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题名: Purification and characterization of 2-haloacid dehalogenase from marine bacterium Paracoccus sp DEH99, isolated from marine sponge Hymeniacidon perlevis
作者: Zhang Jinyou1, 3;  Xin Yanjuan1;  Cao Xupeng1;  Xue Song1;  Zhang Wei2
关键词: Paracoccus sp. ;  2-Haloacid dehalogenase ;  purification ;  marine bacterium ;  marine sponge
刊名: JOURNAL OF OCEAN UNIVERSITY OF CHINA
发表日期: 2014-02-01
DOI: 10.1007/s11802-014-2357-3
卷: 13, 期:1, 页:91-96
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Physical Sciences
类目[WOS]: Oceanography
研究领域[WOS]: Oceanography
英文摘要: 2-haloacid dehalogenases constitute a group of dehalogenases which are capable of dehalogenating the halogenated organic compounds. So far, the 2-haloacid dehalogenases have been found in many bacteria, but not in Paracoccus genus. In the present study, one enzyme 2-haloacid dehalogenase (designated as Deh99), induced by DL-2-chloropropionate (DL-2-CPA), was purified from the marine bacterium Paracoccus sp. DEH99, isolated from marine sponge Hymeniacidon perlevis. The enzyme of Deh99 was purified to homogeneity by ammonium sulfate precipitation, ion exchange chromatography (Q-Sepharose HP), and Superdex 200 gel filtration chromatography. The molecular weight of Deh99 was estimated to be 25.0 kDa by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE), and 50.0 kDa natively by gel filtration chromatography. The enzyme of Deh99 stereospecifically dehalogenated L-2-CPA to produce D-lactate, with an apparent Michaelis-Menten constant (K (m) ) value of 0.21 mmol L-1 for L-2-CPA. The optimal pH and temperature for Deh99 activity were 10.0 and 40A degrees C, respectively. The enzyme of Deh99 acted on short-carbon-chain 2-haloacids, with the highest activity towards monochloroacetate. The activity of Deh99 was slightly affected by DTT and EDTA, but strongly inhibited by Cu2+ and Zn2+. The enzyme of Deh99 shows unique substrate specificity and inhibitor sensitivities compared to previously characterized 2-haloacid dehalogenases and is the reported one about purified 2-haloacid dehalogenase isolated from the bacteria of Paracoccus genus.
关键词[WOS]: ACID DEHALOGENASE ;  PSEUDOMONAS-PUTIDA ;  ENZYMES ;  GENES ;  STEREOSPECIFICITY ;  PROTEIN
语种: 英语
WOS记录号: WOS:000330312000011
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/145454
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, Dalian Inst Chem Phys, Marine Bioprod Engn Grp, Dalian 116023, Peoples R China
2.Flinders Univ S Australia, Sch Med, Flinders Ctr Marine Bioprod Dev FCMB2, Adelaide, SA 5042, Australia
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China

Recommended Citation:
Zhang Jinyou,Xin Yanjuan,Cao Xupeng,et al. Purification and characterization of 2-haloacid dehalogenase from marine bacterium Paracoccus sp DEH99, isolated from marine sponge Hymeniacidon perlevis[J]. JOURNAL OF OCEAN UNIVERSITY OF CHINA,2014,13(1):91-96.
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