Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermoclostridium stercorarium | - |
xylanase B | - |
Thermoclostridium stercorarium F-9 | - |
xylanase B | - |
Purification (Comment) | Organism |
---|---|
xylanase B | Thermoclostridium stercorarium |
Renatured (Comment) | Organism |
---|---|
the enzyme begins to denature at around 80°C and is completely denatured at 100°C. After 5 min at 100°C a large quantity of precipitate without any activity is formed. Aggregated xylanase B is disentangled and dissolved by urea treatment. The native structure is restored by rapid refolding after dilution of urea. Irreversible denaturation of the protein is caused by the same mechanism in solution and in aggregate. The remaining activity detected at 60°C after incubation at pH 7.0 and 100°C is due to the activity of the enzyme that recovers its native structure by correct protein refolding from the denatured state during chilling on ice | Thermoclostridium stercorarium |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
- |
Thermoclostridium stercorarium |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
enzyme begins to denature at around 80°C | Thermoclostridium stercorarium |
100 | - |
pH 7.0, 10 min, about 40% loss of activity. pH 5.5, 10 min, complete inactivation | Thermoclostridium stercorarium |