| Summary: | The extracellular crude-proteins of Shewanella baltica OS223 showed about 50-fold higher collagenase activity compared with that of other strains in the screening. The crude-collagenases had maximal activity at 35°C and at pH7, respectively; they were activated by Sr2+ and Ca2+, and strongly inhibited by Chymostatin and EDTA-Na2. The crude-collagenases remained 80% activity after 60min incubation at 30°C and 50% activity after 25min at 40°C. S. baltica OS223, a non-pathogenic strain, grew best at room temperature with the doubling time of 1.6 h. A putative collagenase gene, encoding an extracellular zinc metalloprotease which was classified as peptidase M9A collagenase, was found in its genome. Cloning of the gene into recombinant vector for purification and large-scale production could be done in future and the characters of the collagenases indicated wide potential applications in health care and cosmetic industries.
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