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题名: Purification and characterization of a dehalogenase from Pseudomonas stutzeri DEH130 isolated from the marine sponge Hymeniacidon perlevis
作者: 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
发表日期: 2013-10-01
DOI: 10.1007/s11274-013-1340-2
卷: 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
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.
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
语种: 英语
WOS记录号: WOS:000325035100006
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/137921
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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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

Recommended Citation:
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.
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