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
KeywordParacoccus Sp. 2-haloacid Dehalogenase Purification Marine Bacterium Marine Sponge
Source PublicationJOURNAL OF OCEAN UNIVERSITY OF CHINA
2014-02-01
DOI10.1007/s11802-014-2357-3
Volume13Issue:1Pages:91-96
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectOceanography
WOS Research AreaOceanography
WOS KeywordACID DEHALOGENASE ; PSEUDOMONAS-PUTIDA ; ENZYMES ; GENES ; STEREOSPECIFICITY ; PROTEIN
Abstract2-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.
Language英语
WOS IDWOS:000330312000011
Citation statistics
Cited Times:11[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/145454
Collection中国科学院大连化学物理研究所
Affiliation1.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
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.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Zhang Jinyou]'s Articles
[Xin Yanjuan]'s Articles
[Cao Xupeng]'s Articles
Baidu academic
Similar articles in Baidu academic
[Zhang Jinyou]'s Articles
[Xin Yanjuan]'s Articles
[Cao Xupeng]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Zhang Jinyou]'s Articles
[Xin Yanjuan]'s Articles
[Cao Xupeng]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.