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Literature summary for 3.2.1.1 extracted from

  • Demirkan, E.S.; Mikami, B.; Adachi, M.; Higasa, T.; Utsumi, S.
    alpha-Amylase from B. amyloliquefaciens: purification, characterization, raw starch degradation and expression in E. coli (2005), Process Biochem., 40, 2629-2636.
No PubMed abstract available
Search for more literature for 3.2.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strains JM109, HB101, HMS174(DE3), and BL21(DE3) Bacillus amyloliquefaciens

Inhibitors

Inhibitors Comment Organism Structure
Fe2+ 90% inhibition at 1-5 mM Bacillus amyloliquefaciens
Hg2+ complete inhibition at 5 mM, 94% inhibition at 1 mM Bacillus amyloliquefaciens
Zn2+ 88% inhibition at 1-5 mM Bacillus amyloliquefaciens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.92
-
 soluble starch pH 5.9, 37°C Bacillus amyloliquefaciens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 1 Ca2+ bound per enzyme molecule Bacillus amyloliquefaciens
additional information the enzyme is poorly affected by Ca2+, Mg2+, Li+, Cu2+, Ba2+, and Mn2+ Bacillus amyloliquefaciens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
 x * 52000, SDS-PAGE Bacillus amyloliquefaciens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
maltopentaose + H2O Bacillus amyloliquefaciens
-
 malto-oligomers + maltose
-
 ?
starch + H2O Bacillus amyloliquefaciens
-
 malto-oligosaccharides
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
 isolated from soil in Turkey
-

Purification (Commentary)

Purification (Comment) Organism
native extracellular enzyme from culture medium by adsorption chromatography, the enzyme is sensitive to proteolytic degradation during purification and requires PMSF addition for protection Bacillus amyloliquefaciens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 activities with soluble starch of wild-type native enzyme, and recombinant wild-type enzyme from different expressing Escherichia coli strains, overview Bacillus amyloliquefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 starch + H2O hydrolysis of soluble starch, and degradation of raw starch granules of different source, overview Bacillus amyloliquefaciens 2 malto-oligosaccharides + maltose
-
 ?
maltopentaose + H2O
-
 Bacillus amyloliquefaciens malto-oligomers + maltose
-
 ?
maltopentaose + H2O preferred substrate Bacillus amyloliquefaciens malto-oligomers + maltose
-
 ?
starch + H2O
-
 Bacillus amyloliquefaciens malto-oligosaccharides
-
 ?

Subunits

Subunits Comment Organism
? x * 52000, SDS-PAGE Bacillus amyloliquefaciens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Bacillus amyloliquefaciens

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 70 temperature profile Bacillus amyloliquefaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 4 h, 69% remaining activity Bacillus amyloliquefaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Bacillus amyloliquefaciens

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 pH profile Bacillus amyloliquefaciens

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 8 stable for 1 h Bacillus amyloliquefaciens