Affiliation:
1. Pure and Applied Biochemistry, Chemical Center, University of Lund, S-220 07 Lund 7, Sweden
Abstract
Immobilized penicillinase was applied in an enzyme thermistor for calorimetric analysis of samples containing penicillin G. Standard solutions as well as extracts from fermentation broth were analyzed. The enzyme was applied bound either to porous glass or, when dealing with crude preparations, to the inner surface of nylon tubing. In the fermentation system studied, high concentrations of penicillin were present, thus allowing dilution to reduce the influence of the composition of the medium on the analysis. The useful linear concentration range was from 0.1 to 100 mM. The coefficient of correlation between analytical results obtained with the present method and those from conventional assays was 0.997.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Reference15 articles.
1. Clark L. C. Jr. 1972. A family of polarographic enzyme electrodes and a measurement of alcohol p. 377-394. In L. B. Wingard Jr. (ed.) Biotechnology and Bioengineering Symposium no. 3. Wiley Interscience Publishers New York.
2. Enzyme thermistor analysis in clinical chemistry and biotechnology;Danielsson B.;Pure Appl. Chem.,1979
3. Use of an enzyme thermistor in continuous measurements and enzyme reactor control;Danielsson B.;Biotechnol. Bioeng.,1979
4. Design and response characteristics of an enzyme electrode for measurement of penicillin in fermentation broth;Enfors S.;Enzyme Microb. Technol.,1979
5. Enzyme electrodes and solid surface fluorescence methods;Guilbault G. G.;Methods Enzymol.,1976
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