Rhodococcus sp. strain B1 could degrade 100 mg/L butachlor within 5 days. Butachlor was first hydrolyzed by strain B1 through N-dealkylation, which resulted in the production of butoxymethanol and 2-chloro-
N-(2,6-dimethylphenyl)acetamide. Butoxymethanol could be further degraded and utilized as the carbon source for the growth of strain B1, whereas 2-chloro-
N-(2,6-dimethylphenyl)acetamide could not be degraded further. The hydrolase designated ChlH, responsible for the N-dealkylation of the side chain of butachlor, was purified 185.1-fold to homogeneity with 16.1% recovery. The optimal pH and temperature of ChlH were observed to be 7.0鈥?.5 and 30 掳C, respectively. This enzyme was also able to catalyze the N-dealkylation of other chloroacetamide herbicides; the catalytic efficiency followed the order alachlor > acetochlor >butachlor > pretilachlor, which indicated that the alkyl chain length influenced the N-dealkylation of the chloroacetamide herbicides. This is the first report on the biodegradation of chloroacetamide herbicides at the enzyme level.
Keywords:
butachlor; biodegradation; Rhodococcus sp. B1; protein purification; N-dealkylation