Identification and characterization of a novel carboxylesterase (FpbH) that hydrolyzes aryloxyphenoxypropionate herbicides

Biotechnol Lett. 2017 Apr;39(4):553-560. doi: 10.1007/s10529-016-2276-z. Epub 2017 Jan 5.

Abstract

Objective: To identify and characterize a novel aryloxyphenoxypropionate (AOPP) herbicide-hydrolyzing carboxylesterase from Aquamicrobium sp. FPB-1.

Results: 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.

Conclusions: 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.

Keywords: Aquamicrobium sp. FPB-1; Aryloxyphenoxypropionate herbicide; Biodegradation; Carboxylesterase; FpbH.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Biodegradation, Environmental
  • Carboxylesterase / genetics
  • Carboxylesterase / metabolism*
  • Cell Culture Techniques
  • Chromatography, High Pressure Liquid
  • Cloning, Molecular
  • Enzyme Assays
  • Escherichia coli
  • Herbicides / metabolism*
  • Hydrolysis
  • Models, Molecular
  • Phyllobacteriaceae / enzymology*
  • Phyllobacteriaceae / genetics
  • Propionates / metabolism
  • Tandem Mass Spectrometry

Substances

  • Bacterial Proteins
  • Herbicides
  • Propionates
  • Carboxylesterase