1993
DOI: 10.1021/ac00053a007
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Amperometric sensors for peroxide, choline, and acetylcholine based on electron transfer between horseradish peroxidase and a redox polymer

Abstract: Amperometric sensors have been developed for hydrogen peroxide, choline, and acetylcholine by immobilization of horseradish peroxidase, (HRP), choline oxidase, and acetylcholinesterase in a cross-linked redox polymer deposited on glassy carbon electrodes. Peroxide sensors, prepared by immobilization of HRP alone, gave detection limits of 10 nM and a linear response up to ca. 1 mM. Coimmobilization of HRP and glucose oxidase was used to establish the feasibility of highly efficient bienzyme sensors at low subst… Show more

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Cited by 204 publications
(95 citation statements)
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“…Furthermore, though membranes and composites incorporating permselective conducting polymers such as polypyrrole (PPY) have other desirable properties (such as high conductivity and being redox active), it should be noted that coating the biosensor transducer with these polymeric films can lead to longer response times and lower signals due to the added diffusion barrier for both the substrate for the enzyme and the redox active species produced in the enzyme-catalyzed reaction. Co-immobilization of peroxidase with a redox polymer [50], immobilization of ascorbate oxidase [9], and self-referencing [51] have also been utilized as strategies to minimize interference from other electroactive species. On the other hand, performing electrochemical peroxidation, a process that utilizes sacrificial electrodes and stoichiometrically balanced applications of hydrogen peroxide to efficiently destroy interfering species in the aqueous phase, poses a risk of also oxidizing the analyte of interest.…”
Section: Glutamate Oxidase-based Biosensorsmentioning
confidence: 99%
“…Furthermore, though membranes and composites incorporating permselective conducting polymers such as polypyrrole (PPY) have other desirable properties (such as high conductivity and being redox active), it should be noted that coating the biosensor transducer with these polymeric films can lead to longer response times and lower signals due to the added diffusion barrier for both the substrate for the enzyme and the redox active species produced in the enzyme-catalyzed reaction. Co-immobilization of peroxidase with a redox polymer [50], immobilization of ascorbate oxidase [9], and self-referencing [51] have also been utilized as strategies to minimize interference from other electroactive species. On the other hand, performing electrochemical peroxidation, a process that utilizes sacrificial electrodes and stoichiometrically balanced applications of hydrogen peroxide to efficiently destroy interfering species in the aqueous phase, poses a risk of also oxidizing the analyte of interest.…”
Section: Glutamate Oxidase-based Biosensorsmentioning
confidence: 99%
“…In addition, both Os(II) and Os(III) complexes, as monitored by cyclic voltammetry and UV-vis spectrophotometry, have been stable in aqueous solution over a wide pH range (pH 1 -12). 18,27 It has been presented that the redox potential of the couple FAD/FADH2 at 25.0˚C (pH 7.0) is -0.46 V vs. SCE, corresponding to the electrode reaction shown in Eq. (6).…”
Section: Redox Potentials Of Os(iii/ii) Complexesmentioning
confidence: 99%
“…The currently preferred mediators are monomeric ferrocenes, quinones, and osmium bipyridine complexes. All have redox potentials of about 0.3-0.6 V positive with respect to the redox potential of the enzyme [2].…”
Section: Introductionmentioning
confidence: 99%