Operational stability of copolymerized enzymes at elevated temperatures
✍ Scribed by V. V. Mozhaev; V. A. Šikšnis; V. P. Torchilin; Karel Martinek
- Publisher
- John Wiley and Sons
- Year
- 1983
- Tongue
- English
- Weight
- 465 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
The copolymerization method of immobilization was used to obtain preparations of enzymes covalently incorporated in polyacrylamide gel. They possess properties making them suitable for practical use. First, the preparations are hundreds of times more stable against irreversible thermoinactivation than native enzymes. Second, on immobilization, the reversible conformational changes which also lower enzyme activity at elevated temperatures are completely suppressed. As a result, the temperatures of maximum activity for trypsin and a-chymotrypsin covalently entrapped in polyacrylamide gel are 75 and 7OoC, respectively-25 and 30°C higher than the corresponding values for the native enzymes. Therefore, the copolymerized enzyme preparations have a high operational stability at elevated temperatures.
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Stress relaxation experiments were carried out in a dry nitrogen atmosphere on polydimethylsiloxane and an ethylene-propylene terpolymer. Relaxation times much longer than expected were observed, and plots of In f(t)/f(O) versus time were linear in all cases.