Yunbo Wu

Nankai University

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Chao Yang

Nankai University

Ping Xu

Shanghai Jiao Tong University

Xiaoqing Xu

Harbin Medical University

Shufang Wang

Nankai University

Hong Jiang

Chinese Academy of Sciences

Hui‐Lei Yu

East China University of Science and Technology

Yulei Dang

Nankai University

Yanping Liu

Ministry of Agriculture and Rural Affairs

Fan Xu

First Affiliated Hospital Zhejiang University

Ruihua Liu

Nankai University

Cooperative Institutions

Nankai University

Chinese Academy of Sciences

Peking University

State Key Laboratory of Medicinal Chemical Biology

Yancheng Third People's Hospital

Hebei Chemical and Pharmaceutical College

Chinese Academy of Medical Sciences & Peking Union Medical College

Nanjing Tech University

Sichuan University

Shanghai Jiao Tong University

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An engineered Pseudomonas putida can simultaneously degrade organophosphates, pyrethroids and carbamates

The Science of The Total Environment (2018)

Ting Gong Xiaoqing Xu Yulei Dang Annie Kong Yunbo Wu

Pseudomonas putida

10.1016/j.scitotenv.2018.02.143

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Citations (90)

Enhanced synthesis of alginate oligosaccharides in Pseudomonas mendocina NK-01 by overexpressing MreB

3 Biotech (2019)

Fan Xu Ting Gong Yunbo Wu Fengjie Zhao Mingqiang Qiao

MreB

10.1007/s13205-019-1873-7

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Citations (7)

Simultaneous hydrolysis of carbaryl and chlorpyrifos by Stenotrophomonas sp. strain YC-1 with surface-displayed carbaryl hydrolase

Scientific Reports (2017)

Chao Yang Xiaoqing Xu Yanping Liu Hong Jiang Yunbo Wu

Many sites are often co-contaminated with multiple pesticides. To date, there are no reports on simultaneous degradation of different classes of pesticides by a natural microorganism. In this work, we aim at constructing a live biocatalyst able to simultaneously hydrolyze carbaryl and chlorpyrifos. For this purpose, carbaryl hydrolase (CH) was displayed on the cell surface of a chlorpyrifos-degrading bacterium Stenotrophomonas sp. strain YC-1 using N- and C-terminal domain of ice nucleation protein (INPNC) from Pseudomonas syringae INA5 as an anchoring motif. The localization of INPNC-CH fusion protein in the outer membrane fraction was demonstrated by cell fractionation followed by Western blot analysis. Surface display of INPNC-CH was further confirmed by proteinase accessibility experiment and immunofluorescence microscope. CH was present in an active form on cell surface without causing any growth inhibition, suggesting that the INP-based display system is a useful tool for surface expression of macromolecular heterologous proteins on the bacterial cell surface. Because surface-displayed CH has free access to pesticides, this bacterium can be used as a whole-cell biocatalyst for efficient hydrolysis of pesticides.

Carbaryl

Stenotrophomonas

Hydrolase

Pseudomonas syringae

10.1038/s41598-017-13788-0

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Citations (9)