Stripping measurements of hydrogen peroxide based on biocatalytic accumulation at mediatorless peroxidase/carbon paste electrodes

Wang, Joseph; Ciszewski, Aleksander; Naser, Najih

doi:10.1002/elan.1140040807

Cited by 35 publications

(19 citation statements)

References 10 publications

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“…[11][12][13] The use of crude extract rather than isolated enzymes represents not only alternative and attractive analytical properties, but also simplicity, stability, longer lifetime, lower cost and reduced co-factor requirements. 19,20,36 Figure 1 shows a scheme of the enzymatic processes between catecholamine (adrenaline or dopamine) and laccase (PPO) of crude extract incorporated into a carbon paste electrode.…”

Section: Principle Of Measurementsmentioning

confidence: 99%

“…10 In addition to purified enzymes, [11][12][13] animal, 14 and vegetable extracts, [15][16][17][18] immobilized on the electrode surface by different methods, have also been employed as catalyst sources in both aqueous and organic solutions. Carbon paste electrodes have been widely used owing to the possibility of immobilizing not only enzymes, but also ligands, redox mediators, biological tissues, to catalyze the oxidation/reduction of compounds involved in enzymatic reaction.…”

Section: Introductionmentioning

confidence: 99%

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Determination of catecholamines in pharmaceutical formulations using a biosensor modified with a crude extract of fungi laccase (Pleurotus ostreatus)

Leite¹,

Fatibello‐Filho²,

Barbosa-Dekker³

2003

J. Braz. Chem. Soc.

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Um biossensor de pasta de carbono modificado com extrato bruto enzimático do fungo Pleurotus ostreatus como fonte de lacase é proposto para a determinação de catecolaminas em formulações farmacêuticas. Essa enzima catalisa a oxidação de adrenalina ou dopamina nas quinonas correspondentes e a corrente obtida na redução eletroquímica de cada um dos produtos é relacionada a concentração dessas catecolaminas em solução da amostra. O efeito da concentração de lacase de 0,29 a 1,8 U/mg de pasta de carbono, do pH de 3,0 a 8,0, da velocidade de varredura de 10 a 40 mV s -1 e amplitudes de pulso de potencial de 10 a 60 mV sobre a resposta voltamétrica de pulso diferencial foi investigado. O desvio padrão relativo foi menor que 1,8% para solução de hidroquinona 2,8 x 10 -4 mol L -1 em pH 7 (n=10). Recuperações variando de 97,3 a 101% para adrenalina e de 95,8 a 102% para dopamina foram obtidas. As curvas analíticas foram lineares no intervalo de concentração de adrenalina de 6,0 x 10 -5 a 7,0 x 10 -4 mol L -1 e de 7,0 x 10 -5 a 4,0 x 10 -4 mol L -1 para dopamina, com limites de detecção de 7,9 x 10 -6 mol L -1 e 9,8 x 10 -6 mol L -1 , respectivamente. Esse biossensor foi empregado para a determinação de adrenalina e dopamina em formulações farmacêuticas. Os resultados obtidos com o biossensor para a determinação dessas catecolaminas em formulações farmacêuticas estão em concordância a um nível de confiança de 95% com o procedimento da Farmacopéia americana.A carbon paste biosensor modified with a crude enzymatic extract of the Pleurotus ostreatus fungi as a laccase source is proposed for catecholamine determination in pharmaceutical formulations. This enzyme catalyzes the oxidation of adrenaline or dopamine in the corresponding quinones and the current obtained in the electrochemical reduction of each of the products is related to the concentration of these catecholamines in the sample solution. The effect of the laccase concentration from 0.29 to 1.8 U/mg of carbon paste, pH from 3.0 to 8.0, scan rate from 10 to 40 mV s -1 and potential pulse amplitude from 10 to 60 mV on the differential pulse voltammetric response was investigated. The relative standard deviation was smaller than 1.8% for a 2.8 x 10 -4 mol L -1 hydroquinone solution at pH 7.0 (n=10). Recoveries varied from 97.3 to 101% for adrenaline and from 95.8 to 102% for dopamine. The analytical curves were rectilinear in the adrenaline concentration range from 6.0 x 10 -5 to 7.0 x 10 -4 mol L -1 and 7.0 x 10 -5 to 4.0 x 10 -4 mol L -1 for dopamine, with detection limits of 7.9 x 10 -6 mol L -1 and 9.8 x 10 -6 mol L -1 , respectively. This biosensor was used for adrenaline and dopamine determinations in pharmaceutical formulations. The results obtained using the proposed biosensor are in close agreement with those obtained using an American Pharmacopoeia procedure at a 95% confidence level. Keywords: laccase, Pleurotus ostreatus, catecholamines, biosensor IntroductionCatecholamines play an important role in the central nervous system as neurotransmitters. They als...

