Biodegradation of diphenyl ether herbicide lactofen by Bacillus sp. YS-1 and characterization of two initial degrading esterases

The extensive use of the diphenyl ether herbicide lactofen in recent years has caused serious environmental problems. Therefore, detoxification and elimination of lactofen from the environment are urgently required. In this study, the lactofen-degrading strain Bacillus sp. YS-1 was isolated, which achieved a 97.6% degradation rate of 50 mg/L lactofen within 15 h. The ester bond of lactofen was hydrolyzed, which generated acifluorfen, and then, the nitro group was reduced to the amino group, which generated aminoacifluorfen. Finally, the amino group was acetylated, which formed acetylated aminoacifluorfen, a novel end product in the degradation of lactofen. The toxicity of acetylated aminoacifluorfen to the root and seedling growth of cucumber and sorghum was significantly decreased compared with that of lactofen. The two esterase genes rhoE and rapE, encoding two esterases responsible for lactofen hydrolysis to acifluorfen, were cloned and expressed. The amino acid sequences encoded by rhoE and rapE were 27.78% and 88.21% identical with known esterases, respectively. The optimum temperatures for RhoE and RapE degradation of lactofen were 35 °C and 25 °C, respectively, and both esterases displayed maximal activity at pH 8.0. Both RhoE and RapE prioritized the degradation of (S)-(+)-lactofen, (S)-(−)-quizalofop-ethyl, and (S)-(−)-diclofop-methyl. This study provided the resources of bacterial strain and hydrolyzing enzyme for the removal of lactofen from the environment and the bioremediation of herbicide-contaminated soil.