We have developed a strategy to immobilize β-galactosidase as a model enzyme by using polymeric supports having Schiff bases, which were prepared from (aminomethyl)polystyrene and 2-phenlyindole-3-carboxaldehyde by condensation. β-galactosidase was immobilized onto the new polymer supports via covalent bonds. The influence of temperature, pH, reusability, and storage capacity on the free and immobilized β-galactosidase was investigated. Our results indicate that the (aminomethyl)polystyrene with Schiff bases is most suitable for the immobilization of β-galactosidase. These kinds of new supports can be used for the immobilization of β-galactosidase due to their strong storage capacity and reusability.
In this paper, a novel amperometric L-glutamate (Glu) biosensor with immobilization of L-glutamate oxidase (L-GlOx) on polypyrrole-polyvinylsulphonate (PPy-PVS) film has been successfully developed. L-GlOx enzyme was immobilized on PPy-PVS film by cross-linking with glutaraldehyde (GA) and bovine serum albumin (BSA). Determination of Glu was carried out by oxidation of enzymatically produced H2O2 at 0.3 V versus Ag/AgCl. The optimum pH and temperature parameters were found to be 9.0 and 55 °C, respectively. There were three linear parts in the regions between 1.0 × 10(-9) and 1.0 × 10(-8) M (R(2) = 0.847), 5.0 × 10(-8) and 5.0 × 10(-7) M (R(2) = 0.997), 5.0 × 10(-7) and 5.0 × 10(-5) M (R(2) = 0.994). Storage stability, operation stability of the enzyme electrode were also studied.
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