Amperometric enzyme electrodes

Albery, W. John; Bartlett, Philip N.; Driscoll, Bryan J.; Lennox, R. Bruce

doi:10.1016/0022-0728(92)80004-n

Cited by 51 publications

(16 citation statements)

References 13 publications

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“…Unlike the models based on Albery et al [5], the steady state analytical model of Sorochinskii and Kurganov [22] incorporated concentration polarization. This model considered the possibility of enzyme reversibility (i.e.…”

Section: The Influence Of Concentration Polarization In the Immobilizmentioning

confidence: 99%

“…Although such systems have sometimes claimed the biosensor title, their applicability would seem relatively low, since either the shelf life would be unremarkable, or else its need for 'on-site' assembly would demand an expert user. Albery et al [5] described an analytical model for homogeneous mediation of an enzyme, where seven separate cases were described, two of which involve the mediator as part of the electrode, as in conducting salt electrodes, and in the other five the mediator is provided from bulk solution. It was shown that steady state was reached when the mediator was in excess (i.e.…”

Section: Homogeneous Solutionmentioning

confidence: 99%

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Redox enzyme linked electrochemical sensors: Theory meets practice

1995

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Abstract.Information from theoretical models of redox enzyme linked biosensors highlights the importance of membrane thickness and enzyme loading on signal response in regard to both sensitivity and reproducibility. The conclusions are substantiated by examination of practical examples in the literature and, with a view to the importance of the character of the enzyme layer and overlayers, immobilization techniques are assessed which are in current use.

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Section: The Influence Of Concentration Polarization In the Immobilizmentioning

confidence: 99%

Section: Homogeneous Solutionmentioning

confidence: 99%

Redox enzyme linked electrochemical sensors: Theory meets practice

1995

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“…This linear relationship between I and the scan rate indicates that there is no diffusion limitation and that redox processes are controlled by the electron transfer of the adsorbed species at the electrode surface [40,41]. From the slope of the I vs. ν graph the total surface coverage Γ could be calculated.…”

Section: Influence Of Scan Rate In Biosensors Responsementioning

confidence: 99%

Advantages of the Biomimetic Nanostructured Films as an Immobilization Method vs. the Carbon Paste Classical Method

et al. 2012

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Tyrosinase-based biosensors containing a phthalocyanine as electron mediator have been prepared by two different methods. In the first approach, the enzyme and the electron mediator have been immobilized in carbon paste electrodes. In the second method, they have been introduced in an arachidic acid Langmuir-Blodgett nanostructured film that provides a biomimetic environment. The sensing properties of non-nanostructured and nanostructured biosensors towards catechol, catechin and phenol have been analyzed and compared. The enzyme retains the biocatalytic properties in both matrixes. However, the nanostructured biomimetic films show higher values of maximum reaction rates and lowest apparent Michaelis-Menten constants. In both types of sensors, the sensitivity follows the decreasing order catechol > catechin > phenol. The detection limits observed are in the range of 1.8-5.4 μM for Langmuir-Blodgett biosensors and 8.19-8.57 μM for carbon paste biosensors. In summary, it has been demonstrated that the Langmuir-Blodgett films provide a biomimetic environment and nanostructured biosensors show better performances in terms of kinetic, detection limit and stability. OPEN ACCESSCatalysts 2012, 2 518

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“…The treatment is originally given by Albery et al [26] and the model has been reviewed by Bartlett and Pratt [27]; it represents one of the most generally used theoretical approaches to analyze experimental voltammetric data for the homogeneous system in order to extract the relevant kinetic constants for the considered reactions. Briefly, according to the steady state approach for solving the enzyme kinetic, the rate of reaction catalyzed by peroxidase (E) in presence of substrate (S) and a mediator (M) can be expressed by [28,29]:…”

Section: Mediated Electron Transfer Characterizationmentioning

confidence: 99%

Bioelectrochemical Characterization of Horseradish and Soybean Peroxidases

Frasconi¹,

Favero²,

Tortolini³

et al. 2009

Electroanalysis

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Heme peroxidase are ubiquitous enzymes catalyzing the oxidation of a broad range of substrates by hydrogen peroxide. In this paper the bioelectrochemical characterization of horseradish peroxidase (HRP) and soybean peroxidase (SBP), belonging to class III of the plant peroxidase superfamily, was studied. The homogeneous reactions between peroxidases and some common redox mediators in the presence of hydrogen peroxide have been carried out by cyclic voltammetry. The electrochemical characterization of the reactions involving enzyme, substrate and mediators concentrations allowed us to calculate the kinetic parameters for the substrate-enzyme reaction (K(MS)) and for the redox mediator-enzyme reaction (K(MM)). A full characterization of the direct electron transfer kinetic parameters between the electrode and enzyme active site was also performed by opportunely modeling data obtained from cyclic voltammetry and square wave voltammetry experiments. The experimental data obtained with immobilized peroxidases show enhanced direct electron transfer and excellent electrocatalytical performance for H(2)O(2). Despite the structural similarities and common catalytic cycle, HRP and SBP exhibit differences in their substrate affinity and catalytic efficiency. Basing on our results, it can be concluded that peroxidase from soybean represents an interesting alternative to the classical and largely employed one obtained from horseradish as biorecognition element of electrochemical mediated biosensors

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Amperometric enzyme electrodes

Cited by 51 publications

References 13 publications

Redox enzyme linked electrochemical sensors: Theory meets practice

Redox enzyme linked electrochemical sensors: Theory meets practice

Advantages of the Biomimetic Nanostructured Films as an Immobilization Method vs. the Carbon Paste Classical Method

Bioelectrochemical Characterization of Horseradish and Soybean Peroxidases

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