Abstract
Toluene dioxygenase from Pseudomonas putida F1 has been implicated as an enzyme capable of degrading trichloroethylene. This has now been confirmed with Escherichia coli JM109(pDTG601) that contains the structural genes (todC1C2BA) of toluene dioxygenase under the control of the tac promoter. The extent of trichloroethylene degradation by the recombinant organism depended on the cell concentration and the concentration of trichloroethylene. A linear rate of trichloroethylene degradation was observed with the E. coli recombinant strain. In contrast, P. putida F39/D, a mutant strain of P. putida F1 that does not contain cis-toluene dihydrodiol dehydrogenase, showed a much faster initial rate of trichloroethylene degradation which decreased over time.
MeSH Terms
Biodegradation, Environmental
Chemical Phenomena
Chemistry
Chromatography, Gas
Cloning, Molecular
Escherichia coli/enzymology,genetics
Oxidation-Reduction
Oxygenases/genetics,metabolism
Pseudomonas/enzymology,genetics
Trichloroethylene/metabolism
Chemicals
Trichloroethylene
Oxygenases
toluene dioxygenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Zylstra G J
Department of Microbiology, University of Iowa, Iowa City 52242.
Wackett L P
Gibson D T
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