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Literature summary for 4.2.2.10 extracted from
- Studies on pH and thermal deactivation of pectolytic enzymes from Aspergillus niger (2003), Biochem. Eng. J., 16, 57-67.
No PubMed abstract available
General Stability
| General Stability | Organism |
|---|---|
| addition of protein stabilizes the enzyme and doubles the half-life time | Aspergillus niger |
| partially purified enzyme is less stable than the crude enzyme | Aspergillus niger |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| partially | Aspergillus niger |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pectinlyase | - |
Aspergillus niger |
| PL | - |
Aspergillus niger |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 29 | - |
minimum deactivation rate constant at pH 3.9 and 29°C, deactivation process is modelled as first-order kinetics | Aspergillus niger |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3.9 | - |
minimum deactivation rate constant at pH 3.9 and 29°C, deactivation process is modelled as first-order kinetics | Aspergillus niger |
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