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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
Source PublicationJOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN1389-1723
Volume115Issue:6Pages:628-632
AbstractMarine 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.
DepartmentLMB
KeywordMarine Sediment Enzyme Purification Protease Cold-active Enzyme Genome Walking
Subject AreaBiotechnology & Applied Microbiology ; Food Science & Technology
Funding OrganizationThis 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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Language英语
Funding OrganizationThis 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 IDWOS:000321026700008
Citation statistics
Cited Times:19[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.scsio.ac.cn/handle/344004/11020
Collection中科院海洋生物资源可持续利用重点实验室
Corresponding Authorzhsimd@scsio.ac.cn
Recommended Citation
GB/T 7714		 [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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