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Purification and Characterization of a Cold Alkaline Protease from a Psychrophilic Pseudomonas aeruginosa HY1215

文献类型： 外文期刊

作者： Hao, Jian-Hua 1 ; Sun, Mi 1 ;

作者机构： 1.Chinese Acad Fishery Sci, Minist Agr, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Marine Fisheries, Qingdao 266071, Peoples R China

关键词： Alkaline protease;Antioxygenation;Antisurfactant;Cold adaption

期刊名称：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY （ 影响因子：2.926； 五年影响因子：2.685 ）

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收录情况： SCI

摘要： A novel alkaline protease was purified from Pseudomonas aeruginosa HY1215 using ammonium sulfate, DEAE-Sepharose and Sephacryl S-200 gel filtration chromatographic techniques. The protease had a relative molecular weight of 32.8 KDa by SDS-PAGE, and the optimal temperature and pH for excellent stability and activity were determined as 25 A degrees C and 10.0, respectively. Within the pH range of 7.0-11.0, the protease had a good stability, which could retain more than 80 % of its original activity; in the temperature range of 15-35 A degrees C, the protease had a higher activity, and its activity at 20 A degrees C could amount to 85 % of the maximum activity at 25 A degrees C. Besides, the enzyme activity showed a valuable stability towards several commercially available surfactants (Tween-80, Tween-40, and Triton X-100) and bleaches (H2O2) even when their concentrations ranged up to 2.0 and 1.6 %.

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[1]Identification of Latent Periodicity in Domains of Alkaline Proteases. Ji, Xiaofeng,Sheng, Jun,Wang, Fang,Hao, Jianhua,Wang, Haiying,Sun, Mi,Zhang, Suzhen.

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