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Existing procedures help express the fusion protein prepared by the coupling of the C-terminus of citrate synthase with the N-terminus of malate dehydrogenase in Escherichia coli. Gel filtration and Western blot analyses help determine the molecular weight of isolated, purified proteins. Kinetic studies of the fusion protein reveal less transient time for the coupled reaction sequence for fusion proteins in comparison with that of free enzymes. The fusion protein exhibits higher sequestering capacity toward oxaloacetate in comparison with that of systems with free enzymes.

Simultaneous application of two chemically unique functional monomers, the feebly basic-2-vinylpyridine and the acidic and hydrogen bonding methacrylic acid, reveal noncovalent molecular imprinting in ethylene glycol dimethylacrylate based copolymers. Polymers synthesized with only one of these monomers, do not exhibit the enhanced recognition abilities of imprinted polymers.

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Previously reported flow microcalorimeter devices for enzymic reaction heat measurement, enzyme thermistors, have here been extended with systems for on-line sample treatment. Glucose analysis was performed by intermittent flow injections of 50 μl samples through such an enzyme thermistor device containing immobilized glucose oxidase and catalase. Sucroce analysis was performed by allowing diluted samples to continuously pass through an additional enzyme thermistor containing immobilized invertase. The reaction heats were recorded as temperature changes in the order of 10-50 m°C for concentrations of 0.05-0.30 M glucose or sucrose present in the original non-diluted samples. The performance of this system was investigated by its ability to follow concentration changes obtained from a gradient mixer. The system was applied to monitoring and controlling the hydrolysis of sucrose to glucose and fructose in a plug-flow reactor with immobilized invertase. The reactor was continuously fed by a flow of scurose of up to 0.3 M (100 g/l). Glucose and remaining sucrose were monitored in the effluent of the column. By using flow rate controlled feed pumps for sucrose and diluent the influent concentration of sucrose was varied while the overall flow rate remained constant. On-line control of the effluent concentration of lucose and sucrose was achieved by a proportional and integral regulator implemented on a microcomuter. Preset concentration of glucose in the effluent could be maintained over an extended period of time espite changes in the overall capacity of the invertase reactor. Long delay times in the sensor system and the enzyme column made it necessary to carefully tune the control parameters. Changes of set-point value and temperature disturbances were used to verify accuracy of controlling performance. [ABSTRACT FROM AUTHOR]