Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.1 extracted from

  • Asoodeh, A.; Chamani, J.; Lagzian, M.
    A novel thermostable, acidophilic alpha-amylase from a new thermophilic Bacillus sp. Ferdowsicous isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization (2010), Int. J. Biol. Macromol., 46, 289-297.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EDTA 85% residual activity at 10 mM EDTA Bacillus sp. (in: Bacteria)
Hg2+ complete inhibition at 5 and 10 mM Bacillus sp. (in: Bacteria)
additional information not affected by NaCl, KCl, phenylmethylsulfonyl fluoride, and beta-mercaptoethanol Bacillus sp. (in: Bacteria)
Zn2+ about 30% residual activity at 10 mM Bacillus sp. (in: Bacteria)

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ the activity is increased by approximately 15% by 1 mM Ba2+ Bacillus sp. (in: Bacteria)
Fe2+ the activity is increased by approximately 15% by 1 mM Fe2+ Bacillus sp. (in: Bacteria)
Mg2+ the activity is increased by approximately 15% by 10 mM Mg2+ Bacillus sp. (in: Bacteria)
additional information the enzyme is Ca2+-independent Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
SDS-PAGE Bacillus sp. (in: Bacteria)

Organism

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

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation and Q-Sepharose column chromatography Bacillus sp. (in: Bacteria)

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12
-
crude extract, at 42°C Bacillus sp. (in: Bacteria)
267
-
after 23fold purification, at 42°C Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylopectin + H2O 78% activity compared to starch Bacillus sp. (in: Bacteria) malto-oligosaccharides
-
?
amylose + H2O 145% activity compared to starch, the enzyme activity on the amylose as substrate is 1.98times greater than amylopectin Bacillus sp. (in: Bacteria) malto-oligosaccharides
-
?
glycogen + H2O 14% activity compared to starch Bacillus sp. (in: Bacteria) malto-oligosaccharides
-
?
maltodextrin + H2O 85% activity compared to starch Bacillus sp. (in: Bacteria) malto-oligosaccharides
-
?
additional information does not hydrolyze alpha- and beta-cyclodextrin Bacillus sp. (in: Bacteria) ?
-
?
starch + H2O 100% activity Bacillus sp. (in: Bacteria) malto-oligosaccharides maltoheptaose is observed as a predominant product. When further hydrolysis is performed, glucose, maltose, maltotriose, maltotetraose, maltopentaose and maltohexaose appear. Glucose and maltose are produced after 2 h of incubation, and after 24 h, the main products are maltotriose, maltose and glucose ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
optimum around 70°C Bacillus sp. (in: Bacteria)

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 75
-
Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 75 the amylase is very stable at temperatures between 30 and 70°C after 150 min of incubation. It becomes completely inactivated at temperatures higher than 85°C for this period. The enzyme remains active to more than 75% up to 75°C for 45 min, the relative activities at 55 and 65°C are approximately 79% and 90% of the activity at 70°C, respectively. The enzyme displays a half-life of 48 min at 80°C Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
Bacillus sp. (in: Bacteria)

pH Range

pH Minimum pH Maximum Comment Organism
4 9
-
Bacillus sp. (in: Bacteria)

pH Stability

pH Stability pH Stability Maximum Comment Organism
3.5 7.5 remains stable from pH 3.5-7.0, the enzyme activity keeps above 75% after treatment at pH values ranging from 3.5 to 6.0, for pH values beyond 7.5 or less than 3.5 the enzyme activity decreases drastically Bacillus sp. (in: Bacteria)