Molecular and Biochemical Diagnosis Journal
Molecular and Biochemical Diagnosis Journal
Molecular and Biochemical Diagnosis Journal
Medical Sciences
http://mbd.modares.ac.ir
1
admin
2383-0522
2476-6607
2267
en
jalali
1394
12
1
gregorian
2016
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2
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online
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fulltext
en
Purification and characterization of an extracellular thermostable alkaline α-amylase from the moderately halophilic bacterium, Bacillus persicus
<strong><span style="font-size: small;">Background: </span></strong><span style="font-size: small; font-family: Times New Roman,Times New Roman;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;">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, </span></span><em><span style="font-size: small; font-family: Times New Roman,Times New Roman;"><em><span style="font-size: small; font-family: Times New Roman,Times New Roman;">Bacillus persicus </span></em></span></em>
<span style="font-size: small; font-family: Times New Roman,Times New Roman;">from the Aran-Bidgol, Iran. </span>
Methods
<strong><span style="font-size: small;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;">: Purification of enzyme, was carried out by acetone precipitation, ultrafiltration and Q-Sepharose cation exchange chromatography. </span></span></span></strong>
Results
<strong><span style="font-size: small;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;">: 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 </span></span><span style="font-size: small; font-family: Cambria Math,Cambria Math;" lang="ZH-CN"><span style="font-size: small; font-family: Cambria Math,Cambria Math;" lang="ZH-CN">∘</span></span><span style="font-size: small; font-family: Times New Roman,Times New Roman;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;">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. </span></span></span></strong>
Conclusion
<strong><span style="font-size: small;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;">: In the present study we report the purification and characterization of a moderately halophilic α-amylase from a newly isolated </span></span><em><span style="font-size: small; font-family: Times New Roman,Times New Roman;"><em><span style="font-size: small; font-family: Times New Roman,Times New Roman;">Bacillus persicus</span></em></span></em><span style="font-size: small; font-family: Times New Roman,Times New Roman;"><span style="font-size: small; font-family: Times New Roman,Times New Roman;">. 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. </span></span></span></strong>
79
94
http://mbd.modares.ac.ir/browse.php?a_code=A-10-1000-2701&slc_lang=en&sid=8
Shima
Hadipour
Shima
Hadipour
100319475328460064035
100319475328460064035
No
Department of Biology, Payam-e-Noor University, Tehran Branch, Pardis, Iran
Department of Biology, Payam-e-Noor University, Tehran Branch, Pardis, Iran
Hossein
Ghafoori
Hossein
Ghafoori
100319475328460064034
100319475328460064034
Yes
Department of Biology, University of Guilan, Rasht, Iran
Department of Biology, University of Guilan, Rasht, Iran
Nooshin
Sohrabi
Nooshin
Sohrabi
100319475328460064029
100319475328460064029
No
Department of Biology, Payam-e-Noor University, Tehran Branch, Pardis, Iran
Department of Biology, Payam-e-Noor University, Tehran Branch, Pardis, Iran
Maryam
Izaddoust
Maryam
Izaddoust
100319475328460064028
100319475328460064028
No
Department of Biology, University of Guilan, Rasht, Iran
Department of Biology, University of Guilan, Rasht, Iran