Purification and properties of a collagenolytic protease produced by marine bacteriumVibrio vulnificus CYK279H |
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Authors: | Sung-Il Kang Young-Boo Jang Yeung-Joon Choi Jai-Yul Kong |
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Institution: | (1) Department of Biotechnology & Bioengineering, Pukyong National University, 608-737 Pusan, Korea;(2) Division of Marine Bioscience/Institute of Marine Industry, Gyeongsang National University, 650-160 Gyeongnam, Korea |
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Abstract: | A collagenolytic enzyme, produced byVibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme
from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was estimated
by SDS-PAGE to be approximately 35.0 kDa. The N-terminal sequence of the enzyme was determined as Gly-Asp-Pro-Cys-Met-Pro-Ile-Ile-Asn.
The optimum temperature and pH for the enzyme activity were 35°C and 7.5, respectively. The enzyme activity was stable within
the pH and temperature ranges 6.8∼8.0 and 20∼35°C, respectively. The purified enzyme was strongly activated by Zn2+, Li2+, and Ca2+, but inhibited by Cu2+. In addition, the enzyme was strongly inhibited by 1, 10-phenanthroline and EDTA. The purified enzyme was suggested to be
a neutral metalloprotease. |
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Keywords: | collagenase gelatin metalloprotease purification Vibrio vulnificus |
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