Biodegradation of fenoxaprop-P-ethyl (FE) by Acinetobacter sp. strain DL-2 and cloning of FE hydrolase gene afeH

Weiliang Dong; Sheng Jiang; Kaiwen Shi; Fei Wang; Shuhuan Li; Jie Zhou; Fei Huang; Yicheng Wang; Yuxiao Zheng; Ying Hou; Yan Huang; Zhongli Cui

doi:10.1016/j.biortech.2015.03.039

Biodegradation of fenoxaprop-P-ethyl (FE) by Acinetobacter sp. strain DL-2 and cloning of FE hydrolase gene afeH

Weiliang Dong, Sheng Jiang, Kaiwen Shi, Fei Wang, Shuhuan Li, Jie Zhou, Fei Huang, Yicheng Wang, Yuxiao Zheng, Ying Hou, Yan Huang, Zhongli Cui

Research output: Contribution to journal › Article › peer-review

46 Scopus citations

Abstract

Fenoxaprop-P-ethyl (FE) is widely used as a post-emergence aryloxyphenoxy propionate (AOPP) herbicide in agriculture. An efficient FE-degrading strain DL-2 was isolated from the enrichment culture and identified as Acinetobacter sp. and the metabolite fenoxaprop acid (FA) was identified by HPLC/MS analysis. The strain DL-2 could also degrade a wide range of other AOPP herbicides. A novel FE hydrolase esterase gene afeH was cloned from strain DL-2 and functionally expressed in Escherichia coli BL21(DE3). The specific activities of recombinant AfeH was 216.39Umg^-1 for FE with Km and Vmax values of 0.82μM and 7.94μmolmin^-1mg^-1. AfeH could also hydrolyze various AOPP herbicides, p-nitrophenyl esters and triglycerides. The optimal pH and temperature for recombinant AfeH were 9.0 and 50°C, respectively; the enzyme was activated by Co²⁺ and inhibited by Ca²⁺, Zn²⁺, Ba²⁺. AfeH was inhibited strongly by phenylmethylsulfonyl and SDS and weakly by dimethyl sulfoxide.

Original language	English
Pages (from-to)	114-121
Number of pages	8
Journal	Bioresource Technology
Volume	186
DOIs	https://doi.org/10.1016/j.biortech.2015.03.039
State	Published - 1 Jun 2015
Externally published	Yes

Keywords

Acinetobacter sp
AfeH
Biodegradation
Fenoxaprop-P-ethyl
Metabolic pathway

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.biortech.2015.03.039

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title = "Biodegradation of fenoxaprop-P-ethyl (FE) by Acinetobacter sp. strain DL-2 and cloning of FE hydrolase gene afeH",

abstract = "Fenoxaprop-P-ethyl (FE) is widely used as a post-emergence aryloxyphenoxy propionate (AOPP) herbicide in agriculture. An efficient FE-degrading strain DL-2 was isolated from the enrichment culture and identified as Acinetobacter sp. and the metabolite fenoxaprop acid (FA) was identified by HPLC/MS analysis. The strain DL-2 could also degrade a wide range of other AOPP herbicides. A novel FE hydrolase esterase gene afeH was cloned from strain DL-2 and functionally expressed in Escherichia coli BL21(DE3). The specific activities of recombinant AfeH was 216.39Umg-1 for FE with Km and Vmax values of 0.82μM and 7.94μmolmin-1mg-1. AfeH could also hydrolyze various AOPP herbicides, p-nitrophenyl esters and triglycerides. The optimal pH and temperature for recombinant AfeH were 9.0 and 50°C, respectively; the enzyme was activated by Co2+ and inhibited by Ca2+, Zn2+, Ba2+. AfeH was inhibited strongly by phenylmethylsulfonyl and SDS and weakly by dimethyl sulfoxide.",

keywords = "Acinetobacter sp, AfeH, Biodegradation, Fenoxaprop-P-ethyl, Metabolic pathway",

author = "Weiliang Dong and Sheng Jiang and Kaiwen Shi and Fei Wang and Shuhuan Li and Jie Zhou and Fei Huang and Yicheng Wang and Yuxiao Zheng and Ying Hou and Yan Huang and Zhongli Cui",

note = "Publisher Copyright: {\textcopyright} 2015.",

year = "2015",

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doi = "10.1016/j.biortech.2015.03.039",

language = "英语",

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T1 - Biodegradation of fenoxaprop-P-ethyl (FE) by Acinetobacter sp. strain DL-2 and cloning of FE hydrolase gene afeH

AU - Dong, Weiliang

AU - Jiang, Sheng

AU - Shi, Kaiwen

AU - Wang, Fei

AU - Li, Shuhuan

AU - Zhou, Jie

AU - Huang, Fei

AU - Wang, Yicheng

AU - Zheng, Yuxiao

AU - Hou, Ying

AU - Huang, Yan

AU - Cui, Zhongli

PY - 2015/6/1

Y1 - 2015/6/1

N2 - Fenoxaprop-P-ethyl (FE) is widely used as a post-emergence aryloxyphenoxy propionate (AOPP) herbicide in agriculture. An efficient FE-degrading strain DL-2 was isolated from the enrichment culture and identified as Acinetobacter sp. and the metabolite fenoxaprop acid (FA) was identified by HPLC/MS analysis. The strain DL-2 could also degrade a wide range of other AOPP herbicides. A novel FE hydrolase esterase gene afeH was cloned from strain DL-2 and functionally expressed in Escherichia coli BL21(DE3). The specific activities of recombinant AfeH was 216.39Umg-1 for FE with Km and Vmax values of 0.82μM and 7.94μmolmin-1mg-1. AfeH could also hydrolyze various AOPP herbicides, p-nitrophenyl esters and triglycerides. The optimal pH and temperature for recombinant AfeH were 9.0 and 50°C, respectively; the enzyme was activated by Co2+ and inhibited by Ca2+, Zn2+, Ba2+. AfeH was inhibited strongly by phenylmethylsulfonyl and SDS and weakly by dimethyl sulfoxide.

AB - Fenoxaprop-P-ethyl (FE) is widely used as a post-emergence aryloxyphenoxy propionate (AOPP) herbicide in agriculture. An efficient FE-degrading strain DL-2 was isolated from the enrichment culture and identified as Acinetobacter sp. and the metabolite fenoxaprop acid (FA) was identified by HPLC/MS analysis. The strain DL-2 could also degrade a wide range of other AOPP herbicides. A novel FE hydrolase esterase gene afeH was cloned from strain DL-2 and functionally expressed in Escherichia coli BL21(DE3). The specific activities of recombinant AfeH was 216.39Umg-1 for FE with Km and Vmax values of 0.82μM and 7.94μmolmin-1mg-1. AfeH could also hydrolyze various AOPP herbicides, p-nitrophenyl esters and triglycerides. The optimal pH and temperature for recombinant AfeH were 9.0 and 50°C, respectively; the enzyme was activated by Co2+ and inhibited by Ca2+, Zn2+, Ba2+. AfeH was inhibited strongly by phenylmethylsulfonyl and SDS and weakly by dimethyl sulfoxide.

KW - Acinetobacter sp

KW - AfeH

KW - Biodegradation

KW - Fenoxaprop-P-ethyl

KW - Metabolic pathway

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ER -

Biodegradation of fenoxaprop-P-ethyl (FE) by Acinetobacter sp. strain DL-2 and cloning of FE hydrolase gene afeH

Abstract

Keywords

UN SDGs

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