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Isolation of an aryloxyphenoxy propanoate (AOPP) herbicide-degrading strain Rhodococcus ruber JPL-2 and the cloning of a novel carboxylesterase gene (feh).

Hongming L, Xu L, Zhaojian G, Fan Y, Dingbin C, Jianchun Z, Jianhong X, Shunpeng L, Qing H - Braz. J. Microbiol. (2015)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Nanjing Agricultural University, College of Life Science, Nanjing Agricultural University, Ministry of Agriculture, Nanjing, China, Key Laboratory of Agricultural Environmental Microbiology, College of Life Science, Nanjing Agricultural University, Ministry of Agriculture, Nanjing, China.

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.

No MeSH data available.


Related in: MedlinePlus

SDS-PAGE analysis of expression of feh gene inEscherichia coli. Lane 1, protein markers; lane 2,purified FeH.
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f04: SDS-PAGE analysis of expression of feh gene inEscherichia coli. Lane 1, protein markers; lane 2,purified FeH.

Mentions: The FeH produced in E. coli BL21(DE3) was purified from crudeextract using Ni-nitrilotriacetic acid affinity chromatography, and the purifiedFeH showed a single band on SDS-PAGE (Figure4). The molecular mass of the denatured enzyme was approximately 39kDa, which coincided with the molecular mass calculated from the amino acidsequence.


Isolation of an aryloxyphenoxy propanoate (AOPP) herbicide-degrading strain Rhodococcus ruber JPL-2 and the cloning of a novel carboxylesterase gene (feh).

Hongming L, Xu L, Zhaojian G, Fan Y, Dingbin C, Jianchun Z, Jianhong X, Shunpeng L, Qing H - Braz. J. Microbiol. (2015)

SDS-PAGE analysis of expression of feh gene inEscherichia coli. Lane 1, protein markers; lane 2,purified FeH.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4507534&req=5

f04: SDS-PAGE analysis of expression of feh gene inEscherichia coli. Lane 1, protein markers; lane 2,purified FeH.
Mentions: The FeH produced in E. coli BL21(DE3) was purified from crudeextract using Ni-nitrilotriacetic acid affinity chromatography, and the purifiedFeH showed a single band on SDS-PAGE (Figure4). The molecular mass of the denatured enzyme was approximately 39kDa, which coincided with the molecular mass calculated from the amino acidsequence.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Nanjing Agricultural University, College of Life Science, Nanjing Agricultural University, Ministry of Agriculture, Nanjing, China, Key Laboratory of Agricultural Environmental Microbiology, College of Life Science, Nanjing Agricultural University, Ministry of Agriculture, Nanjing, China.

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.

No MeSH data available.


Related in: MedlinePlus