Elsevier

Synthetic Metals

Volume 92, Issue 2, 30 January 1998, Pages 173-178
Synthetic Metals

Electrochemical synthesis of polypyrrole for the immobilization of galactose oxidase

https://doi.org/10.1016/S0379-6779(98)80108-2Get rights and content

Abstract

Based on the results of the atomic force microscopy (AFM) experiment, the images of the polypyrrole films are modified, which are dependent on the composition of the pyrrole solution for electrolysis and the method of electrolysis. Only one kind of polypyrrole film, which is synthesized using repeated potential cycling in the solution consisting of 0.1 M pyrrole and 1 M NaCl with pH 2, can be used for the immobilization of galactose oxidase. The Raman spectra of the polypyrrole galactose oxidase electrode show a characteristic peak of the amino acid, which is evidence for galactose oxidase immobilized in the polypyrrole film. The enzyme electrode has a bioelectrochemical response to galactose; its response current increases linearly with increasing concentration of galactose in the range below 2 mM. Thus, this enzyme electrode can be used to determine galactose concentration.

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Cited by (22)

  • A novel amperometric galactose biosensor based on galactose oxidase-poly(N-glycidylpyrrole-co-pyrrole)

    2011, Synthetic Metals
    Citation Excerpt :

    A combination of the immobilized enzyme and electrochemical method provides a fast and reliable method to study the enzyme-catalyzed reaction kinetics and determine the substrate concentration. Galactose oxidase is the most commonly used enzyme for galactose determinations [4,7,8]. Various amperometric biosensors containing the immobilized galactose oxidase have been reported to use for the galactose detection [9–11].

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