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KMID : 0545119990090060861
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Journal of Microbiology and Biotechnology
1999 Volume.9 No. 6 p.861 ~ p.869
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Purification and Characterization of Co2+-Activated Extracellular Metalloprotease from Bacillus sp.JH108
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Jung, Hyun Joo
Kim, Hae Kwon/Kim, Jong Il
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Abstract
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An extracellular protease was purified to homogeneity from the culture supernatant of psychrotrophic bacteria Bacillus sp. JH 108 using procedures including ammonium sulfate fractionation, anion exchange chromatography, gel filtration chromatography, and cation exchange chromatography. The enzyme exhibited a molecular weight of 36kDa, an optimum pH of 8 to 9, and optimum temperature of 60℃. The enzyme preferentially hydrolyzed leucine at the N-terminus of peptides and thus can be classified as an aminopeptidase. It was strongly inhibited by metal chelating agents such as EDTA and 1,10-phenanthroline. The activity lost by EDTA was restored with Zn^2+ or Co^2+. These divalent cations also stimulated the native enzyme. This suggests that the enzyme is a metalloprotease acting as a leucine aminopeptidase.
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