1. Isolation of an aryloxyphenoxy propanoate (AOPP) herbicide-degrading strain Rhodococcus ruber JPL-2 and the cloning of a novel carboxylesterase gene (feh).
- Author
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Hongming L, Xu L, Zhaojian G, Fan Y, Dingbin C, Jianchun Z, Jianhong X, Shunpeng L, and Qing H
- Subjects
- Biotransformation, Carboxylesterase chemistry, Cloning, Molecular, Cluster Analysis, DNA, Bacterial chemistry, DNA, Bacterial genetics, DNA, Ribosomal chemistry, DNA, Ribosomal genetics, Molecular Sequence Data, Molecular Weight, Phylogeny, RNA, Ribosomal, 16S genetics, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Rhodococcus enzymology, Rhodococcus genetics, Sequence Analysis, DNA, Soil Microbiology, Substrate Specificity, Triticum growth & development, Carboxylesterase genetics, Carboxylesterase metabolism, Herbicides metabolism, Oxazoles metabolism, Propionates metabolism, Rhodococcus isolation & purification, Rhodococcus metabolism
- Abstract
The strain JPL-2, capable of degrading fenoxaprop-P-ethyl (FE), was isolated from the soil of a wheat field and identified as Rhodococcus ruber. This strain could utilize FE as its sole carbon source and degrade 94.6% of 100 mg L(-1) FE in 54 h. Strain JPL-2 could also degrade other aryloxyphenoxy propanoate (AOPP) herbicides. The initial step of the degradation pathway is to hydrolyze the carboxylic acid ester bond. A novel esterase gene feh, encoding the FE-hydrolyzing carboxylesterase (FeH) responsible for this initial step, was cloned from strain JPL-2. Its molecular mass was approximately 39 kDa, and the catalytic efficiency of FeH followed the order of FE > quizalofop-P-ethyl > clodinafop-propargyl > cyhalofop-butyl > fluazifop-P-butyl > haloxyfop-P-methyl > diclofop-methy, which indicated that the chain length of the alcohol moiety strongly affected the hydrolysis activity of the FeH toward AOPP herbicides.
- Published
- 2015
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