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KMID : 0545120130230111554
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Journal of Microbiology and Biotechnology
2013 Volume.23 No. 11 p.1554 ~ p.1559
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Purification and Characterization of Heat-Tolerant Protease Produced by Bacillus polyfermenticus SCD
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Choi Gooi-Hun
Jo Mi-Na
Kim Jin-Man
Kim Cheon-Jei
Kim Kee-Tae
Paik Hyun-Dong
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Abstract
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A protease produced by Bacillus polyfermenticus SCD was purified and characterized as a new detergent material. The protease was purified from supernatant produced by B. polyfermenticus SCD, by ammonium sulfate precipitation, ion-exchange chromatography on a DEAE-Sephadex A-50, and finally gel filtration chromatography on Sephadex G-50. The molecular mass of this enzyme was 44 kDa based on SDS-PAGE. The optimum temperature and pH were 50oC and pH 8.0. The ranges of its stability to the pH and temperature were 7.0 to 9.0 and under 40oC, respectively. The enzyme was highly stable in the presence of the surfactants like Triton X-100 (0.1%), showing a 2-fold increase in its proteolytic activity. However, the enzyme was slightly inhibited by the chelating agent EDTA (1 mM). The enzyme has a maximum activity at 50°C and the activity can be increased by surfactants such as Triton X-100 and Tween 80.
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KEYWORD
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Bacillus polyfermenticus SCD, protease, purification, surfactant, Triton X-100, Tween-80
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