purification and characterization of an extracellular thermostable alkaline α-amylase from the moderately halophilic bacterium, bacillus persicus
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abstract
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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Journal title:
molecular and biochemical diagnosis (journal)جلد ۲، شماره ۱، صفحات ۷۹-۹۴
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