1,721,110 research outputs found
Enzyme based amperometric biosensors
No full textCurrent research on enzyme based electrochemical biosensors deals essentially with the same target analytes as was at focus in the early days of biosensor research, that is those within the clinical/medical, food/agriculture, and environmental fields [1•–13]. However, there has been substantial progress through the years and progress continues, as resumed in Figure 1A. One of the major differences is that (bio)electrochemists finally seem to start to understand what kind of molecules they deal with, that is with biological molecules and vice versa, biochemists, (micro)biologists start to become interested in (bio)electrochemistry. This is clearly shown for example in the recent very intense research on biofuel cells [14–26] and lately also on biosupercapacitors [27] that has absolutely had a great influence on current research on enzyme based biosensors and bioelectrochemistry as a whole
Electrochemical Study Of Flavins, Phenazines, Phenoxazines And Phenothiazines Immobilized On Zirconium Phosphate
No full textAdsorption of a number of flavins, phenazines, phenoxazines, and phenothiazines on zirconium phosphate (ZP) was carried out in aqueous solution. The adsorbed organic dyes on ZP were used to prepare modified carbon paste electrodes. The electrochemical properties of the immobilized dyes were investigated and also their possible use to electrocatalytically oxidize NADH. The formal potential (E0′) of most of the adsorbed flavins, phenoxazines, and phenothiazines shifted markedly towards more positive potentials compared with their values in solution. The pH of the contacting solution did not affect their E0′-values between pH 1 and 9. The phenazines did neither present good electrochemical response nor electrocatalytic activity for NADH oxidation and their E0′-values remained pH dependent. 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Cellobiose dehydrogenase: Insights on the nanostructuration of electrodes for improved development of biosensors and biofuel cells
No full textCellobiose dehydrogenase (CDH) is a versatile bioelectrocatalyst lately at focus due to its sugar oxidising properties in combination with its inherent ability for direct electron transfer communication with electrodes making it possible to be used in bioanodes in the enzymatic fuel cells (EFCs), self-powered biosensors, and biosupercapacitors. During the last 20 years, many new nanomaterials and hybrid nanocomposites have been developed and employed in combination with various oxidoreductases, such as CDH, to increase the overall performance of electrical devices (e.g. biosensors, EFCs etc.). It has also been shown that nanomaterials can be further chemically modified to facilitate electron transfer pathways between the biocomponent and electrodes. Both carbon and metal based nanomaterials and combinations thereof have been used together with CDH to improve the performance. In this review, we resume all the findings related to the influence of effective nanostructuration to improve the electron transfer communication with electrodes yielding higher sensitivity of biosensors or increasing the power output of EFC based on CDH from different sources
Direct electron transfer of dehydrogenases for development of 3rd generation biosensors and enzymatic fuel cells
No full textDehydrogenase based bioelectrocatalysis has been increasingly exploited in recent years in order to develop new bioelectrochemical devices, such as biosensors and biofuel cells, with improved performances. In some cases, dehydrogeases are able to directly exchange electrons with an appropriately designed electrode surface, without the need for an added redox mediator, allowing bioelectrocatalysis based on a direct electron transfer process. In this review we briefly describe the electron transfer mechanism of dehydrogenase enzymes and some of the characteristics required for bioelectrocatalysis reactions via a direct electron transfer mechanism. Special attention is given to cellobiose dehydrogenase and fructose dehydrogenase, which showed efficient direct electron transfer reactions. An overview of the most recent biosensors and biofuel cells based on the two dehydrogenases will be presented. The various strategies to prepare modified electrodes in order to improve the electron transfer properties of the device will be carefully investigated and all analytical parameters will be presented, discussed and compared
A new osmium-polymer modified screen-printed graphene electrode for fructose determination
No full textThis paper describes the development and performance of the first fructose biosensor based on a com-mercial screen-printed graphene electrode (SPGE). The electrode was modified with an osmium-polymer,which allowed the efficient wiring of the enzyme fructose dehydrogenase (FDH). The immobilization ofboth osmium-polymer and FDH was realized in an easy way. Aliquots of 10 microL Os-polymer and 10 microLFDH were thoroughly mixed with poly(ethylene glycol) (400) diglycidyl ether (PEDGE) and deposited onthe electrode surface and left there to dry overnight. The biosensor exhibits a detection limit of 0.8 microM, a linear range between 0.1 and 8 mM, high sensitivity to fructose (2.15 microA cm−2/mM), good reproducibility( RSD = 1.9%), fast response time (3 s) and a stability of 2 months when stored in the freezer.The proposed fructose biosensor was tested in real food samples and validated with a commercial spectrophotometric enzymatic kit. No significant interference was observed with the proposed biosensor
Synthesis and characterization of “green” metallic nanoparticles for electrochemical biosensors development
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Supercapacitive biofuel cells
No full textSupercapacitive biofuel cells’ (SBFCs) most recent advancements are herein disclosed. In conventional SBFCs the biocomponent is employed as the pseudocapacitive component, while in self-charging biodevices it also works as the biocatalyst. The performance of different types of SBFCs are summarized according to the categorization based on the biocatalyst employed: supercapacitive microbial fuel cells (s-MFCs), supercapacitive biophotovoltaics (SBPV) and supercapacitive enzymatic fuel cells (s-EFCs). SBFCs could be considered as promising ‘alternative’ energy devices (low-cost, environmentally friendly, and technically undemanding electric power sources etc.) being suitable for powering a new generation of miniaturized electronic applications
Improved DET communication between cellobiose dehydrogenase and a gold electrode modified with a rigid self-assembled monolayer and green metal nanoparticles: the role of an ordered nanostructuration
No full textEnhanced Direct Electron Transfer of Fructose Dehydrogenase Rationally Immobilized on a 2-Aminoanthracene Diazonium Cation Grafted Single-Walled Carbon Nanotube Based Electrode
No full textIn this paper, an efficient direct electron transfer (DET) reaction was achieved between fructose dehydrogenase (FDH) and a glassy-carbon electrode (GCE) upon which anthracene-modified single-walled carbon nanotubes were deposited. The SWCNTs were activated in situ with a diazonium salt synthesized through the reaction of 2-aminoanthracene with NaNO2 in acidic media (0.5 M HCl) for 5 min at 0 °C. After the in situ reaction, the 2-aminoanthracene diazonium salt was electrodeposited by running cyclic voltammograms from +1000 to -1000 mV. The anthracene-SWCNT-modified GCE was further incubated in an FDH solution, allowing enzyme adsorption. Cyclic voltammograms of the FDH-modified electrode revealed two couples of redox waves possibly ascribed to the heme c1 and heme c3 of the cytochrome domain. In the presence of 10 mM fructose two catalytic waves could clearly be seen and were correlated with two heme cs (heme c1 and c2), with a maximum current density of 485 ± 21 μA cm-2 at 0.4 V at a sweep rate of 10 mV s-1. In contrast, for the plain SWCNT-modified GCE only one catalytic wave and one couple of redox waves were observed. Adsorbing FDH directly onto a GCE showed no non-turnover electrochemistry of FDH, and in the presence of fructose only a slight catalytic effect could be seen. These differences can be explained by considering the hydrophobic pocket close to heme c1, heme c2, and heme c3 of the cytochrome domain at which the anthracenyl aromatic structure could interact through π-π interactions with the aromatic side chains of the amino acids present in the hydrophobic pocket of FDH
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