Journal of the Iranian Chemical Society

, Volume 7, Issue 2, pp 432–440 | Cite as

Purification of α-Amylase from Bacillus sp. GHA1 and its partial characterization

  • A. Ahmadi
  • S. Ghobadi
  • K. Khajeh
  • B. Nomanpour
  • A. Badoei Dalfard


Bacillus sp. GHA1 was isolated from water samples and screened for the production of α-amylase. Maximum production of amylase by this strain occurs at 42 °C, pH 6.5 and 72 h after cultivation in production medium. The enzyme was purified through successive applications of ammonium sulfate precipitation, ion exchange and hydrophobic interaction chromatography, resulting in a single band with an apparent molecular weight of 66 kDa, as judged by SDS-PAGE. Calcium analysis of the purified enzyme revealed that it contained three metal ions per molecule. The new extracellular α-amylase is active in a wide range of pH with its maximum activity at pH values 5.5–8.0. The optimum temperature for enzyme activity is 57 °C and the presence of calcium has relatively low influence on its activity and thermostability. The Bacillus sp. GHA1 α-amylase with these properties may be suitable for use in detergent and food industries.


α-Amylase Bacillus sp. GHA1 pH profile Broad range of pH Industrial applications 


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Copyright information

© Iranian Chemical Society 2010

Authors and Affiliations

  • A. Ahmadi
    • 1
  • S. Ghobadi
    • 1
  • K. Khajeh
    • 2
  • B. Nomanpour
    • 3
  • A. Badoei Dalfard
    • 2
  1. 1.Department of Biology, Faculty of ScienceRazi UniversityKermanshahIran
  2. 2.Department of Biochemistry, Faculty of ScienceTarbiat Modarres UniversityTehranIran
  3. 3.Department of Microbiology, School of MedicineTehran University of Medical SciencesTehranIran

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