Purification, characterization, and gene cloning of a cold-adapted thermolysin-like protease from Halobacillus sp SCSIO 20089
[Yang, Jian; Li, Jie; Mai, Zhimao; Tian, Xinpeng; Zhang, Si] Chinese Acad Sci, South China Sea Inst Oceanol, Key Lab Marine Bioresources Sustainable Utilizat, Guangzhou 510301, Guangdong, Peoples R China; Zhang, Si] Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China; zhsimd@scsio.ac.cn
2013
发表期刊JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN1389-1723
卷号115期号:6页码:628-632
摘要Marine sediment is a distinctive habitat of cold enzyme producing bacteria. A protease producing strain Halobacillus sp. SCSIO 20089 was isolated from a marine sediment of South China Sea. Using chromatographic techniques, the extracellular protease was purified to homogeneity from the culture supernatant. The purified protease exhibited maximal activity at 30 degrees C, pH 8.0, and remained more than 20% of its activity at 0 degrees C. Its activation energy was calculated to be 34.4 kJ/mol, suggesting it is a cold-adapted protease. Based on the N-terminal amino acid sequence of the purified enzyme, full gene encoding the enzyme was obtained by combination of degenerate primer PCR and hiTAIL-PCR. The deduced amino acid sequence showed 57% and 52% identity with mesothermal and thermophilic protease in thermolysin family respectively. All these indicate the enzyme is a unique cold-active thermolysin-like protease with potential in both basic research and industrial application areas. (C) 2012, The Society for Biotechnology, japan. All rights reserved.
部门归属LMB
关键词Marine Sediment Enzyme Purification Protease Cold-active Enzyme Genome Walking
学科领域Biotechnology & Applied Microbiology ; Food Science & Technology
资助者This research was supported by National High Technology Research and Development Program of China (863 Program, 2012AA092104), Public Science and Technology Research Funds Projects of Ocean (Grant: 201305018) and National Basic Research Program of China (973 Program) (2010CB833804). ; This research was supported by National High Technology Research and Development Program of China (863 Program, 2012AA092104), Public Science and Technology Research Funds Projects of Ocean (Grant: 201305018) and National Basic Research Program of China (973 Program) (2010CB833804). ; This research was supported by National High Technology Research and Development Program of China (863 Program, 2012AA092104), Public Science and Technology Research Funds Projects of Ocean (Grant: 201305018) and National Basic Research Program of China (973 Program) (2010CB833804). ; This research was supported by National High Technology Research and Development Program of China (863 Program, 2012AA092104), Public Science and Technology Research Funds Projects of Ocean (Grant: 201305018) and National Basic Research Program of China (973 Program) (2010CB833804).
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资助者This research was supported by National High Technology Research and Development Program of China (863 Program, 2012AA092104), Public Science and Technology Research Funds Projects of Ocean (Grant: 201305018) and National Basic Research Program of China (973 Program) (2010CB833804). ; This research was supported by National High Technology Research and Development Program of China (863 Program, 2012AA092104), Public Science and Technology Research Funds Projects of Ocean (Grant: 201305018) and National Basic Research Program of China (973 Program) (2010CB833804). ; This research was supported by National High Technology Research and Development Program of China (863 Program, 2012AA092104), Public Science and Technology Research Funds Projects of Ocean (Grant: 201305018) and National Basic Research Program of China (973 Program) (2010CB833804). ; This research was supported by National High Technology Research and Development Program of China (863 Program, 2012AA092104), Public Science and Technology Research Funds Projects of Ocean (Grant: 201305018) and National Basic Research Program of China (973 Program) (2010CB833804).
WOS记录号WOS:000321026700008
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被引频次:15[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.scsio.ac.cn/handle/344004/11020
专题中科院海洋生物资源可持续利用重点实验室
通讯作者zhsimd@scsio.ac.cn
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[Yang, Jian,Li, Jie,Mai, Zhimao,et al. Purification, characterization, and gene cloning of a cold-adapted thermolysin-like protease from Halobacillus sp SCSIO 20089[J]. JOURNAL OF BIOSCIENCE AND BIOENGINEERING,2013,115(6):628-632.
APA [Yang, Jian.,Li, Jie.,Mai, Zhimao.,Tian, Xinpeng.,Zhang, Si] Chinese Acad Sci, South China Sea Inst Oceanol, Key Lab Marine Bioresources Sustainable Utilizat, Guangzhou 510301, Guangdong, Peoples R China.,...&zhsimd@scsio.ac.cn.(2013).Purification, characterization, and gene cloning of a cold-adapted thermolysin-like protease from Halobacillus sp SCSIO 20089.JOURNAL OF BIOSCIENCE AND BIOENGINEERING,115(6),628-632.
MLA [Yang, Jian,et al."Purification, characterization, and gene cloning of a cold-adapted thermolysin-like protease from Halobacillus sp SCSIO 20089".JOURNAL OF BIOSCIENCE AND BIOENGINEERING 115.6(2013):628-632.
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