Rio Tinto as a niche for acidophilus enzymes of industrial relevance

Lignocellulosic residues are amongst the most abundant waste products on Earth. Therefore, there is an increasing interest in the utilization of these residues for bioethanol production and for biorefineries to produce compounds of industrial interest. Enzymes that breakdown cellulose and hemicellul...

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Autores: Daddaoua, Abdelali, Álvarez, C., Oggerin, Monike, Rodríguez, N., Duque, Estrella, Amils, Ricardo, Armengaud, J., Segura, Ana, Ramos, Juan L.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/335573
Acceso en línea:http://hdl.handle.net/10261/335573
Access Level:acceso abierto
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spelling Rio Tinto as a niche for acidophilus enzymes of industrial relevanceDaddaoua, AbdelaliÁlvarez, C.Oggerin, MonikeRodríguez, N.Duque, EstrellaAmils, RicardoArmengaud, J.Segura, AnaRamos, Juan L.Lignocellulosic residues are amongst the most abundant waste products on Earth. Therefore, there is an increasing interest in the utilization of these residues for bioethanol production and for biorefineries to produce compounds of industrial interest. Enzymes that breakdown cellulose and hemicellulose into oligomers and monosaccharides are required in these processes and cellulolytic enzymes with optimum activity at a low pH area are desirable for industrial processes. Here, we explore the fungal biodiversity of Rıo Tinto, the largest acidic ecosystem on Earth, as far as the secretion of cellulolytic enzymes is concerned. Using colorimetric and industrial substrates, we show that a high proportion of the fungi present in this extremophilic environment secrete a wide range of enzymes that are able to hydrolyze cellulose and hemicellulose at acidic pH (4.5–5). Shotgun proteomic analysis of the secretomes of some of these fungi has identified different cellulases and hemicellulolytic enzymes as well as a number of auxiliary enzymes. Supplementation of pre-industrial cocktails from Myceliophtora with Rio Tinto secretomes increased the amount of monosaccharides released from corn stover or sugar cane straw. We conclude that the Rio Tinto fungi display a good variety of hydrolytic enzymes with high industrial potential.Consejo Superior de Investigaciones Científicas, Grant/Award Number: PTI- SusPlast+ ref 2021 AEP084; European Union, Grant/Award Number: FEDER funds; Ministerio de Ciencia e Innovación, Grant/Award Number: RTI2018-094370- B- I00John Wiley & SonsMinisterio de Ciencia e Innovación (España)European CommissionConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2023202320232023info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/335573reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-094370-B-I00http://dx.doi.org/10.1111/1751-7915.14192Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3355732026-05-22T06:33:51Z
dc.title.none.fl_str_mv Rio Tinto as a niche for acidophilus enzymes of industrial relevance
title Rio Tinto as a niche for acidophilus enzymes of industrial relevance
spellingShingle Rio Tinto as a niche for acidophilus enzymes of industrial relevance
Daddaoua, Abdelali
title_short Rio Tinto as a niche for acidophilus enzymes of industrial relevance
title_full Rio Tinto as a niche for acidophilus enzymes of industrial relevance
title_fullStr Rio Tinto as a niche for acidophilus enzymes of industrial relevance
title_full_unstemmed Rio Tinto as a niche for acidophilus enzymes of industrial relevance
title_sort Rio Tinto as a niche for acidophilus enzymes of industrial relevance
dc.creator.none.fl_str_mv Daddaoua, Abdelali
Álvarez, C.
Oggerin, Monike
Rodríguez, N.
Duque, Estrella
Amils, Ricardo
Armengaud, J.
Segura, Ana
Ramos, Juan L.
author Daddaoua, Abdelali
author_facet Daddaoua, Abdelali
Álvarez, C.
Oggerin, Monike
Rodríguez, N.
Duque, Estrella
Amils, Ricardo
Armengaud, J.
Segura, Ana
Ramos, Juan L.
author_role author
author2 Álvarez, C.
Oggerin, Monike
Rodríguez, N.
Duque, Estrella
Amils, Ricardo
Armengaud, J.
Segura, Ana
Ramos, Juan L.
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
European Commission
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description Lignocellulosic residues are amongst the most abundant waste products on Earth. Therefore, there is an increasing interest in the utilization of these residues for bioethanol production and for biorefineries to produce compounds of industrial interest. Enzymes that breakdown cellulose and hemicellulose into oligomers and monosaccharides are required in these processes and cellulolytic enzymes with optimum activity at a low pH area are desirable for industrial processes. Here, we explore the fungal biodiversity of Rıo Tinto, the largest acidic ecosystem on Earth, as far as the secretion of cellulolytic enzymes is concerned. Using colorimetric and industrial substrates, we show that a high proportion of the fungi present in this extremophilic environment secrete a wide range of enzymes that are able to hydrolyze cellulose and hemicellulose at acidic pH (4.5–5). Shotgun proteomic analysis of the secretomes of some of these fungi has identified different cellulases and hemicellulolytic enzymes as well as a number of auxiliary enzymes. Supplementation of pre-industrial cocktails from Myceliophtora with Rio Tinto secretomes increased the amount of monosaccharides released from corn stover or sugar cane straw. We conclude that the Rio Tinto fungi display a good variety of hydrolytic enzymes with high industrial potential.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/335573
url http://hdl.handle.net/10261/335573
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-094370-B-I00
http://dx.doi.org/10.1111/1751-7915.14192

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv John Wiley & Sons
publisher.none.fl_str_mv John Wiley & Sons
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
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