Immobilization of glucose oxidase with polyurethane on carbon support

Abstract

Glucose oxidase (GOD) has been immobilized by physical entrapment on polyurethane PU-6 matrix. It has been found that the enzyme acquires greater thermal stability on immobilization. Oxygen acts as a co-substrate for the redox reaction. However, maintaining oxygen concentration constant throughout the experiment is a difficult task. To overcome this we have coimmobilized ferrocene, which can act as an electron acceptor. ³¹P NMR results indicate that ferrocene is located in the close proximity of the active site of GOD. Moreover, simultaneous use of mediators such as ferricyanide, phenazine methosulphate or flavine mononucleotide have been found to facilitate electron transfer. Platinum, apart from being an expensive metal, is likely to exhibit adverse toxic effects during prolonged 'in-vivo' applications. Electrodes prepared using carbon in the place of platinum, show comparably good response. This opens a new possibility for making cheaper and biocompatible sensors.