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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 37 (1991), S. 854-858 
    ISSN: 0006-3592
    Keywords: Polypyrrole ; glucose oxidase ; immobilization ; autoinactivation ; thermodesactivation ; stability ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article reports the characterization of the biochemical behavior of glucose oxidase entrapped in polypyrrole. The immobilization of glucose oxidase in a polypyrrole film was performed by entrapment during the electropolymerization of pyrrole at a platinum electrode poised at 0.65 V vs. SCE in aqueous solution in a one-compartment electrochemical cell. Thin films of polypyrrole (0.11 μm) were obtained and the entrapped enzyme obeyed Michaelis kinetics, indicating no diffusional constraints of the substrate. Our results indicate that the entrapped glucose oxidase is more resistant to denaturation conditions such as alkaline pH and temperature (50 and 60°C) than the soluble form of the enzyme. The autoinactivation constant for the entrapped enzyme was also determined in presence of 0.25M of glucose and was 6.19 × 10-4 min-1, i.e., corresponding to a half-life value of 20 h. The results reported here show clearly that polypyrrole matrix has a strong stabilizing effect on the stucture and on the activity of glucose oxidase.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1040-0397
    Keywords: Glucose ; biosensor ; Nafion ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A novel glucose biosensor has been prepared by deposition of a mixture containing glucose oxidase dissolved in water and Nafion dissolved in methanol at the surface of a platinum disk electrode. Glucose concentration is evaiuated by measuring the amperometric current corresponding to hydrogen peroxide electrooxidation at 0.7 V vs. SCE. The addition of glucose oxidase to Nafion resulted in a Nafion-glucose oxidase film that was more permeable to anionic species than Nafion alone. The calibration curve for glucose is linear from 5 μM up to about 10 mM. In oxygen-saturated solution, the linear range extended to 15 mM. The optimum pH for the assay was found to be 5.5. The enzyme is not stabilized against temperature deactivation when it is immobilized in Nafion. The Pt/Nafion-glucose oxidase electrodes showed good stability when stored dry at room temperature with 80% of the initial response retained after 250 days.
    Additional Material: 7 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electroanalysis 4 (1992), S. 933-940 
    ISSN: 1040-0397
    Keywords: Glucose biosensor ; Polpyrrole ; Rotating ring-disk electrode ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A rotating ring-disk electrode, (RRDE) of which the platinum disk was coated with a polypyrrole-glucose oxidase (PPy-GOD) film by electrochemical polymerization and the ring was left bare, has been used to characterize the PPy-GOD electrode. Polypyrrole-GOD films of various thicknesses grown in the presence of 100 and 500 U/ml of GOD in the deposition solution were used. The amperometric current generated at 0.7 V versus saturated calomel electrode (SCE) by the electrochemical oxidation of hydrogen peroxide, generated by the enzymatic reaction, has been evaluated at both the coated disk and uncoated ring at various rotation speeds. The collection efficiency of the RRDE was 22% and was used to evaluate the total current of the PPy-GOD electrode. The total current of a polypyrrole electrode was defined as the sum of the disk current and the total ring current taken as the observed ring current divided by the collection efficiency of the RRDE. From this study, it clearly appears that the biotransformation of glucose takes place mainly at the polypyrrole film/solution interface independently of the rotation speed and that the catalysis is not limited by oxygen. The Eadie-Hofstee type plots obtained for disk current with 10-225 mM of glucose show a strong positive deviation for glucose concentrations higher than 100 mM. On the other hand, linear plots are obtained when the total current of the enzyme electrode is considered. No definitive explanation can be given for these behaviors, except that at a higher glucose concentration, the flux of glucose is high enough to permit the diffusion of glucose deeper in the film, where it can be oxidized by the enzyme. Thus, the catalytic reaction is taking place in a thicker layer of the film.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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