1. Identification and characterization of a novel carboxylesterase (FpbH) that hydrolyzes aryloxyphenoxypropionate herbicides
- Author
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Youjian Yang, Jiguo Qiu, Shunpeng Li, Jian He, Cheng-Hong Wang, and Jin-Wei Zheng
- Subjects
Models, Molecular ,0301 basic medicine ,030106 microbiology ,Cell Culture Techniques ,Bioengineering ,Aquamicrobium sp ,medicine.disease_cause ,Applied Microbiology and Biotechnology ,Carboxylesterase ,03 medical and health sciences ,Hydrolysis ,Bacterial Proteins ,Affinity chromatography ,Tandem Mass Spectrometry ,Escherichia coli ,medicine ,Amino Acid Sequence ,Cloning, Molecular ,Gene ,Chromatography, High Pressure Liquid ,Enzyme Assays ,chemistry.chemical_classification ,Herbicides ,Phyllobacteriaceae ,General Medicine ,Sequence identity ,Amino acid ,Biodegradation, Environmental ,030104 developmental biology ,Biochemistry ,chemistry ,Propionates ,Biotechnology - Abstract
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.
- Published
- 2017