General Stability | Organism |
---|---|
the protease is largely pressure stable at room temperature. At 100 MPa a significant stabilisation of the enzyme against temperature-induced inactivation is observed. Pressure drastically inhibits the cleavage by cathepsin D in Bis-Tris buffer (pH 6.0) causing a reduction of the catalytic rate of more than 50% at 100-400 MPa. The enzyme is relatively stable with more than 57% and 40% residual activity after 30 min treatment at 30°C and 300 MPa or 400 MPa, respectively. At higher pressures the enzyme is destabilised rapidly resulting in a residual activity of less than 10% after 30 min treatment at 600 MPa | Bos taurus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
spleen | - |
Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Hemoglobin + H2O | - |
Bos taurus | ? | - |
? | |
Myoglobin + H2O | the hydrolysis rate is fairly slow | Bos taurus | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
maximal substrate cleavage by cathepsin D is identified at 60°C and ambient pressure conditions after 20 min treatment | Bos taurus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 60 | the protease is heat stable at ambient pressure up to 300 MPa and 55°C, respectively, causing less than 10% inactivation after 10 min treatment. Cathepsin D is quickly inactivated at temperatures above 60°C | Bos taurus |