Identification and characterization of a novel carboxylesterase (FpbH) that hydrolyzes aryloxyphenoxypropionate herbicides
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To identify and characterize a novel aryloxyphenoxypropionate (AOPP) herbicide-hydrolyzing carboxylesterase from Aquamicrobium sp. FPB-1.
A carboxylesterase gene, fpbH, was cloned from Aquamicrobium sp. FPB-1. The gene is 798 bp long and encodes a protein of 265 amino acids. FpbH is smaller than previously reported AOPP herbicide-hydrolyzing carboxylesterases and shares only 21–35% sequence identity with them. FpbH was expressed in Escherichia coli BL21(DE3) and the product was purified by Ni–NTA affinity chromatography. The purified FpbH hydrolyzed a wide range of AOPP herbicides with catalytic efficiency in the order: haloxyfop-P-methyl > diclofop-methyl > fenoxaprop-P-ethyl > quizalofop-P-ethyl > fluazifop-P-butyl > cyhalofop-butyl. The optimal temperature and pH for FpbH activity were 37 °C and 7, respectively.
FpbH is a novel AOPP herbicide-hydrolyzing carboxylesterase; it is a good candidate for mechanistic study of AOPP herbicide-hydrolyzing carboxylesterases and for bioremediation of AOPP herbicide-contaminated environments.
KeywordsAquamicrobium sp. FPB-1 Aryloxyphenoxypropionate herbicide Biodegradation Carboxylesterase FpbH
This work was supported by the National Natural Science Foundation of China (31270157 and 31560033) and the Project of University-Industry Collaboration of Guangdong Province-Ministry (2013B090500017).
Supplementary Fig. 1—Phylogenetic tree based on the 16S rRNA gene sequences of strain FPB-1 and related species.
Supplementary Fig. 2—SDS-PAGE of His-tagged FpbH.
Supplementary Fig. 3—HPLC and tandem mass spectrometry analysis of metabolite generated during fluazifop-P-butyl degradation by the purified FpbH.
Supplementary Fig. 4—Characterization of purified recombinant FpbH.
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