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Issue Date
1989Submitted date
2023-10-11
Metadata
Show full item recordAbstract
Pressure shows a distinct effect on the activity and stability of enzymes in solution. We observed for Trypsin an increase of activity of 39,8 % at 55 °C. The investigations were made continously by using a tubular reactor. Enzymes. immobilized on Eupergit C®, which is a water-insoluble carrier, behave in a similar manner but with smaller influence of pressure. In opposite to Trypsin in solution, the carrierbound enzyme had a denaturation point of 60 °C (Trypsin in solution: 50 °C). Also the stability rose with pressure. Similar results were obtained using immobilized Penicillin-Acylase. At 40°C and 300 bar no decrease of activity could be observed after an incubation time of 2 hours. This high stability leads to to an increased lifetime of the catalyst which is promotive for technical use.Citation
Enzyme in der Lebensmitteltechnologie, 1989, 221 - 225Affiliation
Institut für Technische Chemie |, Lehrstuhl | der Technischen Universität München, Lichtenbergstraße 4, 8046 GarchingType
Book chapterconference paper
Language
deSeries/Report no.
GBF Monographien, Band 11ISSN
0930-4320ISBN
3-527-27877-XCollections
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