John Wiley & Sons, Ltd.

Development of a highly sensitive assay for enzyme‐mediated reductive degradation of polychlorinated dibenzo‐p‐dioxin

0
The degradation of 2‐chloro‐4,5‐O‐(4′‐methyl‐7′, 8′‐diphenyl)ether (CMDPE), an analog of 2,7‐dichlorodibenzo‐p‐dioxin (2,7‐DCDD), mediated by Geobacillus sp. UZO 3 cell‐free extract was monitored. Ethyl acetate extracts of a complete reaction mixture incubated at 65°C for 18 h were analyzed either by thin layer chromatography (TLC) fractionation coupled with spectrometric detection or by gas chromatography–mass spectrometry (GC‐MS). The reaction product 4‐methylumbelliferone (4MU) was successfully isolated by TLC and visualized by a transilluminator at 450 nm. The 4MU, 4‐chlorophenol, and reaction intermediate 6‐chlorophenoxy‐4‐methylumbelliferone were all successfully detected by GC‐MS. The presence of these compounds suggest that Geobacillus sp. UZO 3 cell‐free extract also catalyzes the reductive cleavage of the diaryl ether bonds of CMDPE in a similar mechanism previously reported in 2,7‐DCDD. In the present study, the authors describe a simple and highly sensitive fluorescent assay for a new dioxin degrading enzyme(s). Environ. Toxicol. Chem. 2012; 31: 1072–1075. © 2012 SETAC

Customer comments

No comments were found for Development of a highly sensitive assay for enzyme‐mediated reductive degradation of polychlorinated dibenzo‐p‐dioxin. Be the first to comment!