Thermodynamic and kinetic parameters of the irreversible thermal deactivation (denaturation) of the acid protease

Range Table - link
Organism Fungus Aspergillus foetidus
Reference Souza PM et al., Kinetic and thermodynamic studies of a novel acid protease from Aspergillus foetidus. Int J Biol Macromol. 2015 Nov81 :17-21. doi: 10.1016/j.ijbiomac.2015.07.043 p.20 table 1PubMed ID26210038
Method Abstract: "The kinetics of a thermostable extracellular acid protease produced by an Aspergillus foetidus strain was investigated at different pH, temperatures and substrate concentrations."
Comments P.20 left column 3rd paragraph: "The acid protease investigated here has a ΔH*d value at 55 °C (311.39 kJ/mol) (Table 1) much higher than those of the above-mentioned alkaline or neutral proteases from A. awamori [ref 15], A. fumigatus [ref 7] and N. alba [ref 11], confirming the earlier conclusions. The extent of thermal enzyme denaturation also depends on the activation entropy (ΔS*d) of this event, which expresses the amount of energy per degree involved in the transition from a native to a denatured state [ref 8]. As shown in Table 1, consistently with the increase in the disorder or randomness degree consequent to such a transition, the ΔS*d values were positive (599.59–610.49 J/mol K) at all temperatures at which A. foetidus protease was tested."
Entered by Uri M
ID 114388