Thermotolerant alkaline protease enzyme from Bacillus licheniformis A10: purification,characterization, effects of surfactants and organic solvents |
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Authors: | Bahar Yilmaz Mustafa Ozkan Baltaci |
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Affiliation: | Department of Molecular Biology and Genetics, Faculty of Science, Atatürk University, Erzurum, Turkey |
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Abstract: | In this study, the extracellular thermostable alkaline protease out of A10 strain was purified 1.38-fold with 9.44% efficiency through the ammonium sulfate precipitation-dialysis and DE52 anion exchange chromatography methods. The molecular weight of the enzyme in question along with sodium dodecyl sulfate-polyacrylamide gel electrophoresis was determined to be approximately 40.55?kDa, whereas the optimum pH and temperature ratings were identified as 9.0 and 70?°C, respectively. It was seen that the enzyme had remained stable between pH 7.5–10.5 range, protecting more than 90% of its activity in the wake of 1?h incubation at 60–70?°C. It was also observed that the enzyme enhanced its activity in the presence of Mg2+, Mn2+, K+, while Fe2+, Ni2+, Zn2+, Ag+?and Co2+? decreased the activity. Ca2+, however, did not cause any change in the activity. The enzyme was seen to have been totally inhibited by phenylmethylsulfonyl fluoride, therefore, proved to be a serine alkaline protease. |
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Keywords: | Alkaline protease Bacillus licheniformis characterization purification thermotolerant |
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