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Thermal stability and deactivation rate constants for protease

Table 4 Thermal stability and deactivation rate constants for protease

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Figure 1. Elution profile of protease form Streptomyces sp. A6 on sephacryl S-100.
Figure 1. Elution profile of protease form Streptomyces sp. A6 on sephacryl S-100.
Table 1. Purification of extracellular protease form Streptomyces sp. A6. Thermodynamics of irreversible inactivation of the protease was determined by rearranging the Eyring’s absolute rate Eq. (7) derived from the transition state theory [14]. Free energy change (AG*) for inactivation of protease were calculated by applying Eq. (11):
Table 1. Purification of extracellular protease form Streptomyces sp. A6. Thermodynamics of irreversible inactivation of the protease was determined by rearranging the Eyring’s absolute rate Eq. (7) derived from the transition state theory [14]. Free energy change (AG*) for inactivation of protease were calculated by applying Eq. (11):
Figure 3. Phase contrast microscopy of Fusarium udum spore ger- mination assay (magnification 100X). (a) Germination of spores after treatment with heat inactivated purified protease from Strepto- myces sp. A6 (arrow shows germinated spores); (b) Inhibition of spore germination after treatment with active purified protease from Streptomyces sp. A6. (c) Regression plot of Fusarium udum inhi- bition by antifungal protease from Streptomyces sp. A6. R*= 0.94.
Figure 3. Phase contrast microscopy of Fusarium udum spore ger- mination assay (magnification 100X). (a) Germination of spores after treatment with heat inactivated purified protease from Strepto- myces sp. A6 (arrow shows germinated spores); (b) Inhibition of spore germination after treatment with active purified protease from Streptomyces sp. A6. (c) Regression plot of Fusarium udum inhi- bition by antifungal protease from Streptomyces sp. A6. R*= 0.94.
Table 2. Effect of various chemical agents on protease activity.
Table 2. Effect of various chemical agents on protease activity.
Figure 4. Antifungal activity of (A) heat inactivated purified protease from Streptomyces sp. A6 (negative control); (B) purified protease from Streptomyces sp. A6; (C) chemical fungicide mancozeb, 50 yg/ml of active ingredient (positive control), by well diffusion method.
Figure 4. Antifungal activity of (A) heat inactivated purified protease from Streptomyces sp. A6 (negative control); (B) purified protease from Streptomyces sp. A6; (C) chemical fungicide mancozeb, 50 yg/ml of active ingredient (positive control), by well diffusion method.
Table 3. Substrate specificity of protease with synthetic peptides. Table 4. Kinetic parameters for protease.
Table 3. Substrate specificity of protease with synthetic peptides. Table 4. Kinetic parameters for protease.
Table 5. Deactivation rate constants (K,) and half life (t,,) and thermodynamic parameters AEF,,, AH*, AS* and AG* for de activation of protease at different temperatures. ‘Value of AE,a) was calculated as 50.014 KJ/mol. AH* is change in enthalpy; AS* is change in entropy and AG* is Gibb’s fre energy.
Table 5. Deactivation rate constants (K,) and half life (t,,) and thermodynamic parameters AEF,,, AH*, AS* and AG* for de activation of protease at different temperatures. ‘Value of AE,a) was calculated as 50.014 KJ/mol. AH* is change in enthalpy; AS* is change in entropy and AG* is Gibb’s fre energy.
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