| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 17328 | Enzyme and Microbial Technology | 2011 | 8 Pages |
Bacterial degradation of 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene (DDE) has been previously reported, however, its degradation enzyme system has not been characterized. In this study, a DDE-degrading bacterium, Janibacter sp. TYM3221, was isolated and characterized. Transformation of DDE was demonstrated by TYM3211 resting cells grown in LB in the presence and absence of biphenyl. Gas chromatography–mass spectrometry analysis revealed five metabolites of DDE containing a meta-ring cleavage product and 4-chlorobenzoic acid, suggesting that TYM3221 degrades DDE to 4-chlorobenzoic acid via a meta-ring cleavage product. A gene cluster, bphAaAbAcAd, which codes for biphenyl dioxygenase subunits, was cloned from TYM3221. A mutant strain with a bphAa-gene inactivation did not grow on biphenyl, and showed no DDE degradation activity. These results indicate that in strain TYM3221, the bphAa-coded biphenyl dioxygenase is involved not only in the metabolism of biphenyl but also in the degradation of DDE.
► A DDE-degrading bacterium, Janibacter sp. TYM3221 was isolated. ► It degraded DDE via a meta-ring cleavage product to 4-chlorobenzoate. ► The bphAaAbAcAd genes coding biphenyl dioxygenase subunits were cloned. ► A bphAa-gene inactivated mutant did neither grow on biphenyl nor degrade DDE.
