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Literature summary 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
| EC Number | General Stability | Organism |
|---|---|---|
| 4.2.2.10 | addition of protein stabilizes the enzyme and doubles the half-life time | Aspergillus niger |
| 4.2.2.10 | partially purified enzyme is less stable than the crude enzyme | Aspergillus niger |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.2.10 | Aspergillus niger | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.2.10 | partially | Aspergillus niger |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.2.10 | pectinlyase | - |
Aspergillus niger |
| 4.2.2.10 | PL | - |
Aspergillus niger |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.10 | 29 | - |
minimum deactivation rate constant at pH 3.9 and 29°C, deactivation process is modelled as first-order kinetics | Aspergillus niger |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.10 | 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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Release 2023.1 (January 2023)
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