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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Characterization of a Novel Butachlor Biodegradation Pathway and Cloning of the Debutoxylase (Dbo) Gene Responsible for Debutoxylation of Butachlor in Bacillus sp hys-1
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Characterization of a Novel Butachlor Biodegradation Pathway and Cloning of the Debutoxylase (Dbo) Gene Responsible for Debutoxylation of Butachlor in Bacillus sp hys-1

机译：新型丁草胺生物降解途径的表征和负责芽孢杆菌hys-1中丁草胺脱丁氧基化的脱丁氧基酶（Dbo）基因的克隆

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Bacillus sp. strain hys-1, which was isolated from active sludge, could degrade >90% butachlor at a concentration of 100 mg/L within 7 days. The present work revealed that strain hys-1 could mineralize butachlor via the following pathway: butachlor was initially metabolized to 2-chloro-N-(2,6-diethylphenyl)-N-methylacetainide by debutoxylation and then transformed to form 2-chloro-N-(2,6-diethylphenyl)acetamide by N-demethylation. Subsequently, it was converted to 2,6-diethylaniline and further mineralized into CO, and H2O. In addition, the catalytic efficiency of crude cell extracts descended as follows: alachlor > acetochlor > butachlor. Furthermore, a novel 744 bp gene responsible for transforming butachlor into 2-chloro-N-(2,6-diethylphenyl)-N-methylacetamidewas cloned from strain hys-1 and the encoding debutoxylase was designated Dbo. Then Dbo was expressed in Escherichia coli BL21 (DE3) and purified using Ni-nitrilotriacetic acid affinity chromatography. Dbo displayed the highest activity against butachlor at pH 6.5 and 30 degrees C. Metal ions played an important role in Dbo activity. To the best of the authors' knowledge, this is the first report that strain hys-1 can mineralize butachlor by a novel metabolic mechanism and the first identification of a gene encoding butachlor debutoxylase.
机译：芽孢杆菌从活性污泥中分离出的菌株hys-1可以在7天内降解100％/ L浓度超过90％的丁草胺。目前的工作表明，菌株hys-1可以通过以下途径使丁草胺矿化：丁草胺首先被新的丁氧基化代谢为2-氯-N-（2,6-二乙基苯基）-N-甲基乙炔，然后转化为2-氯-N-。通过N-去甲基化的N-（2，6-二乙基苯基）乙酰胺。随后，将其转化为2,6-二乙基苯胺，并进一步矿化为CO和H2O。此外，粗细胞提取物的催化效率降低如下：甲草胺>乙草胺>丁草胺。此外，从菌株hys-1中克隆了一个新的744 bp基因，该基因负责将丁草胺转化为2-氯-N-（2,6-二乙基苯基）-N-甲基乙酰胺，编码的脱氧乙氧化酶命名为Dbo。然后，Dbo在大肠杆菌BL21（DE3）中表达，并使用Ni-nitrilotriacetic acid亲和色谱纯化。 Dbo在pH 6.5和30摄氏度下显示出对丁草胺的最高活性。金属离子在Dbo活性中起重要作用。据作者所知，这是首次报道hys-1菌株可以通过新的代谢机制使丁草胺矿化，并且首次鉴定了编码丁草胺丁二酰羟化酶的基因。

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