| dc.contributor.author |
Sfetsas, CC |
en |
| dc.contributor.author |
Milios, L |
en |
| dc.contributor.author |
Skopelitou, K |
en |
| dc.contributor.author |
Venieraki, A |
en |
| dc.contributor.author |
Todou, R |
en |
| dc.contributor.author |
Flemetakis, E |
en |
| dc.contributor.author |
Katinakis, P |
en |
| dc.contributor.author |
Labrou, NE |
en |
| dc.date.accessioned |
2014-06-06T06:49:13Z |
|
| dc.date.available |
2014-06-06T06:49:13Z |
|
| dc.date.issued |
2009 |
en |
| dc.identifier.issn |
01410229 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/j.enzmictec.2009.07.013 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4499 |
|
| dc.subject |
1,2-Dibromoethane |
en |
| dc.subject |
Bioremediation |
en |
| dc.subject |
Haloalkane dehalogenase |
en |
| dc.subject |
Hydrolase |
en |
| dc.subject |
Rhizobial |
en |
| dc.subject.other |
1,2-Dibromoethane |
en |
| dc.subject.other |
Active site |
en |
| dc.subject.other |
Bradyrhizobium japonicum |
en |
| dc.subject.other |
Catalytic properties |
en |
| dc.subject.other |
Catalytic triad |
en |
| dc.subject.other |
Dehalogenase |
en |
| dc.subject.other |
Early-exponential phase |
en |
| dc.subject.other |
Environmental applications |
en |
| dc.subject.other |
Environmental pollutants |
en |
| dc.subject.other |
Haloalkane dehalogenase |
en |
| dc.subject.other |
Haloalkanes |
en |
| dc.subject.other |
High activity |
en |
| dc.subject.other |
Hydrogen ions |
en |
| dc.subject.other |
Hydrolase |
en |
| dc.subject.other |
Polar compounds |
en |
| dc.subject.other |
Recombinant enzymes |
en |
| dc.subject.other |
Rhizobial |
en |
| dc.subject.other |
Rhodococcus |
en |
| dc.subject.other |
RT-PCR analysis |
en |
| dc.subject.other |
Substrate specificity |
en |
| dc.subject.other |
Biodegradation |
en |
| dc.subject.other |
Bioremediation |
en |
| dc.subject.other |
Biotechnology |
en |
| dc.subject.other |
Escherichia coli |
en |
| dc.subject.other |
Gene expression |
en |
| dc.subject.other |
Hydrogen |
en |
| dc.subject.other |
Pollution |
en |
| dc.subject.other |
Substrates |
en |
| dc.subject.other |
Enzymes |
en |
| dc.subject.other |
1,2 dibromoethane |
en |
| dc.subject.other |
alcohol |
en |
| dc.subject.other |
alkane derivative |
en |
| dc.subject.other |
halide |
en |
| dc.subject.other |
haloalkane dehalogenase |
en |
| dc.subject.other |
halogenoalkane |
en |
| dc.subject.other |
hydrolase |
en |
| dc.subject.other |
proton |
en |
| dc.subject.other |
unclassified drug |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
bioremediation |
en |
| dc.subject.other |
Bradyrhizobium japonicum |
en |
| dc.subject.other |
catalysis |
en |
| dc.subject.other |
controlled study |
en |
| dc.subject.other |
dehalogenation |
en |
| dc.subject.other |
enzyme active site |
en |
| dc.subject.other |
enzyme activity |
en |
| dc.subject.other |
enzyme kinetics |
en |
| dc.subject.other |
enzyme purification |
en |
| dc.subject.other |
enzyme specificity |
en |
| dc.subject.other |
Escherichia coli |
en |
| dc.subject.other |
gene expression |
en |
| dc.subject.other |
heterologous expression |
en |
| dc.subject.other |
hydrolysis |
en |
| dc.subject.other |
molecular cloning |
en |
| dc.subject.other |
molecular model |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
nucleotide sequence |
en |
| dc.subject.other |
reverse transcription polymerase chain reaction |
en |
| dc.subject.other |
Rhodococcus |
en |
| dc.subject.other |
Xanthobacter |
en |
| dc.subject.other |
Bradyrhizobium japonicum |
en |
| dc.subject.other |
Escherichia coli |
en |
| dc.subject.other |
Rhodococcus |
en |
| dc.subject.other |
Xanthobacter |
en |
| dc.title |
Characterization of 1,2-dibromoethane-degrading haloalkane dehalogenase from Bradyrhizobium japonicum USDA110 |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/j.enzmictec.2009.07.013 |
en |
| heal.publicationDate |
2009 |
en |
| heal.abstract |
Haloalkane dehalogenases (DHAs, E.C. 3.8.1.5) are very promising biocatalytic tools for the bioremediation of environmental pollutants which consists of haloalkanes. In the present work, we investigated the DHA from Bradyrhizobium japonicum USDA110 (BjDHA). The dehalogenase activity of B. japonicum USDA110 and RT-PCR analysis revealed that the BjDHA gene expression is induced by 1,2-dibromoethane (1,2-DBE) during the early exponential phase. The BjDHA gene was cloned, expressed in Escherichia coli BL21 (DE3) and characterized. The enzyme catalyzes the irreversible hydrolysis of a variety of haloalkanes to the corresponding alcohol, halide, and a hydrogen ion. The catalytic properties of the recombinant enzyme were investigated and the kinetic parameters (Km, kcat) for a number of substrates were determined. The results showed that the BjDHA displays wide substrate specificity towards haloalkanes and particular high activity towards 1,2-DBE. The enzyme has a different catalytic triad topology compared to the Xanthobacter haloalkane dehalogenase and is more similar to the Rhodococcus enzyme. In addition, consistent with its broad specificity, the BjDHA has a substantially larger and more polar active site cavity compared to the Xanthobacter and Rhodococcus enzymes and as a consequence, BjDHA is able to dehalogenate longer and polar compounds. These properties make this enzyme very promising bioremediation tool for environmental applications. © 2009 Elsevier Inc. All rights reserved. |
en |
| heal.journalName |
Enzyme and Microbial Technology |
en |
| dc.identifier.issue |
5 |
en |
| dc.identifier.volume |
45 |
en |
| dc.identifier.doi |
10.1016/j.enzmictec.2009.07.013 |
en |
| dc.identifier.spage |
397 |
en |
| dc.identifier.epage |
404 |
en |