Deactivation kinetics parameters enthalpy (ΔH), free energy (ΔG), entropy (ΔS) and half-life t1/2 of the purified protease

Range Table - link
Organism Bacteria Bacillus circulans
Reference Ch. Subba Rao, T. Sathish, P. Ravichandra, R.S. Prakasham, Characterization of thermo- and detergent stable serine protease from isolated Bacillus circulans and evaluation of eco-friendly applications, Process Biochemistry, Volume 44, Issue 3, March 2009, Pages 262-268 link P.266 table 2
Method Abstract: "Alkaline protease from Bacillus circulans has been purified and characterized in detail for its robustness and its eco-friendly application potential at leather processing and detergent industries."
Comments P.266 left column top paragraph: "Evaluation of ΔH (enthalpy), ΔG (free energy) and ΔS (entropy) values at 75, 80, 85 and 90 °C revealed little variation in enthalpy values indicating the stability in enzyme heat capacity as noticed for xylanase produced by Trichoderma reesei QM9414 [ref 36]. ΔG values, however, decreased gradually from 100 to 97 kJ/mol with increase in temperature from 75 to 90 °C (Table 2). Whereas, entropy (ΔS) values showed a different trend with respect to ΔH and ΔG and was almost constant in the temperature range of 75 and 80 °C and decreased with increase in temperature from 80 to 90 °C suggesting the destruction of ordered structure of alkaline protease at 80 °C or above. The half-life of the protease enzyme at 75 and 90 °C was observed to be 150 and 26 min suggesting the thermo stable nature of enzyme (Table 2). This data shows the higher half-life at this temperatures compared to proteases reported from Bacillus licheniformis NH1 by El-Hadi-Ali et al. [ref 14] and Bacillus subtilis PE11 by Adinarayana et al. [ref 37] indicating its for potential industrial application."
Entered by Uri M
ID 114390