Theory of Catalytic Current at the Biocatalyst Electrode with Entrapped Mediator

Ikeda, Tokuji; Miki, Koujiro; Senda, Mitsugi

doi:10.2116/analsci.4.133

Cited by 40 publications

(16 citation statements)

References 16 publications

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“…A number of sophisticated mathematical models of the behavior of enzymes immobilized in surface layers have been described [20,[53][54][55][56]. These complex analyses are often needed to understand and optimize the behavior of thick and/or conducting films [57], and have been used, for example, to determine the site of H 2 O 2 oxidation in polypyrrole-based biosensors [39].…”

Section: Resultsmentioning

confidence: 99%

Design variations of a polymer–enzyme composite biosensor for glucose: Enhanced analyte sensitivity without increased oxygen dependence

McMahon

Killoran

O’Neill

2005

Journal of Electroanalytical Chemistry

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Section: Resultsmentioning

confidence: 99%

Design variations of a polymer–enzyme composite biosensor for glucose: Enhanced analyte sensitivity without increased oxygen dependence

McMahon

Killoran

O’Neill

2005

Journal of Electroanalytical Chemistry

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“…The Is value measured at -0.2 V increased linearly with increasing cI,, up to 0.5 mM, at which concentration a downward deviation was appreciable, as in the case of Figure 6. In the NOD electrode with a large amount of NOD, the effect of the diffusional process of the substrate in the enzyme layer and the membrane layer is expected to be significant, which leads to an extended linear range [15][16][17]. The response time of the electrode was 30 s, which was somewhat longer than that of the NOD electrode used in the previous section ( Figure 4).…”

Section: A Film-nod-cp(q)e As An Amperometricmentioning

confidence: 85%

“…Thus, theories of bioelectrocatalysis [15][16][17] and polarographic catalytic current [18][19][20] can be used to elucidate the experimental data, which predict a saturation tendency of the catalytic current with increasing concentration of the mediator as is observed in Figure 3. When the reaction between BQH, and ES, is the rate-determining step of reaction 2 , that is, when cw.…”

Section: Results and Discusson Eleclrocbemical Redm Reaction Of Bq Inmentioning

confidence: 99%

Nucleoside oxidase‐modified carbon paste electrode containing quinone: Cathodic current response to nucleosides

et al. 1991

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The cathodic current for the reduction of benzoquinone at a glassy carbon electrode was increased in the presence of nucleoside oxidase and inosine. This was attributed to the regeneration of benzoquinone from hydroquinone by the laccaselike reaction of the enzyme, the rate of which depended on the concentration of inosine in the solution. Accordingly, an enzyme electrode for nucleosides was constructed by immobilizing nucleoside oxidase behind a dialysis membrane on a carbon paste electrode containing p-benzoquinone or hydroquinone. The current response of the electrode to nucleosides was studied, and the results were discussed on the basis of the laccaselike activity of the enzyme. The nucleoside oxidase-modified electrode was tested as an amperometric enzyme electrode for nucleosides and could be used at least for three weeks.k7W WORDS: Biosensors, nucleosides, nucleoside oxidase. A"TR0DUCTIONConsiderable attention has been given to the coupling of electrode reaction with an enzymatic reaction, in which the substrate of the enzyme can be oxidized or reduced electroenzymatically, i.e., by bioelectrocatalysis [ 1-31. Molecules serving as redox mediators are usually used to achieve the electron transfer coupling, and enzyme electrodes relying on this principle of current response, mediated amperometric enzyme electrodes, have been constructed (4, 51. A variety of redox molecules including redox polymers have been studied for the mediated electron transfer coupling based on glucose oxidase and other oxidoreductases [ 1-31. Similar coupling without mediators has also been reported between ordinary electrodes (such as carbon and metal surfaces), and several kinds of oxidoreductases [ 6-91.This article describes a new type of electroenzymatic coupling different from the above two coupling schemes, which rely on the unique properties of the enzyme used: nucleoside oxidase [NOD] from Pseudomom maltophiria LB-86 (10-131. NOD has a molecular weight of 'To whom correspondence should be addressed. 8 1992 VCH Publishers, Inc. 1040-0397/92/$3.50 + .25 891 892 Ikeda et al.

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“…In any case, noting that tanh σ ≈ 1 when σ > 2, Eq. (1) in the present case is simplified to 18,20 Thus, the same expression as that of BOD in solution,…”

Section: Theoretical Considerationsmentioning

confidence: 99%

Measurements of Reversible and Irreversible Inactivation Processes of a Redox Enzyme, Bilirubin Oxidase, by Electrochemical Methods Based on Bioelectrocatalysis

Ikeda

Uematsu

et al. 2009

ANAL. SCI.

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The inactivation of a redox enzyme, bilirubin oxidase (BOD), by heat and guanidine hydrochloride (GuHCl) was studied by two bioelectrochemical methods. One is a conventional method, which measures the inactivation of BOD in solution, and the other is a method using a BOD-immobilized electrode (a membrane/BOD/GC electrode), which measures the inactivation of BOD in the immobilized state. The results for thermal inactivation revealed that BOD both in solution and in the immobilized state obeyed the same irreversible inactivation kinetics. The CD and absorption spectra of BOD confirmed that the irreversible thermal inactivation was accompanied by a change in the secondary structure and the dissociation of type-1 copper from BOD. The measurements in the presence of GuHCl demonstrated that the BOD activity was significantly decreased at 1 M GuHCl in both states, and that the decrease proceeded reversibly. The CD spectrum of BOD indicated that the secondary structure of BOD was little affected by GuHCl at this concentration. The effect of GuHCl on the thermal inactivation was studied and evaluated as the resulting values of the Arrhenius activation energy: ΔG ≠ , ΔH ≠ , and ΔS ≠ .

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Theory of Catalytic Current at the Biocatalyst Electrode with Entrapped Mediator

Cited by 40 publications

References 16 publications

Design variations of a polymer–enzyme composite biosensor for glucose: Enhanced analyte sensitivity without increased oxygen dependence

Design variations of a polymer–enzyme composite biosensor for glucose: Enhanced analyte sensitivity without increased oxygen dependence

Nucleoside oxidase‐modified carbon paste electrode containing quinone: Cathodic current response to nucleosides

Measurements of Reversible and Irreversible Inactivation Processes of a Redox Enzyme, Bilirubin Oxidase, by Electrochemical Methods Based on Bioelectrocatalysis

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