Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Ufarté, Lisa, Laville, Elisabeth, Duquesne, Sophie, Morgavi, Diego, Robe, Patrick, Klopp, Christophe, Rizzo, Angeline, Pizzut-Serin, Sandra, Potocki-Veronese, Gabrielle
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
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
_version_ 1783286309948751872
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
work_keys_str_mv AT ufartelisa discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics
AT lavilleelisabeth discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics
AT duquesnesophie discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics
AT morgavidiego discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics
AT robepatrick discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics
AT kloppchristophe discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics
AT rizzoangeline discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics
AT pizzutserinsandra discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics
AT potockiveronesegabrielle discoveryofcarbamatedegradingenzymesbyfunctionalmetagenomics