| Title: | Stability of proteinase from Carica papaya latex in dense gases |
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| Authors: | ID Leitgeb, Maja (Author)
ID Primožič, Mateja (Author)
ID Knez, Željko (Author) |
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| Files: |  http://dx.doi.org/10.1016/j.supflu.2004.05.005
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| Language: | English |
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| Work type: | Unknown |
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| Typology: | 1.01 - Original Scientific Article |
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| Organization: | FKKT - Faculty of Chemistry and Chemical Engineering
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| Abstract: | Proteinase from Carica papaya latex was tested on its thermal stability at atmospheric pressure and in supercritical carbon dioxide, near-critical propane and dimethyl-ether. In supercritical carbon dioxide at 300 bar thermalactivation of the examined proteinase was improved in the comparison toatmospheric pressure. In propane and dimethyl-ether (300 bar) activity of the examined proteinase decreased. Influence of compressionžexpansion cycles on residual activity of the same proteinase in supercritical carbon dioxide (300 bar and 50 °C) was studied, as well. Different ways of transition from supercritical to low-pressure-state were used which affected residual activityof the proteinase.Addition of water in the system increased activity of proteinase from C. papaya, which was incubated in supercritical carbon dioxide for 24 h. Optimum amount of water was found to be between 0.5 and 0.7 g/L. |
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| Keywords: | chemical processing, high pressure technology, supercritical CO2, proteinase, thermal stability, pressure stability, enzyme activity, water content, dense gases |
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| Year of publishing: | 2005 |
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| PID: | 20.500.12556/DKUM-27208  |
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| UDC: | 66.09-987 |
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| ISSN on article: | 0896-8446 |
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| COBISS.SI-ID: | 9162518 |
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| NUK URN: | URN:SI:UM:DK:GURSR0OF |
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| Publication date in DKUM: | 01.06.2012 |
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| Views: | 2015 |
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| Downloads: | 28 |
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| Metadata: |    |
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| Categories: | Misc.
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