Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes

Review Article.

Detalles Bibliográficos
Autores: Ferrer, Manuel, Bargiela, Rafael, Martínez-Martínez, Mónica, Mir, Jaume, Koch, Rainhard, Golyshina, Olga V., Golyshin, Peter N.
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/129730
Acceso en línea:http://hdl.handle.net/10261/129730
Access Level:acceso abierto
Palabra clave:Biocatalysis
Biotransformations
Esterases
Extremophiles
Lipases
Metagenome
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oai_identifier_str oai:digital.csic.es:10261/129730
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network_name_str España
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dc.title.none.fl_str_mv Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes
title Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes
spellingShingle Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes
Ferrer, Manuel
Biocatalysis
Biotransformations
Esterases
Extremophiles
Lipases
Metagenome
title_short Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes
title_full Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes
title_fullStr Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes
title_full_unstemmed Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes
title_sort Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomes
dc.creator.none.fl_str_mv Ferrer, Manuel
Bargiela, Rafael
Martínez-Martínez, Mónica
Mir, Jaume
Koch, Rainhard
Golyshina, Olga V.
Golyshin, Peter N.
author Ferrer, Manuel
author_facet Ferrer, Manuel
Bargiela, Rafael
Martínez-Martínez, Mónica
Mir, Jaume
Koch, Rainhard
Golyshina, Olga V.
Golyshin, Peter N.
author_role author
author2 Bargiela, Rafael
Martínez-Martínez, Mónica
Mir, Jaume
Koch, Rainhard
Golyshina, Olga V.
Golyshin, Peter N.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv European Commission
Royal Society (UK)
Ministerio de Economía y Competitividad (España)
Biotechnology and Biological Sciences Research Council (UK)
Federal Ministry of Education and Research (Germany)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Biocatalysis
Biotransformations
Esterases
Extremophiles
Lipases
Metagenome
topic Biocatalysis
Biotransformations
Esterases
Extremophiles
Lipases
Metagenome
description Review Article.
publishDate 2015
dc.date.none.fl_str_mv 2015
2016
2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
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dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/129730
url http://hdl.handle.net/10261/129730
dc.language.none.fl_str_mv Inglés
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http://dx.doi.org/10.3109/10242422.2016.1151416
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
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spelling Biodiversity for biocatalysis: A review of the α/β-hydrolase fold superfamily of esterases-lipases discovered in metagenomesFerrer, ManuelBargiela, RafaelMartínez-Martínez, MónicaMir, JaumeKoch, RainhardGolyshina, Olga V.Golyshin, Peter N.BiocatalysisBiotransformationsEsterasesExtremophilesLipasesMetagenomeReview Article.Natural biodiversity undoubtedly inspires biocatalysis research and innovation. Biotransformations of interest also inspire the search for appropriate biocatalysts in nature. Indeed, natural genetic resources have been found to support the hydrolysis and synthesis of not only common but also unusual synthetic scaffolds. The emerging tool of metagenomics has the advantage of allowing straightforward identification of activity directly applicable as biocatalysis. However, new enzymes must not only have outstanding properties in terms of performance but also other properties superior to those of well-established commercial preparations in order to successfully replace the latter. Esterases (EST) and lipases (LIP) from the α/β-hydrolase fold superfamily are among the enzymes primarily used in biocatalysis. Accordingly, they have been extensively examined with metagenomics. Here we provided an updated (October 2015) overview of sequence and functional data sets of 288 EST–LIP enzymes with validated functions that have been isolated in metagenomes and (mostly partially) characterized. Through sequence, biochemical, and reactivity analyses, we attempted to understand the phenomenon of variability and versatility within this group of enzymes and to implement this knowledge to identify sequences encoding EST–LIP which may be useful for biocatalysis. We found that the diversity of described EST–LIP polypeptides was not dominated by a particular type of protein or highly similar clusters of proteins but rather by diverse nonredundant sequences. Purified EST–LIP exhibited a wide temperature activity range of 10–85 °C, although a preferred bias for a mesophilic temperature range (35–40 °C) was observed. At least 60% of the total characterized metagenomics-derived EST–LIP showed outstanding properties in terms of stability (solvent tolerance) and reactivity (selectivity and substrate profile), which are the features of interest in biocatalysis. We hope that, in the future, the search for and utilization of sequences similar to those already encoded and characterized EST–LIP enzymes from metagenomes may be of interest for promoting unresolved biotransformations in the chemical industry. Some examples are discussed in this review.The authors gratefully acknowledge the financial support provided by the European Community project MAMBA (FP7-KBBE-2008-226977), MAGIC-PAH (FP7-KBBE-2009-245226), ULIXES (FP7-KBBE-2010-266473), MicroB3 (FP7-OCEAN.2011-2-287589), KILL-SPILL (FP7-KBBE-2012-312139) and Royal Society UK-Russia Exchange Grant (IE130218). We thank EU Horizon 2020 Program for the support of the Project INMARE H2020-BG-2014-2634486. This work was further funded by grants BIO2011-25012,PCIN-2014-107 and BIO2014-54494-R from the Spanish Ministry of Economy and Competitiveness. The present investigation was funded by the Spanish Ministry of Economy and Competitiveness, the UK Biotechnology and Biological Sciences Research Council (BBSRC) and the German Federal Ministry of Education and Research (BMBF) within the ERA NET-IB2 program, grant number ERA-IB-14-030. The authors gratefully acknowledge the financial support provided by the European Regional Development Fund (ERDF).Peer reviewedTaylor & FrancisEuropean CommissionRoyal Society (UK)Ministerio de Economía y Competitividad (España)Biotechnology and Biological Sciences Research Council (UK)Federal Ministry of Education and Research (Germany)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201620162015info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/129730reponame:DIGITAL.CSIC. 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