Literature summary for 3.2.1.1 extracted from

Kubrak, O.I.; Storey, J.M.; Storey, K.B.; Lushchak, V.I.
Production and properties of alpha-amylase from Bacillus sp. BKL20 (2010), Can. J. Microbiol., 56, 279-288.

Search for more literature for 3.2.1.1

General Stability

General Stability	Organism
the enzyme shows good resistance to urea	Bacillus sp. (in: Bacteria)

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	no inhibition by EGTA or EDTA at 1-10 mM	Bacillus sp. (in: Bacteria)

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	no activation by Ca2+ or other divalent cations	Bacillus sp. (in: Bacteria)

Organism

Organism	UniProt	Comment	Textmining
Bacillus sp. (in: Bacteria)	-	-	-
Bacillus sp. (in: Bacteria) BKL20	-	-	-

Oxidation Stability

Oxidation Stability	Organism
the enzyme shows good resistance to H2O2	Bacillus sp. (in: Bacteria)

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	strain BKL20 produces thermostable alkaline alpha-amylase, optimization of culture conditions, overview	Bacillus sp. (in: Bacteria)	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
60	70	30 min, no loss of activity	Bacillus sp. (in: Bacteria)

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
6	11	hig activity is retained, activity remains after 24 h incubation at alkaline pH	Bacillus sp. (in: Bacteria)

Expression

Organism	Comment	Expression
Bacillus sp. (in: Bacteria)	enzyme production is stimulated by peptone 0.3% w/v and yeast extract 0.2% w/v	up

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Release 2023.1 (January 2023)