Purification and characterization of a dehalogenase from Pseudomonas stutzeri DEH130 isolated from the marine sponge Hymeniacidon perlevis
文献类型:期刊论文
作者 | Zhang, Jinyou1,2; Cao, Xupeng1; Xin, Yanjuan1; Xue, Song1; Zhang, Wei3 |
刊名 | world journal of microbiology & biotechnology |
出版日期 | 2013-10-01 |
卷号 | 29期号:10页码:1791-1799 |
关键词 | Dehalogenase Pseudomonas stutzeri DEH130 Purification Mairne bacterium Marine sponge |
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. |
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 |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000325035100006 |
公开日期 | 2015-11-10 |
源URL | [http://159.226.238.44/handle/321008/137921] |
专题 | 大连化学物理研究所_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 |
推荐引用方式 GB/T 7714 | 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. |
入库方式: OAI收割
来源:大连化学物理研究所
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