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Literature summary extracted from

  • Liu, Y.; Meng, Z.; Shi, R.; Zhan, L.; Hu, W.; Xiang, H.; Xie, Q.
    Effects of temperature and additives on the thermal stability of glucoamylase from Aspergillus niger (2014), J. Microbiol. Biotechnol., 24, 33-43.
    View publication on PubMed

Activating Compound

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

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Aspergillus niger
-
-
-

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 GAM-1
-
 Aspergillus niger
3.2.1.3 GAM-2
-
 Aspergillus niger

Temperature Stability [°C]

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