Journal
BIOTECHNOLOGY LETTERS
Volume 39, Issue 4, Pages 553-560Publisher
SPRINGER
DOI: 10.1007/s10529-016-2276-z
Keywords
Aquamicrobium sp FPB-1; Aryloxyphenoxypropionate herbicide; Biodegradation; Carboxylesterase; FpbH
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Funding
- National Natural Science Foundation of China [31270157, 31560033]
- Project of University-Industry Collaboration of Guangdong Province-Ministry [2013B090500017]
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Objective To identify and characterize a novel ary-loxyphenoxypropionate (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 degrees 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.
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