where the volume of solution is very restricted miniaturization of pH sensors is very important. The glass electrode does not respond properly to pH in some corrosive environments (e.g., in hydrogen fluoride [HF] solutions). At present, among alternatives to the hydrogen-selective glass electrode group of sensors, potentiometric metal-metal oxide pH sensors respond to pH, ideally due to an equilibrium involving the metal and its oxide. In the case of metal oxide electrodes, the metal is not involved in the potential-determining reaction. This distinction is of course not clear in many cases because the mechanism giving the pH response is not always unequivocal.
Optical biosensing schemes based on enzymatically modified inorganic/organic transparent films predominately composed of Prussian Blue are demonstrated. The composite film, which is non-electrochemically deposited on a non-conducting support. is used as an optical transducer for flow-through biosensors based on hydrolases and oxidases. Urease and glucose oxidase are utilized as model enzymes. Action of the urea biosensor is based on optical pH sensitivity of Prussian Blue indicator. The glucose biosensor is acting as first-generation optical biosensor based on in situ generated Prussian White transducer for hydrogen peroxide. These simple, single-pass transmission optical biosensors exhibit sensitivity in the millimolar range of concentration. The biosensors are very stable owing to presence of a poly(pyrrolylbenzoic acid) network in the composite material. This organic polymer plays a dual role as a binding agent for inorganic material and as a functionalized support for strong covalent immobilization of enzyme molecules.
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