Scientific Reports,2017年
Wei Wang, Dian Lei, Yuan Dong, Yee-Chia Yeo, Xiao Gong, Eng Soon Tok
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Scientific Reports,2017年
Guihua Duan, Shanshan Shen, Yuzheng Zhuge, Xiaoping Zou, Yun Wang, Xiaoqi Zhang, Xi Emily Zheng, Bin Zhang, Hongli Yan, Lijuan Xie, Jun Wang, Qianyuan Tang, Wei Wang
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Scientific Reports,2017年
Xiu-Yuan Sun, Wei Wang, Chen Yin, Hui Shen, Yu Zhang, Xiao-Yan Pei, Ya-Nan Gao, Qing Ge
LicenseType:Unknown |
Scientific Reports,2017年
Yilin Tang, Lei Wu, Fengtao Liu, Jian Fei, Jinghui Wang, Jian Wang, Xiaochen Bai, Zishan Wang, Mei Yu, Fang Huang, Wei Wang, Jianliang Ni
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Scientific Reports,2017年
Wei Wang, Guangyi Li, Wentao Wang, Tao Zhang, Ning Li, Xiaodong Wang, Yanting Liu, Aiqin Wang
LicenseType:Unknown |
Scientific Reports,2017年
Lin Lin, Dannong He, Gang Huang, Dongzhi Wei, Wei Wang, Yaling Shen, Xianghai Cai, Wei Wei
LicenseType:Unknown |
Abstract The EstPS1 gene, which encodes a novel carboxylesterase of Pseudomonas synxantha PS1 isolated from oil well-produced water, was cloned and sequenced. EstPS1 has an open reading frame of 1923 bp and encodes the 640-amino acid carboxylesterase (EstPS1), which contains an autotransporter (AT) domain (357–640 amino acids). Homology analysis revealed that EstPS1 shared the highest identity (88%) with EstA from Pseudomonas fluorescens A506 (NCBI database) and belonged to the carboxylesterase family (EC 3.1.1.1). The optimum pH and temperature of recombinant EstPS1 were found to be 8.0 and 60 °C, respectively. EstPS1 showed high thermostability, and the half-lives (T1/2 thermal inactivation) at 60, 70, 80, 90, and 100 °C were 14 h, 2 h, 31 min, 10 min, and 1 min, respectively. To understand the role of the AT domain in carboxylesterase, AT domain-truncated carboxylesterase (EstPS1ΔAT) was generated. EstPS1ΔAT showed a clearly decreased secretion rate, owing to the AT domain strongly improved secretory expression in the heterogeneous system. EstPS1 degraded various pyrethroid pesticides, and hydrolysis efficiencies were dependent on the pyrethroid molecular structure. EstPS1 degraded all the tested pyrethroid pesticides and hydrolysed the p-nitrophenyl esters of medium-short-chain fatty acids, indicating that EstPS1 is an esterase with broad specificity.