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Purification and characterization of a dehalogenase from Pseudomonas stutzeri DEH130 isolated from the marine sponge Hymeniacidon perlevis
Zhang, Jinyou1,2; Cao, Xupeng1; Xin, Yanjuan1; Xue, Song1; Zhang, Wei3
关键词Dehalogenase Pseudomonas Stutzeri Deh130 Purification Mairne Bacterium Marine Sponge
刊名WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
2013-10-01
DOI10.1007/s11274-013-1340-2
29期:10页:1791-1799
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]BACTERIAL 2-HALOACID DEHALOGENASES ; 2-HALOALKANOIC ACID DEHALOGENASE ; SP STRAIN CBS3 ; HALOALKANOATE DEHALOGENASES ; OPPOSITE STEREOSPECIFICITY ; L-2-HALOACID DEHALOGENASE ; ESCHERICHIA-COLI ; MODEL ORGANISM ; CEPACIA MBA4 ; SPEC CBS-3
英文摘要2-haloacid dehalogenases are enzymes that are capable of degrading 2-haloacid compounds. These enzymes are produced by bacteria, but so far they have only been purified and characterized from terrestrial bacteria. The present study describes the purification and characterization of 2-haloacid dehalogenase from the marine bacterium Pseudomonas stutzeri DEH130. P. Stutzeri DEH130 contained two kinds of 2-haloacid dehalogenase (designated as Dehalogenase I and Dehalogenase II) as detected in the crude cell extract after ammonium sulfate fractionation. Both enzymes appeared to exhibit stereo-specificity with respect to substrate. Dehalogenase I was a 109.9-kDa enzyme that preferentially utilized D-2-chloropropropionate and had optimum activity at pH 7.5. Dehalogenase II, which preferentially utilized L-2-chloropropionate, was further purified by ion-exchange chromatography and gel filtration. Purified Dehalogenase II appeared to be a dimeric enzyme with a subunit of 26.0-kDa. It had maximum activity at pH 10.0 and a temperature of 40 A degrees C. Its activity was not inhibited by DTT and EDTA, but strongly inhibited by Cu2+, Zn2+, and Co2+. The K (m) and V (max) for L-2-chloropropionate were 0.3 mM and 23.8 mu mol/min/mg, respectively. Its substrate specificity was limited to short chain mono-substituted 2-halocarboxylic acids, with no activity detected toward fluoropropionate and monoiodoacetate. This is the first report on the purification and characterization of 2-haloacid dehalogenase from a marine bacterium.
语种英语
WOS记录号WOS:000325035100006
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文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/137921
专题中国科学院大连化学物理研究所
作者单位1.Chinese Acad Sci, Marine Bioprod Engn Grp, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Flinders Univ S Australia, Sch Med, Flinders Ctr Marine Bioprod Dev FCMB2, Adelaide, SA 5042, Australia
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Zhang, Jinyou,Cao, Xupeng,Xin, Yanjuan,et al. Purification and characterization of a dehalogenase from Pseudomonas stutzeri DEH130 isolated from the marine sponge Hymeniacidon perlevis[J]. WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY,2013,29(10):1791-1799.
APA Zhang, Jinyou,Cao, Xupeng,Xin, Yanjuan,Xue, Song,&Zhang, Wei.(2013).Purification and characterization of a dehalogenase from Pseudomonas stutzeri DEH130 isolated from the marine sponge Hymeniacidon perlevis.WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY,29(10),1791-1799.
MLA Zhang, Jinyou,et al."Purification and characterization of a dehalogenase from Pseudomonas stutzeri DEH130 isolated from the marine sponge Hymeniacidon perlevis".WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY 29.10(2013):1791-1799.
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