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KMID : 0613820060160020245
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Journal of Life Science
2006 Volume.16 No. 2 p.245 ~ p.252
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Purification and Characterization of Collagenase Produced by Staphylococcus aureus JJ-11 Isolated from the Human Skin
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Lee Jin-Kyoung
Kim Hae-Nam
Kang Ho-Young
Jun Hong-Ki
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Abstract
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A bacterial strain, identified as Staphylococcus aureus JJ-11, producing collagenase was isolated out of 40 persons having skin troubles. S. aureus JJ-11 produced collagenase optimally in the media containing 1.5%(w/v) gelatin, 1%(w/v) yeast extract, 0.4%(w/v) K₂HPO₄, 0.005%(w/v) NiSO₄ㆍ6H₂O at 37℃ for 18 hrs. The collagenase produced by Staphylococcus aureus JJ-11 was purified at 6.66-folds purity through application of chromatography with Amberlite IRA-900 and Sephacryl S-300 HR columns. The molecular weight of the partially purified enzyme was estimated to be 62 kDa by SDS-PAGE. The protein exhibited optimum enzymatic activity at pH 7.0, and showed a stable activity at pH 4-8. The optimum temperature for collagenase was at 37℃, and activity was maintained upto 40℃. The enzyme activity was slightly elevated in the presence of divalents such as, Fe2+, Co2+ and Ba2+. However, the activity was inhibited in the presence of Sr2+ or Hg2+. The inhibition of activity by O-phenanthroline and EDTA suggested that the enzyme may contain metal which is required for activity. The enzyme showed the highest activity when insoluble collagen (type Ⅰ) was used as a substrate.
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KEYWORD
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Collagen, collagenase, purification, Staphylococcus aureus
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