EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.7 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.7 | Aspergillus niger | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.7 | commercial preparation | - |
Aspergillus niger | - |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.7 | endo-inulinase | - |
Aspergillus niger |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.7 | 37 | - |
assay at | Aspergillus niger |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.7 | 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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.7 | 5.5 | 6 | assay at | Aspergillus niger |