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Literature summary for 3.2.1.1 extracted from

  • Rashid, N.; Ahmed, N.; Saleem Haider, M.; Haque, I.
    Effective solubilization and single-step purification of Bacillus licheniformis alpha-amylase from insoluble aggregates (2010), Folia Microbiol. (Praha), 55, 133-136.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
high level expression of thermostable Bacillus licheniformis alpha-amylase in Escherichia coli strain BL21-CodonPlus(DE3)-RIL mainly in inclusion bodies, subcloning in Escherichia coli strain DH5alpha Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis P06278
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-
Bacillus licheniformis ATCC 27811 P06278
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-

Purification (Commentary)

Purification (Comment) Organism
solubilized recombinant enzyme 138fold from Escherichia coli by cation exchange chromatography Bacillus licheniformis

Renatured (Commentary)

Renatured (Comment) Organism
solubilization of recombinant enzyme from inclusion bodies after expression in Escherichia coli without the use of denaturing agents, extraction by resuspending in 50 mmol/l sodium acetate, pH 5.0, containing 20% v/v glycerol followed by stirring at 40°C for 3-4 h, and subsequent centrifugation Bacillus licheniformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1343
-
purified recombinant enzyme, pH 5.0, 60°C Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
assay at Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
assay at Bacillus licheniformis