Characterization of proteolytic bacteria from the Aleutian deep-sea and their proteases

doi:10.1007/s10295-006-0165-5

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	Characterization of proteolytic bacteria from the Aleutian deep-sea and their proteases
	Xiong, Hairong ; Song, Linsheng ; Xu, Ying ; Tsoi, Man-Yee ; Dobretsov, Sergey ; Qian, Pei-Yuan
	2007
发表期刊	JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
ISSN	1367-5435
卷号	34 期号:1 页码:63-71
文章类型	Article
摘要	Six deep-sea proteolytic bacteria taken from Aleutian margin sediments were screened; one of them produced a cold-adapted neutral halophilic protease. These bacteria belong to Pseudoalteromonas spp., which were identified by the 16S rDNA sequence. Of the six proteases produced, two were neutral cold-adapted proteases that showed their optimal activity at pH 7-8 and at temperature close to 35 degrees C, and the other four were alkaline proteases that showed their optimal activity at pH 9 and at temperature of 40-45 degrees C. The neutral cold-adapted protease E1 showed its optimal activity at a sodium chloride concentration of 2 M, whereas the activity of the other five proteases decreased at elevated sodium chloride concentrations. Protease E1 was purified to electrophoretic homogeneity and its molecular mass was 34 kDa, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight of protease E1 was determined to be 32,411 Da by mass spectrometric analysis. Phenylmethyl sulfonylfluoride (PMSF) did not inhibit the activity of this protease, whereas it was partially inhibited by ethylenediaminetetra-acetic acid sodium salt (EDTA-Na). De novo amino acid sequencing proved protease E1 to be a novel protein.; Six deep-sea proteolytic bacteria taken from Aleutian margin sediments were screened; one of them produced a cold-adapted neutral halophilic protease. These bacteria belong to Pseudoalteromonas spp., which were identified by the 16S rDNA sequence. Of the six proteases produced, two were neutral cold-adapted proteases that showed their optimal activity at pH 7-8 and at temperature close to 35 degrees C, and the other four were alkaline proteases that showed their optimal activity at pH 9 and at temperature of 40-45 degrees C. The neutral cold-adapted protease E1 showed its optimal activity at a sodium chloride concentration of 2 M, whereas the activity of the other five proteases decreased at elevated sodium chloride concentrations. Protease E1 was purified to electrophoretic homogeneity and its molecular mass was 34 kDa, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight of protease E1 was determined to be 32,411 Da by mass spectrometric analysis. Phenylmethyl sulfonylfluoride (PMSF) did not inhibit the activity of this protease, whereas it was partially inhibited by ethylenediaminetetra-acetic acid sodium salt (EDTA-Na). De novo amino acid sequencing proved protease E1 to be a novel protein.
关键词	Deep-sea Bacteria Halophilic Protease Pseudoalteromonas
学科领域	Biotechnology & Applied Microbiology
DOI	10.1007/s10295-006-0165-5
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000242824600009
引用统计	被引频次：31[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/5692
专题	实验海洋生物学重点实验室
作者单位	1.Hong Kong Univ Sci & Technol, Dept Biol, Coastal Marine Lab, Hong Kong, Hong Kong, Peoples R China 2.Chinese Acad Sci, Inst Oceanol, Expt Marine Biol Lab, Qingdao 266071, Peoples R China
推荐引用方式 GB/T 7714	Xiong, Hairong,Song, Linsheng,Xu, Ying,et al. Characterization of proteolytic bacteria from the Aleutian deep-sea and their proteases[J]. JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY,2007,34(1):63-71.
APA	Xiong, Hairong,Song, Linsheng,Xu, Ying,Tsoi, Man-Yee,Dobretsov, Sergey,&Qian, Pei-Yuan.(2007).Characterization of proteolytic bacteria from the Aleutian deep-sea and their proteases.JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY,34(1),63-71.
MLA	Xiong, Hairong,et al."Characterization of proteolytic bacteria from the Aleutian deep-sea and their proteases".JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY 34.1(2007):63-71.

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