DICP OpenIR
Purification and characterization of 2-haloacid dehalogenase from marine bacterium Paracoccus sp DEH99, isolated from marine sponge Hymeniacidon perlevis
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
2014-02-01
DOI10.1007/s11802-014-2357-3
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
关键词[WOS]ACID DEHALOGENASE ; PSEUDOMONAS-PUTIDA ; ENZYMES ; GENES ; STEREOSPECIFICITY ; PROTEIN
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.
语种英语
WOS记录号WOS:000330312000011
引用统计
被引频次:8[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/321008/145454
专题中国科学院大连化学物理研究所
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
推荐引用方式
GB/T 7714
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.
APA Zhang Jinyou,Xin Yanjuan,Cao Xupeng,Xue Song,&Zhang Wei.(2014).Purification and characterization of 2-haloacid dehalogenase from marine bacterium Paracoccus sp DEH99, isolated from marine sponge Hymeniacidon perlevis.JOURNAL OF OCEAN UNIVERSITY OF CHINA,13(1),91-96.
MLA Zhang Jinyou,et al."Purification and characterization of 2-haloacid dehalogenase from marine bacterium Paracoccus sp DEH99, isolated from marine sponge Hymeniacidon perlevis".JOURNAL OF OCEAN UNIVERSITY OF CHINA 13.1(2014):91-96.
条目包含的文件
条目无相关文件。
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Zhang Jinyou]的文章
[Xin Yanjuan]的文章
[Cao Xupeng]的文章
百度学术
百度学术中相似的文章
[Zhang Jinyou]的文章
[Xin Yanjuan]的文章
[Cao Xupeng]的文章
必应学术
必应学术中相似的文章
[Zhang Jinyou]的文章
[Xin Yanjuan]的文章
[Cao Xupeng]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。