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Literature summary for 3.2.1.7 extracted from
- Endo-inulinase stabilization by pyridoxal phosphate modification: a kinetics, thermodynamics, and simulation approach (2011), Appl. Biochem. Biotechnol., 165, 1661-1673.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | structural and storage and functional thermostabilization of endo-inulinase through semi-rational modification of surface accessible lysine residues by pyridoxal 5'-phosphate and ascorbate reduction, method, molecular dynamics simulation, overview | Aspergillus niger |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Aspergillus niger | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endo-inulinase | - |
Aspergillus niger |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Aspergillus niger |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermostability and thermodynamics analysis of native and of modified enzymes, detailed overview. The thermal unfolding processes of endo-inulinase is irreversible | Aspergillus niger |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 6 | assay at | Aspergillus niger |
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Release 2023.1 (January 2023)
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