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Discovery of carbamate degrading enzymes by functional metagenomics
Bioremediation of pollutants is a major concern worldwide, leading to the research of new processes to break down and recycle xenobiotics and environment contaminating polymers. Among them, carbamates have a very broad spectrum of uses, such as toxinogenic pesticides or elastomers. In this study, we...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5730166/ https://www.ncbi.nlm.nih.gov/pubmed/29240834 http://dx.doi.org/10.1371/journal.pone.0189201 |
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author | Ufarté, Lisa Laville, Elisabeth Duquesne, Sophie Morgavi, Diego Robe, Patrick Klopp, Christophe Rizzo, Angeline Pizzut-Serin, Sandra Potocki-Veronese, Gabrielle |
author_facet | Ufarté, Lisa Laville, Elisabeth Duquesne, Sophie Morgavi, Diego Robe, Patrick Klopp, Christophe Rizzo, Angeline Pizzut-Serin, Sandra Potocki-Veronese, Gabrielle |
author_sort | Ufarté, Lisa |
collection | PubMed |
description | Bioremediation of pollutants is a major concern worldwide, leading to the research of new processes to break down and recycle xenobiotics and environment contaminating polymers. Among them, carbamates have a very broad spectrum of uses, such as toxinogenic pesticides or elastomers. In this study, we mined the bovine rumen microbiome for carbamate degrading enzymes. We isolated 26 hit clones exhibiting esterase activity, and were able to degrade at least one of the targeted polyurethane and pesticide carbamate compounds. The most active clone was deeply characterized. In addition to Impranil, this clone was active on Tween 20, pNP-acetate, butyrate and palmitate, and on the insecticide fenobucarb. Sequencing and sub-cloning of the best target revealed a novel carboxyl-ester hydrolase belonging to the lipolytic family IV, named CE_Ubrb. This study highlights the potential of highly diverse microbiota such as the ruminal one for the discovery of promiscuous enzymes, whose versatility could be exploited for industrial uses. |
format | Online Article Text |
id | pubmed-5730166 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-57301662017-12-22 Discovery of carbamate degrading enzymes by functional metagenomics Ufarté, Lisa Laville, Elisabeth Duquesne, Sophie Morgavi, Diego Robe, Patrick Klopp, Christophe Rizzo, Angeline Pizzut-Serin, Sandra Potocki-Veronese, Gabrielle PLoS One Research Article Bioremediation of pollutants is a major concern worldwide, leading to the research of new processes to break down and recycle xenobiotics and environment contaminating polymers. Among them, carbamates have a very broad spectrum of uses, such as toxinogenic pesticides or elastomers. In this study, we mined the bovine rumen microbiome for carbamate degrading enzymes. We isolated 26 hit clones exhibiting esterase activity, and were able to degrade at least one of the targeted polyurethane and pesticide carbamate compounds. The most active clone was deeply characterized. In addition to Impranil, this clone was active on Tween 20, pNP-acetate, butyrate and palmitate, and on the insecticide fenobucarb. Sequencing and sub-cloning of the best target revealed a novel carboxyl-ester hydrolase belonging to the lipolytic family IV, named CE_Ubrb. This study highlights the potential of highly diverse microbiota such as the ruminal one for the discovery of promiscuous enzymes, whose versatility could be exploited for industrial uses. Public Library of Science 2017-12-14 /pmc/articles/PMC5730166/ /pubmed/29240834 http://dx.doi.org/10.1371/journal.pone.0189201 Text en © 2017 Ufarté et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Ufarté, Lisa Laville, Elisabeth Duquesne, Sophie Morgavi, Diego Robe, Patrick Klopp, Christophe Rizzo, Angeline Pizzut-Serin, Sandra Potocki-Veronese, Gabrielle Discovery of carbamate degrading enzymes by functional metagenomics |
title | Discovery of carbamate degrading enzymes by functional metagenomics |
title_full | Discovery of carbamate degrading enzymes by functional metagenomics |
title_fullStr | Discovery of carbamate degrading enzymes by functional metagenomics |
title_full_unstemmed | Discovery of carbamate degrading enzymes by functional metagenomics |
title_short | Discovery of carbamate degrading enzymes by functional metagenomics |
title_sort | discovery of carbamate degrading enzymes by functional metagenomics |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5730166/ https://www.ncbi.nlm.nih.gov/pubmed/29240834 http://dx.doi.org/10.1371/journal.pone.0189201 |
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