EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.3 | sorbitol | presence of sorbitol and trehalose significantly increase the substrate affinity and catalytic efficiency of glucoamylases GAM-1 and GAM-2 | Aspergillus niger | |
3.2.1.3 | trehalose | presence of sorbitol and trehalose significantly increase the substrate affinity and catalytic efficiency of glucoamylases GAM-1 and GAM-2 | Aspergillus niger |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.3 | Aspergillus niger | - |
- |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.3 | GAM-1 | - |
Aspergillus niger |
3.2.1.3 | GAM-2 | - |
Aspergillus niger |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | additional information | - |
during the thermal inactivation progress, combined with the loss of the helical structure and a majority of the tertiary structure, tryptophan residues are partially exposed and further lead to glucoamylases aggregating. The thermal stability of isoforms GAM-1 and GAM-2 is largely improved in the presence of sorbitol and trehalose by maintaining the native state of glucoamylases and preventing their thermal aggregation | Aspergillus niger |
3.2.1.3 | 70 | - |
isoform GAM-1, half-life 45 min, isoform GAM-2, half-life 216 min | Aspergillus niger |