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Structural and functional analysis of a low-temperature-active alkaline esterase from South China Sea marine sediment microbial metagenomic library
Hu, Yongfei1,2,3; Liu, Yinghui4; Li, Jing1,2; Feng, Yanbin4; Lu, Na1,2; Zhu, Baoli1,2,3; Xue, Song4
关键词Marine Sediment Fosmid Library Esterase Low-temperature Active Crystal Structure
刊名JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
2015-11-01
DOI10.1007/s10295-015-1653-2
42期:11页:1449-1461
收录类别SCI
文章类型Article
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biotechnology & Applied Microbiology
研究领域[WOS]Biotechnology & Applied Microbiology
关键词[WOS]ENVIRONMENTAL DNA LIBRARIES ; INDUSTRIAL APPLICATIONS ; UNCULTURED BACTERIA ; LIPOLYTIC ENZYMES ; ESCHERICHIA-COLI ; LIPASE ; IDENTIFICATION ; GENES ; FAMILY ; MICROORGANISMS
英文摘要A low-temperature-active alkaline esterase, Est12, from a marine sediment metagenomic fosmid library was identified. Est12 prefers short- and middle-chain p-nitrophenol esters as substrate with optimum temperature and pH value of 50 A degrees C and 9.0, respectively, and nearly 50 % of maximum activity retained at 5 A degrees C. The hydrolysis activity of Est12 was stable at 40 A degrees C. Ca2+ especially activated the activity of Est12 to about 151 % of the control. DEPC and PMSF inhibited the activity of Est12 to 34 and 25 %, respectively. In addition, Est12 was more tolerable to methanol compared to other organic solvents tested. The crystal structure of Est12 at 1.39 resolution showed that the cap domain which is composed of an alpha-helix and a flexible region resulted in a relatively wide spectrum of substrate, with p-nitrophenol caproate as the preferred one. Furthermore, the flexible cap domain and the high percentage of Gly, Ser, and Met may play important roles in the adaptation of Est12 to low temperature.
语种英语
WOS记录号WOS:000362964900003
引用统计
被引频次:4[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/146600
专题中国科学院大连化学物理研究所
作者单位1.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China
2.Beijing Key Lab Microbial Drug Resistance & Resis, Beijing 100101, Peoples R China
3.Zhejiang Univ, Coll Med, Affiliated Hosp 1, Collaborat Innovat Ctr Diag & Treatment Infect Di, Hangzhou 310006, Zhejiang, Peoples R China
4.Chinese Acad Sci, Dalian Inst Chem Phys, Marine Bioengn Grp, Dalian 116023, Peoples R China
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Hu, Yongfei,Liu, Yinghui,Li, Jing,et al. Structural and functional analysis of a low-temperature-active alkaline esterase from South China Sea marine sediment microbial metagenomic library[J]. JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY,2015,42(11):1449-1461.
APA Hu, Yongfei.,Liu, Yinghui.,Li, Jing.,Feng, Yanbin.,Lu, Na.,...&Xue, Song.(2015).Structural and functional analysis of a low-temperature-active alkaline esterase from South China Sea marine sediment microbial metagenomic library.JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY,42(11),1449-1461.
MLA Hu, Yongfei,et al."Structural and functional analysis of a low-temperature-active alkaline esterase from South China Sea marine sediment microbial metagenomic library".JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY 42.11(2015):1449-1461.
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