Previous Article | Next Article ![]()
Applied and Environmental Microbiology, August 1998, p. 3023-3024, Vol. 64, No. 8
Department of Chemical and Biochemical
Engineering, University of California, Irvine, California
92697-2575,1 and
Dipartimento di
Genetica e di Biologia dei Microrganismi, Università degli studi
di Milano, 20133 Milan, Italy2
Received 24 February 1998/Accepted 8 June 1998
Toluene/o-xylene monooxygenase (ToMO) from
Pseudomonas stutzeri OX1, which oxidizes toluene and
o-xylene, was examined for its ability to degrade the
environmental pollutants trichloroethylene (TCE), 1,1-dichloroethylene
(1,1-DCE), cis-1,2-DCE, trans-1,2-DCE, chloroform, dichloromethane, phenol, 2,4-dichlorophenol,
2,4,5-trichlorophenol, 2,4,6-trichlorophenol,
2,3,5,6-tetrachlorophenol, and 2,3,4,5,6-pentachlorophenol. Escherichia coli JM109 that expressed ToMO from genes on
plasmid pBZ1260 under control of the lac promoter degraded
TCE (3.3 µM), 1,1-DCE (1.25 µM), and chloroform (6.3 µM) at
initial rates of 3.1, 3.6, and 1.6 nmol/(min · mg of protein),
respectively. Stoichiometric amounts of chloride release were seen,
indicating mineralization (2.6, 1.5, and 2.3 Cl
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Oxidation of Trichloroethylene,
1,1-Dichloroethylene, and Chloroform by Toluene/o-Xylene
Monooxygenase from Pseudomonas stutzeri OX1
atoms per
molecule of TCE, 1,1-DCE, and chloroform, respectively). Thus, the
substrate range of ToMO is extended to include aliphatic chlorinated
compounds.
*
Corresponding author. Present address:
Department of Chemical Engineering, University of Connecticut, Storrs,
CT 06269-3222. Phone: (860) 486-4019. Fax: (860) 486-2959.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»