Volume 2, Issue 1 (2016)                   2016, 2(1): 79-94 | Back to browse issues page

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Hadipour S, Ghafoori H, Sohrabi N, Izaddoust M. Purification and characterization of an extracellular thermostable alkaline α-amylase from the moderately halophilic bacterium, Bacillus persicus. Molecular and Biochemical Diagnosis Journal. 2 (1) :79-94
URL: http://journals.modares.ac.ir/article-8-3549-en.html
1- Department of Biology, Payam-e-Noor University, Tehran Branch, Pardis, Iran
2- Department of Biology, University of Guilan, Rasht, Iran
Abstract:   (1826 Views)
  Background: Today a large number of bacterial amylases are available commercially in industry. The goal of the present study was purification and biochemical characterization of an extracellular thermostable alkaline α-amylase from the novel moderately halophilic, Bacillus persicus from the Aran-Bidgol, Iran.   Methods : Purification of enzyme, was carried out by acetone precipitation, ultrafiltration and Q-Sepharose cation exchange chromatography. Results : The purified native enzyme showed a molecular mass of 53 kDa composed of a monomer by SDS–PAGE. The optimum pH, temperature and NaCl concentration were 10, 45 C and 0.85 M respectively. It retained 50% of activity at 1.25 M NaCl and about 73% of activity at highly alkaline pH of 10.5, therefore it was a moderately halophilic and also can activate by divalent metal ions especially Ca2+ and Mg2+. The apparent values of Km and Vmax were obtained 1.053 mg/ml and 356μ/min respectively. Conclusion : In the present study we report the purification and characterization of a moderately halophilic α-amylase from a newly isolated Bacillus persicus. The purified enzyme shows interesting properties useful for industrial and biotechnological applications. The molecular cloning and structural studies of this α-amylase are in progress in our laboratory.
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Received: 2016/09/17 | Accepted: 2016/03/1 | Published: 2016/09/17

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