Cold-active serine alkaline protease from the psychrophilic bacterium Pseudomonas strain DY-A: enzyme purification and characterization

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	Cold-active serine alkaline protease from the psychrophilic bacterium Pseudomonas strain DY-A: enzyme purification and characterization
	Zeng, RY ; Zhang, R ; Zhao, J ; Lin, NW ; Ceng RY(曾润颖) ; Zhang R(张锐)
刊名	http://dx.doi.org/10.1007/s00792-003-0323-x
	2003-08
英文摘要	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 10degreesC, and the protease was secreted only at temperatures under 20degreesC. The enzyme was most active at 40degreesC 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.
语种	英语
出版者	EXTREMOPHILES
内容类型	期刊论文
源URL	[http://dspace.xmu.edu.cn/handle/2288/90539]
专题	生命科学－已发表论文
推荐引用方式 GB/T 7714	Zeng, RY,Zhang, R,Zhao, J,et al. Cold-active serine alkaline protease from the psychrophilic bacterium Pseudomonas strain DY-A: enzyme purification and characterization[J]. http://dx.doi.org/10.1007/s00792-003-0323-x,2003.
APA	Zeng, RY,Zhang, R,Zhao, J,Lin, NW,曾润颖,&张锐.(2003).Cold-active serine alkaline protease from the psychrophilic bacterium Pseudomonas strain DY-A: enzyme purification and characterization.http://dx.doi.org/10.1007/s00792-003-0323-x.
MLA	Zeng, RY,et al."Cold-active serine alkaline protease from the psychrophilic bacterium Pseudomonas strain DY-A: enzyme purification and characterization".http://dx.doi.org/10.1007/s00792-003-0323-x (2003).