Abstract
A psychrotrophic bacterial strain, Pseudoaltermonas sp. SM9913, was isolated from deep-sea sediment collected at 1,855 m depth. Two proteases produced by Pseudoaltermonas sp. SM9913 were purified, MPC-01 and MCP-02. MCP-01 is a serine protease with a molecular weight of 60.7 kDa. It is cold-adapted with an optimum temperature of 30–35°C. Its K m and E a for the hydrolysis of casein were 0.18% and 39.1 kJ mol−1, respectively. It had low thermostability, and its activity was reduced by 73% after incubation at 40°C for 10 min. MCP-02 is a mesophilic metalloprotease with a molecular weight of 36 kDa. Its optimum temperature for the hydrolysis of casein was 50–55°C. The K m and E a of MCP-02 for the hydrolysis of casein were 0.36% and 59.3 kJ mol−1, respectively. MCP-02 had high thermostability, and its activity was reduced by only 30.5% after incubation at 60°C for 10 min. At low temperatures, Pseudoaltermonas sp. SM9913 mainly produced the psychrophilic protease MCP-01.
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Acknowledgements
The work was supported by the Hi-Tech Research and Development Program of China (No. 2002AA628100) and the National Natural Science Foundation of China (No. 40276047).
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Communicated by O. Kinne, Oldendorf/Luhe
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Chen, XL., Zhang, YZ., Gao, PJ. et al. Two different proteases produced by a deep-sea psychrotrophic bacterial strain, Pseudoaltermonas sp. SM9913. Marine Biology 143, 989–993 (2003). https://doi.org/10.1007/s00227-003-1128-2
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DOI: https://doi.org/10.1007/s00227-003-1128-2