Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 60, Issue 50, Pages 12238-12244Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf303936j
Keywords
butachlor; biodegradation; Rhodococcus sp B1; protein purification; N-dealkylation
Funding
- Chinese National Natural Science Foundation [31070099, 31000060]
- National Science and Technology Project in Rural Areas of the twelfth five-year-plan [2012AA101403-4]
- Project for Science and Technology of Jiangsu Province [BE201270608]
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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 ChIH, 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 ChIH were observed to be 7.0-7.5 and 30 degrees 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.
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