{"refrec":{"BRefID":260618,"RR":"<b>Chen, X.-L.; Zhang, Y.-Z.; Gao, P.-J.; Luan, X.-W.</b> (2003). Two different proteases produced by a deep-sea psychrotrophic bacterial strain, <i>Pseudoaltermonas</i> sp. SM9913. <i>Mar. Biol. (Berl.) 143(5)</i>: 989-993. <a href=\"http://dx.doi.org/10.1007/s00227-003-1128-2\" target=\"_blank\">http://dx.doi.org/10.1007/s00227-003-1128-2</a>","BEntID":252637,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>Mar. Biol. (Berl.) 143(5)</i>: 989-993. <a href=\"http://dx.doi.org/10.1007/s00227-003-1128-2\" target=\"_blank\">http://dx.doi.org/10.1007/s00227-003-1128-2</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Chen, X.-L.; Zhang, Y.-Z.; Gao, P.-J.; Luan, X.-W.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Chen, X.-L. <i>et al.</i>","Englishabstract":"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.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Two different proteases produced by a deep-sea psychrotrophic bacterial strain, <i>Pseudoaltermonas</i> sp. 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