Direct electrochemistry of membrane-entrapped horseradish peroxidase.

Ferri, Tommaso; Poscia, Alessandro; Santucci, Roberto

doi:10.1016/s0302-4598(98)00102-0

Cited by 103 publications

(69 citation statements)

References 16 publications

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“…In the inset, the linear dependence of peak current intensities vs. scan rate, indicating the absence of diffusion. in the direct electron transfer mechanism of the selected peroxidases, as already reported in literature [9,24].…”

Section: Direct Electron Transfer Characterizationsupporting

confidence: 55%

“…Prior the enzymatic immobilization, the PG electrode surface was polished with 1 mm alumina and then sonicated thoroughly to remove the alumina; the electroactive area (A ¼ 0.12 AE 0.20 cm 2 ) was determined using the Randles -Sevčik equation [25] from cyclic voltammograms of ferricyanide ion, whose diffusion coefficient is known. Then the physical immobilization was obtained by means of a reticulated ion exchange resin (TBMPC) by adding the selected enzyme (0.2 mM) to the polymeric solution, spreading 30 mL onto the electrode surface and letting to dry 48 hours at 4 8C before use [24].…”

Section: Electrochemical Measurementsmentioning

confidence: 99%

“…The redox potentials of the peroxidases under study were measured by means of both cyclic and square wave voltammetry. Studies performed on the direct electrochemistry of immobilized peroxidases indicate that they display enhanced direct electron transfer and excellent electrocatalytical performance for their main substrate: H 2 O 2 [13,24]. Moreover, the obtained peroxidase-based enzymatic electrodes could also be tested as hydrogen peroxide transducers, coupling them with glucose oxidase enzyme, for building glucose biosensors.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Direct Electron Transfer Characterizationsupporting

confidence: 55%

Section: Electrochemical Measurementsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Bioelectrochemical Characterization of Horseradish and Soybean Peroxidases

Frasconi¹,

Favero²,

Tortolini³

et al. 2009

Electroanalysis

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“…Thus, the presence of colloidal gold played an important role in accelerating the electron transfer between HRP and the electrode. The formal potential of the Fe III/II couple in HRP-Au-SPCE calculated from the average of anodic and cathodic peak potentials at pH 7.0 was -338±3 mV (vs. SCE) at 50 mV s -1 , which was closer to -0.22 V of native HRP in solution [26] than the formal potential of -0.377 V for the HRP entrapped within a solid matrix at a pyrolytic graphite electrode [27] , and equal to -(0.346 ±0.002) V of our previous results [14], suggesting that the most HRP molecules preserved their native structure after the adsorption procedure. Fig.…”

Section: Electrochemical Properties Of Hrp Immobilized On Colloidal Gmentioning

confidence: 99%

A Novel Hydrogen Peroxide Sensor via the Direct Electrochemistry of Horseradish Peroxidase Immobilized on Colloidal Gold Modified Screen-printed Electrode

Liu

2003

Sensors

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Abstract:The direct electrochemistry of horseradish peroxidase (HRP) immobilized on a colloidal gold modified screen-printed carbon electrode (HRP-Au-SPCE) and its application as a disposable sensor were studied. The immobilized HRP displayed a couple of stable and well-defined redox peaks with a formal potential of -0.338 V (vs. SCE) and a heterogeneous electron transfer rate constant of (0.75±0.04) s -1 in 0.1 M pH 7.0 PBS. It showed a highly thermal stability, fast amperometric response and an electrocatalytic activity to the reduction of hydrogen peroxide (H 2 O 2 ) without the aid of an electron mediator. The biosensor exhibited high sensitivity, good reproducibility, and long-term stability for the determination of H 2 O 2 with a linear range from 0.8 M to 1.0 mM and a detection limit of 0. 4 M at 3σ. The variation coefficients are 2.7 % and 2.3 % for over 10 successive assays at the H 2 O 2 concentrations of 8.0 and 20 M, respectively. The K M app for H 2 O 2 sensor was determined to be 1.3 mM.

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“…The apparent Michaelis-Menten constant (K M app ), a reflection of both the enzymatic affinity and the ratio of microscopic kinetic constants, can be obtained from the electrochemical version of the Linweaver-Burk equation [42]. The K M app value for Mb-Au-CPE was found to be 0.65 AE 0.02 mM at both À 0.380 and À 0.425 V, which was lower than those of 2.28 mM at cyt.c/Au-CPE [24], 3.69 mM at HRP-Au-CPE [25], 5.5 mM for membrane-entrapped HRP [33] and 2.3 mM for HRP/Au colloid self-assemble monolayer electrode [43]. Thus, Mb molecules entrapped in the mixture of Au colloid and carbon paste is of a higher affinity to H 2 O 2 .…”

Section: Electrocatalysis Of Mb Immobilized In Au-cpe Tomentioning

confidence: 99%

Electrocatalysis via Direct Electrochemistry of Myoglobin Immobilized on Colloidal Gold Nanoparticles

Liu

2003

Electroanalysis

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The direct electron transfer between immobilized myoglobin (Mb) and colloidal gold modified carbon paste electrode was studied. The Mb immobilized on the colloidal gold nanoparticles displayed a pair of redox peaks in 0.1 M pH 7.0 PBS with a formal potential of ±(0.108 AE 0.002) V (vs. NHE). The response showed a surface-controlled electrode process with an electron transfer rate constant of (26.7 AE 3.7) s À1 at scan rates from 10 to 100 mV s À1 and a diffusioncontrolled process involving the diffusion of proton at scan rates more than 100 mV s À1 . The immobilized Mb maintained its activity and could electrocatalyze the reduction of both hydrogen peroxide and nitrite. Thus, the novel renewable reagentless sensors for hydrogen peroxide and nitrite were developed, respectively. The activity of Mb with respect to the pseudo peroxidase with a K M app value of 0.65 mM could respond linearly to hydrogen peroxide concentration from 4.6 to 28 mM. The sensor exhibited a fast amperometric response to NO 2 À reduction and reached 93% of steady-state current within 5 s. The linear range for NO 2 À determination was from 8.0 to 112 mM with a detection limit of 0.7 mM at 3s.

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Direct electrochemistry of membrane-entrapped horseradish peroxidase.

Cited by 103 publications

References 16 publications

Bioelectrochemical Characterization of Horseradish and Soybean Peroxidases

Bioelectrochemical Characterization of Horseradish and Soybean Peroxidases

A Novel Hydrogen Peroxide Sensor via the Direct Electrochemistry of Horseradish Peroxidase Immobilized on Colloidal Gold Modified Screen-printed Electrode

Electrocatalysis via Direct Electrochemistry of Myoglobin Immobilized on Colloidal Gold Nanoparticles

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