Cometabolic transformation of cis-1,2-dichloroethylene and cis-1,2-dichloroethylene epoxide by a butane-grown mixed culture

• Published in: Water Science & Technology Vol. 52; no. 8; pp. 125 - 131
• Main Authors: KIM, Y, SEMPRINI, L
• Format: Conference Proceeding Journal Article
• Language: English
• Published: Oxford Pergamon 01.01.2005; IWA Publishing
• Subjects: Acetylene; Acetylene - toxicity; Air. Soil. Water. Waste. Feeding; Applied sciences; Biological and medical sciences; Biotransformation - drug effects; Butane; Butane monooxygenase; Butanes; Chlorides; Chlorides - metabolism; Chlorides - toxicity; Culture; Dechlorination; Dichloroethylenes - metabolism; Environment. Living conditions; Enzymes; Epoxy Compounds - metabolism; Exact sciences and technology; Kinetics; Mass Spectrometry; Mass spectroscopy; Medical sciences; Mercuric chloride; Mercury compounds; Mixed culture; Mixed Function Oxygenases - metabolism; Pollution; Public health. Hygiene; Public health. Hygiene-occupational medicine; Ratios; Washington; Water Microbiology; Water Pollutants, Chemical - metabolism; Water treatment and pollution; Washington
• ISBN: 184339555X; 9781843395553
• ISSN: 0273-1223; 1996-9732
• DOI: 10.2166/wst.2005.0242

Aerobic cometabolism of cis-1,2-dichloroethylene (c-DCE) by a butane-grown mixed culture was evaluated in batch kinetic tests. The transformation of c-DCE resulted in the coincident generation of c-DCE epoxide. Chloride release studies showed approximately 75% oxidative dechlorination of c-DCE. Mass spectrometry confirmed the presence of a compound with mass-to-charge-fragment ratios of 112, 83, 48, and 35. These values are in agreement with the spectra of chemically synthesized c-DCE epoxide. The transformation of c-DCE required O2, was inhibited by butane and was inactivated by acetylene (a known monooxygenase inactivator), indicating that a butane monooxygenase enzyme was likely involved in the transformation of c-DCE. This study showed c-DCE epoxide was biologically transformed, likely by a butane monooxygenase enzyme. c-DCE epoxide transformation was inhibited by both acetylene and c-DCE indicating a monooxygenase enzyme was involved. The epoxide transformation was also stopped when mercuric chloride (HgCl2) was added as a biological inhibitor, further support a biological transformation. To our knowledge this is the first report of the biological transform c-DCE epoxide by a butane-grown culture.