Cold-active serine alkaline protease from the psychrophilic bacterium<Emphasis Type="Italic"> Pseudomonas</Emphasis> strain DY-A: enzyme purification and characterization |
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Authors: | Email author" target="_blank">Runying?ZengEmail author Rui?Zhang Jing?Zhao Nianwei?Lin |
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Institution: | Third Institute of Oceanography, State Oceanic Administration, Daxue Road 178, Xiamen, 361005, Fujian, China. rainz@public.xm.fj.cn |
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Abstract: | An extracellular protease was purified from a deep-sea psychrophilic bacterium strain DY-A which was identified as a Pseudomonas species. The optimal growth and protease-producing temperatures of the strain were all 10 degrees C, and the protease was secreted only at temperatures under 20 degrees C. The enzyme was most active at 40 degrees C and at pH 10.0. It was inhibited by phenylmethyl sulfonylfluoride and diisopropyl fluorophosphate, indicating that it is a serine protease. Chelators such as EDTA, EGTA, 1,10-phenanthroline and 2,2'-bipyridyl produced a decrease of activity. The enzyme was sensitive to denaturing agents such as SDS, urea, and guanidine HCl and resistant to thiol-containing reducing agents such as dithiotreitol. The enzyme was active towards N-succinyl-Ala-Ala-Pro-Phe- p-nitroanilide and N-succinyl-Ala-Ala-Pro-Leu- p-nitroanilide. The native molecular mass of the enzyme determined by native PAGE and SDS-PAGE was 25 kDa. |
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