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Section: Principle Of Measurementsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Determination of catecholamines in pharmaceutical formulations using a biosensor modified with a crude extract of fungi laccase (Pleurotus ostreatus)

Leite¹,

Fatibello‐Filho²,

Barbosa-Dekker³

2003

J. Braz. Chem. Soc.

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“…Many methods such as titrimetry, UV-vis spectrophotometry and electrochemistry have been developed for this purpose [1][2][3]. Among these methods, the amperometric biosensors based on the direct electron transfer between an electrode and the immobilized enzyme/protein is especially promising because of its simplicity and high sensitivity [4][5][6][7][8][9][10][11][12][13][14][15][16][17]. Horseradish peroxidase (HRP), a prototypical hemeprotein peroxidase (FW ca.…”

Section: Introductionmentioning

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 recorded current will then be proportional to the glucose concentration in the sample. Previously it has been clearly shown that using polymeric bound mediators and especially polymeric mediators covalently bound with the enzyme is beneficial to obtain stable biosensors [41][42][43][44][45][46][47][48][49][50][51][52][53][54][55][56][57][58][59][60]. However, in the case stipulated in this work when coimmobilising GOD and HRP it has been possible to achieve long term stable sensors.…”

Section: Resultsmentioning

confidence: 99%

“…The synergetIc effect of redox mediators and peroxidase in a bienzymatic biosensor for glucose assays in FIA (HRP) coupled with ferrocene have been reported [48][49][50][51][52][53].…”

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confidence: 99%

The synergetIc effect of redox mediators and peroxidase in a bienzymatic biosensor for glucose assays in FIA

Rondeau

Larsson²,

Boujtita

et al. 1999

Analusis

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Amperometric biosensors based on enzymes are interesting due to their high sensitivity, excellent selectivity, simplicity, low cost and rapid response. The most frequently used enzymatic methods for glucose determination employ glucose oxidase (GOD), due to its high selectivity towards ß-D-glucose. In the presence of GOD, the oxidation of glucose occurs, producing H 2 O 2 . Most commonly, the electrochemical detection is performed through the anodic oxidation of H 2 O 2 [1]. A drawback with this detection technique is that high overvoltages are required, and an applied potential in the range of 0.6-1.1 V vs. Ag/AgCl is necessary. Working at such high potentials increases the risk of interference from easily oxidisable compounds such as ascorbate, ureate, acetaminophen, paracetamol, phenols, etc. which are common compounds in biological samples.A possible way of improving the selectivity of such a biosensor is to couple a second enzyme (peroxidase) to the oxidase, creating a bienzymatic sensor. Peroxidase catalyses the electrochemical reduction of H 2 O 2 produced by GOD through a direct electron transfer reaction at a much lower applied potential compared with electrochemical oxidation of H 2 O 2 and maximum catalytic current can be obtained at carbon electrodes in a potential range of -0.1 and 0 V [2-14]. However, the kinetics of the direct electron transfer from an electrode to the peroxidase is a sluggish process [15][16][17] hence the advantage of using a mediator.The introduction of a mediator in the bienzymatic system (GOD/HRP) leads to an acceleration of the electron transfer, a decrease in the applied working potential (the reduction of the mediator is detected at the electrode) and an increase in sensitivity. The use of mediators is a well-known technique although the way of adding the mediator to the bienzymatic system (oxidase/peroxidase) may vary. A number of different mediators have been used as additions into sample solutions such as, potassium hexacyanoferrate (II) [18][19][20][21][22][23][24] [44,45], and Nafion-Nmethyl phenazinium [46]. The advantages of using the redox polymers are several, but mainly they result in more stable biosensors since leaking of the mediator from the electrode is minimised and higher and faster responses are observed due to the proximity between the enzyme and the mediator. Although, choosing an appropriate bulk matrix and mediator concentration these properties can be achieved with nonpolymeric mediators and recently a ferrocene mediated bienzymatic graphite-Teflon electrode has been developed for batch and flow-injection measurements [47]. On the other hand several biosensors based on monoenzymatic electrodes 649The synergetIc effect of redox mediators and peroxidase in a bienzymatic biosensor for glucose assays in FIA Abstract. A bienzymatic biosensor incorporating a mediator has been developed in order to achieve a fast and selective detection of glucose in a flow injection system. The working electrode is based on a carbon paste matrix bulk modified with glucose ...

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Stripping measurements of hydrogen peroxide based on biocatalytic accumulation at mediatorless peroxidase/carbon paste electrodes

Cited by 35 publications

References 10 publications

Determination of catecholamines in pharmaceutical formulations using a biosensor modified with a crude extract of fungi laccase (Pleurotus ostreatus)

Determination of catecholamines in pharmaceutical formulations using a biosensor modified with a crude extract of fungi laccase (Pleurotus ostreatus)

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

The synergetIc effect of redox mediators and peroxidase in a bienzymatic biosensor for glucose assays in FIA

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