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Biosensor biocatalytic

Biosensors may be classified into two categories biocatalytic biosensors and bioaffinity biosensors. Biocatalytic sensors contain a biocatalyst such as an enzyme to recognize the analytic selectively. Bioaflinity biosensors, on the other hand, may involve antibody, binding protein or receptor protein, which form stable complexes with the corresponding ligand. An immunosensor in which antibody is used as the receptor may represent a bioaflinity biosensor. [Pg.361]

In a biocatalytic biosensor the molecular recognition component is an enzyme. Enzymes, macromolecular catalysts that are manufactured by plants and animals, affect the rates of biochemical reactions. Virtually all of the millions of chemical reactions involved in Hfe processes have associated enzymes controlling the rates. CoUectively, there are several thousand enzymes known and perhaps many thousand more yet to be discovered. [Pg.107]

Fig. 2. Schematic of an electrochemical biocatalytic biosensor showing enzyme E immobilized onto the electrode where S is the substrate (target) and P is... Fig. 2. Schematic of an electrochemical biocatalytic biosensor showing enzyme E immobilized onto the electrode where S is the substrate (target) and P is...
The simple cases where one enzyme is employed afford a limited scope of potential targets. Usually two or more enzyme reactions are coupled, as exemplified by the development of a piezoelectricaHy-transduced biocatalytic biosensor that couples two enzyme reactions to detect glucose [492-62-6] ... [Pg.108]

Fig. 3. Detail of enzyme-modified quartz radio crystal used in a piezoelectric biocatalytic biosensor. Fig. 3. Detail of enzyme-modified quartz radio crystal used in a piezoelectric biocatalytic biosensor.
Several other biosensors have been developed usiag this oxygen-quenched fluorescence approach. Target species iaclude ethanol [64-17-5] hydrogen peroxide [7722-84-17, H2O2, lactate, and xanthine [69-89-6] C H4N402, usiag alcohol oxidase, catalase [9001-05-2] lactate oxidase, and xanthine oxidase, respectively. An additional technique for biocatalytic biosensors iavolves the firefly chemiluminescent reaction (17) ... [Pg.110]

Toxin (Enzyme Inhibition) Biosensors Enzyme affectors (inhibitors and activators) that influence the rate of biocatalytic reactions can also be measured. Sensing probes for organophosphate and carbamate pesticides, for the respiratory... [Pg.181]

Background current, 21, 65 Background subtraction, 40, 106 Bacteria electrode, 182 Band microelectrodes, 130, 135 Beryllium, 82 Bienzyme electrodes, 175 Biocatalytic devices, 172 Biological recognition, 171 Biosensors, 50, 171 Bipotentiostat, 106 Blood electrolyte, 165 Boltzmann equation, 19 Brain analysis, 40, 116 Butler-Volmer equation, 14... [Pg.205]

Biocatalytic membrane electrodes have an ISE or a gas sensing electrode in contact with a thin layer of biocatalytic material, which can be an immobilized enzyme, bacterial particles or a tissue slice, as shown in Fig. 3 The biocatalyst converts substrate (the analyte) into product, which is measured by the electrode. Electrodes of this type are often referred to as biosensors . [Pg.7]

The laccases, classed as polyphenol oxidases, catalyze the oxidation of diphenols, polyamines, as well as some inorganic ions, coupled to the four-electron reduction of oxygen to water see Fig. 12.4 for the proposed catalytic cycle. Due to this broad specificity, and the recognition that this specificity can be extended by the use of redox mediators [27], laccases show promise in a range of applications [28], from biosensors [29-32], biobleaching [27, 33-35] or biodegradation [36], to biocatalytic fuel cells [1-3, 18, 26, 37-42]. [Pg.415]

The method of enzyme immobilization constitutes a key factor in the construction of these systems as it is the biocatalytic membrane that largely determines sensitivity, stability and response-time characteristics of the biosensor. [Pg.658]

SCATCHARD PLOT BINDING SITE BINOMIAL THEOREM PASCAL S TRIANGLE BIOAVAILABILITY BIOCATALYTIC ELECTRODE BIOSENSOR... [Pg.727]

