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(enzyme column)
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Aluminium constant-T jacket Reference column
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Measurement thermistor Wheatstone bridge
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Figure 7.10. Typical con guration of a split- ow enzyme thermistor with an aluminum constant-temperature jacket.
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EVALUATION OF BIOSENSOR PERFORMANCE
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TABLE 7.1. Thermal Biosensorsa Analyte Ascorbic acid ATP Cellobiose Cephalosporin Cholesterol Creatinine Ethanol Galactose Glucose Glucose Lactate Lactate Lactose Oxalic acid Oxalic acid Penicillin
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Immobilized Enzyme(s) Ascorbate oxidase Apyrase b-Glucosidase glucose oxidase/catalase Cephalosporinase Cholesterol oxidase catalase Creatinine iminohydrolase Alcohol oxidase/catalase Galactose oxidase GO/catalase Hexokinase Lactate-2-monooxygenase Lactate oxidase/catalase b-Galactosidase GO/catalase Oxalate oxidase Oxalate decarboxylase b-Lactamase
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Conc. Range (mM) 0.05 0.6 1 8 0.05 5 0.005 10 0.03 0.15 0.01 10 0.01 2 0.01 1 0.001 0.8 0.5 25 0.005 2 0.002 1 0.05 10 0.005 0.5 0.1 3 0.01 500
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See Ref. 11. [Reprinted, by permission, from B. Danielsson and F. Winquist in Biosensors: A Practical Approach , A. E. G. Cass, Ed., Oxford University Press, New York, 1990. The Practical Approach Series, Edited by D. Rickwood and B. D. James. # Oxford University Press 1990.]
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reactions are accompanied by signi cant enthalpy changes, thermistors with immobilized enzymes can detect local temperature changes in the environment near the thermistor surface. For example, the reactions catalyzed by catalase, GO and NADH dehydrogenase are accompanied by enthalpy changes of 100, 80, and 225 kJ/mol, respectively. Figure 7.10 shows a schematic diagram of an enzyme thermistor used to test a variety of immobilized enzymes in a ow-through biosensing device. The temperature probe is sealed inside a ow-through reaction chamber, which is encased in an aluminum constant-temperature jacket (to avoid responses due to ambient temperature uctuations). The Wheatstone bridge allow differential measurement of both termistors, thus permitting measurements of small temperature changes (down to 10 4  C). By using devices similar to that shown in Figure 7.10, many immobilized enzymes have been tested. Table 7.1 summarizes the analytes, the enzymes, and the dynamic ranges over which the enzyme thermistors provide substrate quantitation. 7.4. EVALUATION OF BIOSENSOR PERFORMANCE In addition to the usual evaluation parameters for analytical methods ( 16), the sensitivity, detection limit, dynamic range, and precision pro le, biosensors are also characterized with respect to the rapidity of their response and recovery. This
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additional evaluation is a result of their intended use, for the rapid and continuous monitoring of analytes in biological or environmental samples. The response time of a biosensor has been de ned as the time after analyte addition for the sensor s response to reach 95% of its nal value. Similarly, the recovery time is de ned as the time after analyte removal when 95% of the baseline signal has been achieved. Biosensors with response and recovery times of the order of tens of seconds or less provide useful in vivo or in situ devices. Many enzyme-based biosensors exhibit very similar response and recovery times, with parameters such as the reaction layer thickness and analyte concentration affecting the time required for 95% change to occur. Sensors that employ antibodies or chemoreceptors for chemical recognition often show fast responses, but take inordinate amounts of time to regenerate baseline readings in recovery time studies. This nding is primarily a result of the large association constants of these species for their speci c binding partners, with association kinetics being rapid, and dissociation kinetics being very slow. Chaotropic reagents and denaturants are often used ex situ, to decrease the af nity of the recognition agent for its ligand by interfering with hydrogen bonding or by reversibly altering the tertiary structure of the protein. Biosensors are also evaluated with respect to their stability. The reproducible generation of signal for a given analyte concentration is evaluated with respect to storage time, under various conditions of temperature and pH, and the results indicate the storage stability of the sensor. Operational stability is a similar type of evaluation, performed under conditions of continuous use. Operational stability is usually much poorer than storage stability. Both parameters are reported as the time required for the loss of a given percentage of the initial signal; for example, the time required for the signal generated by a particular analyte concentration to decrease to 50% of its initial value. Interferences are of particular importance for devices destined for continuous use in very complex matrices. Biosensors are tested for interferences not just from species that are expected to bind to or react with the particular chemical recognition agent employed; the end use of the biosensor is considered, and components of that sample matrix are examined for potential interference. Test assays are conducted in the sample matrix, and compared with results obtained in simple buffers in order to determine analyte recovery. In vivo examinations of glucose biosensors have been conducted using rats, dogs, and chimpanzees as test subjects.12,13 The objective of these continuing studies is an arti cial pancreas, where a glucose sensor is combined with a switching mechanism to allow automatic insulin delivery in diabetic patients. These and other studies have shown that immune responses are often generated towards membrane materials and immobilized species that are directly exposed to the living system. For this reason, a considerable worldwide research effort has been directed toward the development of biocompatible materials for use in in vivo sensors. In the references cited above, polyurethane polysiloxane12 and polyethylene oxide13 were used as the outer, biocompatible layers for the short-term in vivo studies. To date, a signi cant variety of enzyme-based biosensors have been commercialized for clinical testing laboratories and even for use by lay consumers. The most
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