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- Title
Expression, purification and functional characterization of a recombinant 2,3-dihydroxybiphenyl-1,2-dioxygenase from Rhodococcus rhodochrous.
- Authors
Xiong, Fei; Shuai, Jian-Jun; Peng, Ri-He; Tian, Yong-Sheng; Zhao, Wei; Yao, Quan-Hong; Xiong, Ai-Sheng
- Abstract
A 2,3-dihydroxybiphenyl (2,3-DHBP) dioxygenase gene from a Rhodococcus sp. strain, named RrbphCI and involved in the degradation of polychlorinated biphenyls (PCBs), was synthesized. RrbphCI was expressed in Escherichia coli and its encoded enzyme was purified. SDS-PAGE analysis indicated that the size of the protein encoded by RrbphCI was about 32 kDa. The activity of the 2,3-DHBP dioxygenase was 82.8 U/mg when the substrate was 2,3-DHBP, with optimum pH 8.0 at 30°C, and optimum temperature was 40°C at pH 8.0. The RrbphCI gene was transformed into Pseudomonas putida strain EG11, to determine the ability of the enzyme to degrade 2,3-DHBP. The wild type EG11 degraded 61.86% of supplied 2,3-DHBP and the transformed EG11 (hosting the RrbphCI gene) utilized 52.68% after 2 min of treatment at 30°C. The overexpressed and purified enzyme was able to degrade 2,3-DHBP. The 2,3-DHBP dioxygenase is a key enzyme in the PCB degradation pathway. RrbphCI and its encoded 2,3-DHBP dioxygenase may have transgenic applications in bioremediation of PCBs.
- Subjects
RHODOCOCCUS; NOCARDIACEAE; POLYCHLORINATED biphenyls; ORGANOCHLORINE compounds; BIOREMEDIATION
- Publication
Molecular Biology Reports, 2011, Vol 38, Issue 7, p4303
- ISSN
0301-4851
- Publication type
Article
- DOI
10.1007/s11033-010-0554-8