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  • Activity and stability of hydrolases in SC CO2 and liquid propane [Elektronski vir]
    Leitgeb, Maja ; Primožič, Mateja, 1975- ; Knez, Željko
    Thermal stability of proteinase from Carica papaya in supercritical CO2 was studied. Optimal temperature for the examined protease was shifted from 60°C at atmospheric pressure to 40°C in nonaqueous ... SC CO2. Between 30°C and 50°C proteinase activity in SC CO2 is higher than atmospheric pressure. The influence of pressurization/depressurization steps on the enzyme activity was examined. Proteinase from Carica papaya was pressurized by adding CO2. In the first series of experiments depressurization was reached fast expansion and cooling of the system, while in the second series of experiments it was achieved by first, cooling the system to 20°C and second, by fast expansion of CO2. The third types of experiments were made to the difference between fast and slow depressurization of the system. The results showed that after few such cycles enzyme activity reversible increased. Stability and Activity of lipases from Pseudomonas fluorescences, Rhizpous javanicus, Rhizpous niveus and Porchine pancreas in aqueous medium at atmospheric pressure and in SC CO2 as well as in liquid propane at 100 bar and 40°C were studied as well.
    Vrsta gradiva - prispevek na konferenci
    Leto - 2001
    Jezik - angleški
    COBISS.SI-ID - 6672662