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KMID : 0613820050150040657
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Journal of Life Science
2005 Volume.15 No. 4 p.657 ~ p.663
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Purification and Characterization of Bacillus subtilis JS-17 Collagenase
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Lim Kyoung-Suk
Son Shung-Hui
Kang Ho-Young
Jun Hong-Ki
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Abstract
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Collagenases are generally defined as enzymes that are capable of degrading the polypeptide backbone of native collagen under conditions that do not denature the protein. An extracellular collagenase-producing bacterial strain was isolated from kimchi and identified to be Bacillus subtilis JS-17 through morphological, cultural, biochemical characteristics and 16S rDNA sequence analysis. Optimum culture condition of Bacillus subtilis JS-17 for the production of collagenase was 1.5% fructose, 1% yeast extract, 0.5% K₂HPO₄, 0.4% KH₂PO₄, 0.01% MgSO₄ㆍ7H₂O, 0.01% MnSO₄ㆍ4H₂O, 0.1% citrate and 0.1% CaCl₂. The production of collagenase was optimal at 30℃ for 72 hr. A collagenase was isolated from the culture filtrate of Bacillus subtilis JS-17. The enzyme was purified using Amberlite IRA-900 column chromatography, Sephacryl S-300 HR column chromatography and DEAE-Sephadex A-50 column chromatography. The purified collagenase has an specific activity 192.1 units/㎎. The molecular weight of the purified enzyme was estimated to be 28 kDa by SDS-PAGE. The purified collagenase has 100% activity up to 55℃.
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