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KMID : 0545119960060010001
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Journal of Microbiology and Biotechnology
1996 Volume.6 No. 1 p.1 ~ p.6
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Purification and Characterization of an Alkaline Protease from Bacillus licheniformis NS70
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KIM, YOUNG-OK
LEE, JUNG-KEE/KIM, HYUNG-KWOUN/PARK, YOUNG-SEO/OH, TAE-KWANG
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Abstract
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A bacterial strain NS70 producing an alkaline protease was isolated from soil samples taken near a hot spring and identified as Bacillus licheniformis by its morphological and physiological properties and cellular fatty acid analysis. The isolates alkaline protease was purified by ammonium sulfate fractionation, DEAE-, CM-, and Phenyl-Sepharose column chromatography. The molecular weight of the purified enzyme was estimated to be 32,000 Da by sodium dodecylsulfate polyacrylamide gel electrophoresis. Its optimal pH and temperature for proteolytic activity against Hammarsten casein were 12 and 65℃, respectively. The enzymes was stable at alkaline pH range from 6.0 to 12.0, and fairly stable up to 65℃. The enzyme was inhibited by phenylmethylsulfonyl fluoride but not EDTA and N-ethylmaleimide indicating that the enzyme is serine protease. Enzyme activity was markedly inhibited by Hg^2+ and Cu^2+. Autolytic phenomena were observed on purified protease NS70 but autolysis was reduced by addition of Ca^2+ ion or bovine serum albumin.
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