Characterization of a versatile nitrile hydratase of the neonicotinoid thiacloprid-degrading bacterium Ensifer meliloti CGMCC 7333
Author:
Affiliation:
1. Jiangsu Key Laboratory for Microbes and Functional Genomics
2. Jiangsu Engineering and Technology Research Center for Industrialization of Microbial Resources
3. College of Life Science
4. Nanjing Normal University
5. Nanjing 210023
Abstract
The nitrogen-fixing bacterium Ensifer meliloti CGMCC 7333 and its nitrile hydratase (NHase) degrade the neonicotinoid insecticides, thiacloprid (THI) and acetamiprid (ACE), to their corresponding amide metabolites.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2016/RA/C5RA27966F
Reference29 articles.
1. Overview of the Status and Global Strategy for Neonicotinoids
2. Hydroxylation of thiacloprid by bacterium Stenotrophomonas maltophilia CGMCC1.1788
3. Biotransformation of the Neonicotinoid Insecticide Thiacloprid by the Bacterium Variovorax boronicumulans Strain J1 and Mediation of the Major Metabolic Pathway by Nitrile Hydratase
4. Hydrolysis of the neonicotinoid insecticide thiacloprid by the N2-fixing bacterium Ensifer meliloti CGMCC 7333
5. Metabolism of the Neonicotinoid Insecticides Acetamiprid and Thiacloprid by the Yeast Rhodotorula mucilaginosa Strain IM-2
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