Literature summary for 3.2.1.3 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.

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Activating Compound

Activating Compound	Comment	Organism	Structure
sorbitol	presence of sorbitol and trehalose significantly increase the substrate affinity and catalytic efficiency of glucoamylases GAM-1 and GAM-2	Aspergillus niger
trehalose	presence of sorbitol and trehalose significantly increase the substrate affinity and catalytic efficiency of glucoamylases GAM-1 and GAM-2	Aspergillus niger

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger	-	-	-

Synonyms

Synonyms	Comment	Organism
GAM-1	-	Aspergillus niger
GAM-2	-	Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
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
70	-	isoform GAM-1, half-life 45 min, isoform GAM-2, half-life 216 min	Aspergillus niger

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Release 2023.1 (January 2023)