云南师范大学丁俊美教授在环境领域一区TOP期刊《Journal of Hazardous Materials》杂志发表题名为《A novel thermostable and salt-tolerant carboxylesterase involved in the initial aerobic degradation pathway for pyrethroids in Glycomyces salinus》的最新研究成果，阐述了一种新的耐热耐盐羧酸酯酶参与盐藻中拟除虫菊酯的厌氧代谢过程。

A novel thermostable and salt-tolerant carboxylesterase involved in the initial aerobic degradation pathway for pyrethroids in Glycomyces salinus.

作者:

Liu, Yan; Tang, Shukun; Wang, Xu; Wang, Xiaoliang; Tang, Xianghua; Wu, Qian; Huang, Zunxi; Ding, JunmeiJournal of hazardous materials

卷451

页131128

DOI10.1016/j.jhazmat.2023.131128

出版时间2023-Mar-02

已索引2023-03-11

文献类型

Journal Article

摘要

The long-term and excessive use of pyrethroid pesticides poses substantial health risks and ecosystem concerns. Several bacteria and fungi have been reported that could degrade pyrethroids. The ester-bond hydrolysis using hydrolases is the initial regulatory metabolic reaction of pyrethroids. However, the thoroughly biochemical characterization of hydrolases involved in this process is limited. Here, a novel carboxylesterase, designated as EstGS1 that could hydrolyze pyrethroid pesticides was characterized. EstGS1 showed low sequence identity (<27.03%) compared to other reported pyrethroid hydrolases and belonged to the hydroxynitrile lyase family that preferred short short-chain acyl esters (C2 to C8). EstGS1 displayed the maximal activity of 213.38U/mg at 60°C and pH 8.5 using pNPC2 as substrate, with Km and Vmax were 2.21±0.72mM and 212.90±41.78M/min, respectively. EstGS1 is a halotolerant esterase and remains stable in 5.1M NaCl. Based on molecular docking and mutational analysis, the catalytic triad of S74-D181-H212 and three other substrate-binding residues I108, S159, and G75 are critical for the enzymatic activity of EstGS1. Additionally, 61 and 40mg/L of deltamethrin and lambda-cyhalothrin were hydrolyzed by 20U of EstGS1 in 4h. This work presents the first report on a pyrethroid pesticide hydrolase characterized from a halophilic actinobacteria.

Copyright © 2023 Elsevier B.V. All rights reserved.

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利益冲突声明

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

关键词

关键词列表BiodegradationCarboxylesteraseEstGS1Glycomyces salinusPyrethroid

地址

Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, China.Yunnan Institute of Microbiology, Key Laboratory for Conservation and Utilization of Bio-Resource, School of Life Sciences, Yunnan University, Kunming 650091, China.Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, China; Key Laboratory of Yunnan Province for Biomass Energy and Environmental Biotechnology, Yunnan Normal University, Kunming 650500, China.Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, China; Key Laboratory of Yunnan Province for Biomass Energy and Environmental Biotechnology, Yunnan Normal University, Kunming 650500, China. Electronic address: djm@ynnu.edu.cn.add 查看更多数据字段

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A novel thermostable and salt-tolerant carboxylesterase involved in the initial .pdf

DOI：10.1016/j.jhazmat.2023.131128

https://www.sciencedirect.com/science/article/pii/S0304389423004107?via%3Dihub