Two different proteases produced by a deep-sea psychrotrophic bacterial strain,<Emphasis Type="Italic"> Pseudoaltermonas</Emphasis> sp. SM9913

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.Communicated by O. Kinne, Oldendorf/Luhe