Xenobiotic Compounds Degradation by Heterologous Expression of a Trametes sanguineus Laccase in Trichoderma atroviride.

Fungal laccases are enzymes that have been studied because of their ability to decolorize and detoxify effluents; they are also used in paper bleaching, synthesis of polymers, bioremediation, etc. In this work we were able to express a laccase from Trametes (Pycnoporus) sanguineus in the filamentous...

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Main Authors: Edgar Balcázar-López, Luz Helena Méndez-Lorenzo, Ramón Alberto Batista-García, Ulises Esquivel-Naranjo, Marcela Ayala, Vaidyanathan Vinoth Kumar, Olivier Savary, Hubert Cabana, Alfredo Herrera-Estrella, Jorge Luis Folch-Mallol
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2016-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4743974?pdf=render
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spelling doaj-0cbdf7dde0ee453b81f758bd5bc3e6af2020-11-24T22:06:49ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01112e014799710.1371/journal.pone.0147997Xenobiotic Compounds Degradation by Heterologous Expression of a Trametes sanguineus Laccase in Trichoderma atroviride.Edgar Balcázar-LópezLuz Helena Méndez-LorenzoRamón Alberto Batista-GarcíaUlises Esquivel-NaranjoMarcela AyalaVaidyanathan Vinoth KumarOlivier SavaryHubert CabanaAlfredo Herrera-EstrellaJorge Luis Folch-MallolFungal laccases are enzymes that have been studied because of their ability to decolorize and detoxify effluents; they are also used in paper bleaching, synthesis of polymers, bioremediation, etc. In this work we were able to express a laccase from Trametes (Pycnoporus) sanguineus in the filamentous fungus Trichoderma atroviride. For this purpose, a transformation vector was designed to integrate the gene of interest in an intergenic locus near the blu17 terminator region. Although monosporic selection was still necessary, stable integration at the desired locus was achieved. The native signal peptide from T. sanguineus laccase was successful to secrete the recombinant protein into the culture medium. The purified, heterologously expressed laccase maintained similar properties to those observed in the native enzyme (Km and kcat and kcat/km values for ABTS, thermostability, substrate range, pH optimum, etc). To determine the bioremediation potential of this modified strain, the laccase-overexpressing Trichoderma strain was used to remove xenobiotic compounds. Phenolic compounds present in industrial wastewater and bisphenol A (an endocrine disruptor) from the culture medium were more efficiently removed by this modified strain than with the wild type. In addition, the heterologously expressed laccase was able to decolorize different dyes as well as remove benzo[α]pyrene and phenanthrene in vitro, showing its potential for xenobiotic compound degradation.http://europepmc.org/articles/PMC4743974?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Edgar Balcázar-López
Luz Helena Méndez-Lorenzo
Ramón Alberto Batista-García
Ulises Esquivel-Naranjo
Marcela Ayala
Vaidyanathan Vinoth Kumar
Olivier Savary
Hubert Cabana
Alfredo Herrera-Estrella
Jorge Luis Folch-Mallol
spellingShingle Edgar Balcázar-López
Luz Helena Méndez-Lorenzo
Ramón Alberto Batista-García
Ulises Esquivel-Naranjo
Marcela Ayala
Vaidyanathan Vinoth Kumar
Olivier Savary
Hubert Cabana
Alfredo Herrera-Estrella
Jorge Luis Folch-Mallol
Xenobiotic Compounds Degradation by Heterologous Expression of a Trametes sanguineus Laccase in Trichoderma atroviride.
PLoS ONE
author_facet Edgar Balcázar-López
Luz Helena Méndez-Lorenzo
Ramón Alberto Batista-García
Ulises Esquivel-Naranjo
Marcela Ayala
Vaidyanathan Vinoth Kumar
Olivier Savary
Hubert Cabana
Alfredo Herrera-Estrella
Jorge Luis Folch-Mallol
author_sort Edgar Balcázar-López
title Xenobiotic Compounds Degradation by Heterologous Expression of a Trametes sanguineus Laccase in Trichoderma atroviride.
title_short Xenobiotic Compounds Degradation by Heterologous Expression of a Trametes sanguineus Laccase in Trichoderma atroviride.
title_full Xenobiotic Compounds Degradation by Heterologous Expression of a Trametes sanguineus Laccase in Trichoderma atroviride.
title_fullStr Xenobiotic Compounds Degradation by Heterologous Expression of a Trametes sanguineus Laccase in Trichoderma atroviride.
title_full_unstemmed Xenobiotic Compounds Degradation by Heterologous Expression of a Trametes sanguineus Laccase in Trichoderma atroviride.
title_sort xenobiotic compounds degradation by heterologous expression of a trametes sanguineus laccase in trichoderma atroviride.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2016-01-01
description Fungal laccases are enzymes that have been studied because of their ability to decolorize and detoxify effluents; they are also used in paper bleaching, synthesis of polymers, bioremediation, etc. In this work we were able to express a laccase from Trametes (Pycnoporus) sanguineus in the filamentous fungus Trichoderma atroviride. For this purpose, a transformation vector was designed to integrate the gene of interest in an intergenic locus near the blu17 terminator region. Although monosporic selection was still necessary, stable integration at the desired locus was achieved. The native signal peptide from T. sanguineus laccase was successful to secrete the recombinant protein into the culture medium. The purified, heterologously expressed laccase maintained similar properties to those observed in the native enzyme (Km and kcat and kcat/km values for ABTS, thermostability, substrate range, pH optimum, etc). To determine the bioremediation potential of this modified strain, the laccase-overexpressing Trichoderma strain was used to remove xenobiotic compounds. Phenolic compounds present in industrial wastewater and bisphenol A (an endocrine disruptor) from the culture medium were more efficiently removed by this modified strain than with the wild type. In addition, the heterologously expressed laccase was able to decolorize different dyes as well as remove benzo[α]pyrene and phenanthrene in vitro, showing its potential for xenobiotic compound degradation.
url http://europepmc.org/articles/PMC4743974?pdf=render
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