Purification and characterization of an alkaline protease from Bacillus licheniformis NS70

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Purification and characterization of an alkaline protease from Bacillus licheniformis NS70
Young Ok Kim; Jung Kee Lee; Hyung Kwoun Kim; Young Seo Park; Tae Kwang Oh
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 6, no. 1, pp. 1-6
Publication Year
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 isolated 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°C, respectively. The enzyme was stable at alkaline pH range from 6.0 to 12.0, and fairly stable up to 65°C. The enzyme was inhibited by phenylmethylsulfonyl fluoride but not by EDTA and N-ethylmaleimide indicating that the enzyme is serine protease. Enzyme activity was markedly inhibited by Hg2+ and Cu2+. Autolytic phenomena were observed on purified protease NS70 but autolysis was reduced by the addtion of Ca2+ ion or bovine serum albumin.
bacillus licheniformisproteasepurification
Korea Soc-Assoc-Inst
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Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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