Bioelectrocatalysis involves the coupling of redox enzymes with electrochemical reactions [44]. Thus, oxidizing enzymes can be incorporated into redox systems applied in bioreactors, biosensors and biofuel cells. While biosensors and enzyme electrodes are not synthetic systems, they are, essentially, biocatalytic in nature (Scheme 3.5) and are therefore worthy of mention here. Oxidases are frequently used as the biological agent in biosensors, in combinations designed to detect specific target molecules. Enzyme electrodes are possibly one of the more common applications of oxidase biocatalysts. Enzymes such as glucose oxidase or cholesterol oxidase can be combined with a peroxidase such as horseradish peroxidase. [Pg.56]

Redox-based biosensors. Noble metals (platinum and gold) and carbon electrodes may be functionalized by oxidation procedures leaving oxidized surfaces. In fact, the potentiometric response of solid electrodes is strongly determined by the surface state [147]. Various enzymes have been attached (whether physically or chemically) to these pretreated electrodes and the biocatalytic reaction that takes place at the sensor tip may create potential shifts proportional to the amount of reactant present. Some products of the enzyme reaction that may alter the redox state of the surface e.g. hydrogen peroxide and protons) are suspected to play a major role in the observed potential shifts [147]. [Pg.131]

Besides the broad applications of electrically contacted enzyme electrodes as amperometric biosensors, substantial recent research efforts are directed to the integration of these functional electrodes as biofuel cell devices. The biofuel cell consists of an electrically contacted enzyme electrode acting as anode, where the oxidation of the fuel occurs, and an electrically wired cathode, where the biocatalyzed reduction of the oxidizer proceeds (Fig. 12.4a). The biocatalytic transformations occurring at the anode and the cathode lead to the oxidation of the fuel substrate and the reduction of the oxidizer, with the concomitant generation of a current through the external circuit. Such biofuel cells can, in principle, transform chemical energy stored in biomass into electrical energy. Also, the use... [Pg.340]

Several electrical aptamer biosensors implemented the biocatalytic hydrolytic activities of thrombin, or the fact that proteins (e.g., thrombin) often include several binding sites for the formation of supramolecular complexes with different aptamers. The bioelectrocatalytic detection of thrombin by an electrical aptasensor was demonstrated by formation of an aptamer-thrombin complex on the electrode, followed by a thrombin-mediated hydrolysis of the nitroaniline-functionalized peptide, (22), yielding the redox-active product nitroaniline, (23), which was analyzed electrochemically76 (Fig. 12.20b). A further bioelectrocatalytic aptasensors configuration is depicted in Fig. 12.20c, where the multidentate formation of aptamer-protein supramolecular complexes was used to analyze thrombin.76 Thrombin includes two different binding sites for aptamers.77 One of the thrombin aptamers... [Pg.362]

The simple cases where one enzyme is employed afford a limited scope of potential targets. Usually two or more enzyme reactions are coupled, as exemplified by the development of a piezoelectrically-transduced biocatalytic biosensor that couples two enzyme reactions to detect glucose [492-62-6], C6H120 > (3) (13). In this biosensor a quartz radio crystal is functionalized with the enzyme glucose-6-phosphate dehydrogenase. As shown in Figure 3, a thin film of Prussian blue [14038 43-8], C18N18Fe7, is then coated onto the crystal. [Pg.108]


See other pages where Biosensor biocatalytic is mentioned: [Pg.396]    [Pg.107]    [Pg.108]    [Pg.109]    [Pg.79]    [Pg.172]    [Pg.173]    [Pg.340]    [Pg.7]    [Pg.9]    [Pg.446]    [Pg.189]    [Pg.410]    [Pg.424]    [Pg.209]    [Pg.212]    [Pg.121]    [Pg.3]    [Pg.113]    [Pg.172]    [Pg.320]    [Pg.321]    [Pg.107]    [Pg.108]    [Pg.109]    [Pg.110]    [Pg.261]   
See also in sourсe #XX -- [ Pg.350 ]




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