Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea

The goal of this study is the selective oxyfunctionalization of aliphatic compounds under mild and environmentally friendly conditions using a low-cost enzymatic biocatalyst. This could be possible taking advantage from a new peroxidase type that catalyzes monooxygenase reactions with H2O2 as the on...

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Autores: Babot, Esteban Daniel, Río Andrade, José Carlos del, Kalum, Lisbeth, Martínez, Ángel T., Gutiérrez Suárez, Ana
Tipo de recurso: artículo
Fecha de publicación:2013
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/82491
Acceso en línea:http://hdl.handle.net/10261/82491
Access Level:acceso abierto
Palabra clave:Peroxygenase
Hydroxylation
Alkanes
Fatty acids
Fatty alcohols
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spelling Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinereaBabot, Esteban DanielRío Andrade, José Carlos delKalum, LisbethMartínez, Ángel T.Gutiérrez Suárez, AnaPeroxygenaseHydroxylationAlkanesFatty acidsFatty alcoholsThe goal of this study is the selective oxyfunctionalization of aliphatic compounds under mild and environmentally friendly conditions using a low-cost enzymatic biocatalyst. This could be possible taking advantage from a new peroxidase type that catalyzes monooxygenase reactions with H2O2 as the only cosubstrate (peroxygenase). With this purpose, recombinant peroxygenase, from gene mining in the sequenced genome of Coprinopsis cinerea and heterologous expression using an industrial fungal host, is tested for the first time on aliphatic substrates. The reaction on free and esterified fatty acids and alcohols, and long-chain alkanes was followed by gas chromatography, and the different reaction products were identified by mass spectrometry. Regioselective hydroxylation of saturated/unsaturated fatty acids was observed at the w-1 and w-2 positions (only at the w-2 position in myristoleic acid). Alkyl esters of fatty acids and monoglycerides were also w-1 or w-2 hydroxylated, but di- and tri-glycerides were not modified. Fatty alcohols yielded hydroxy derivatives at the w-1 or w-2 positions (diols) but also fatty acids and their hydroxy derivatives. Interestingly, the peroxygenase was able to oxyfunctionalize alkanes giving, in addition to alcohols at positions 2 or 3, dihydroxylated derivatives at both sides of the molecule. The predominance of mono- or di-hydroxylated derivatives seems related to the higher or lower proportion of acetone, respectively, in the reaction medium. The recombinant C. cinerea peroxygenase appears as a promising biocatalyst for alkane activation and production of aliphatic oxygenated derivatives, with better properties than the previously reported peroxygenase from Agrocybe aegerita, and advantages related to its recombinant nature for enzyme engineering and industrial production.This study was funded by the PEROXICATS (KBBE-2010-4-265397) EU project. E.D. Babot thanks the Spanish CSIC for a JAE fellowship co-financed by FSE. R. Ullrich and M. Hofrichter are acknowledged for providing wild-type A. aegerita peroxygenase preparation.Peer reviewedJohn Wiley & Sons201320132013info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/82491reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#KBBE-2010-4-265397http://dx.doi.org/10.1002/bit.24904info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/824912026-05-22T06:33:51Z
dc.title.none.fl_str_mv Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea
title Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea
spellingShingle Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea
Babot, Esteban Daniel
Peroxygenase
Hydroxylation
Alkanes
Fatty acids
Fatty alcohols
title_short Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea
title_full Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea
title_fullStr Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea
title_full_unstemmed Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea
title_sort Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from coprinopsis cinerea
dc.creator.none.fl_str_mv Babot, Esteban Daniel
Río Andrade, José Carlos del
Kalum, Lisbeth
Martínez, Ángel T.
Gutiérrez Suárez, Ana
author Babot, Esteban Daniel
author_facet Babot, Esteban Daniel
Río Andrade, José Carlos del
Kalum, Lisbeth
Martínez, Ángel T.
Gutiérrez Suárez, Ana
author_role author
author2 Río Andrade, José Carlos del
Kalum, Lisbeth
Martínez, Ángel T.
Gutiérrez Suárez, Ana
author2_role author
author
author
author
dc.subject.none.fl_str_mv Peroxygenase
Hydroxylation
Alkanes
Fatty acids
Fatty alcohols
topic Peroxygenase
Hydroxylation
Alkanes
Fatty acids
Fatty alcohols
description The goal of this study is the selective oxyfunctionalization of aliphatic compounds under mild and environmentally friendly conditions using a low-cost enzymatic biocatalyst. This could be possible taking advantage from a new peroxidase type that catalyzes monooxygenase reactions with H2O2 as the only cosubstrate (peroxygenase). With this purpose, recombinant peroxygenase, from gene mining in the sequenced genome of Coprinopsis cinerea and heterologous expression using an industrial fungal host, is tested for the first time on aliphatic substrates. The reaction on free and esterified fatty acids and alcohols, and long-chain alkanes was followed by gas chromatography, and the different reaction products were identified by mass spectrometry. Regioselective hydroxylation of saturated/unsaturated fatty acids was observed at the w-1 and w-2 positions (only at the w-2 position in myristoleic acid). Alkyl esters of fatty acids and monoglycerides were also w-1 or w-2 hydroxylated, but di- and tri-glycerides were not modified. Fatty alcohols yielded hydroxy derivatives at the w-1 or w-2 positions (diols) but also fatty acids and their hydroxy derivatives. Interestingly, the peroxygenase was able to oxyfunctionalize alkanes giving, in addition to alcohols at positions 2 or 3, dihydroxylated derivatives at both sides of the molecule. The predominance of mono- or di-hydroxylated derivatives seems related to the higher or lower proportion of acetone, respectively, in the reaction medium. The recombinant C. cinerea peroxygenase appears as a promising biocatalyst for alkane activation and production of aliphatic oxygenated derivatives, with better properties than the previously reported peroxygenase from Agrocybe aegerita, and advantages related to its recombinant nature for enzyme engineering and industrial production.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013
2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/82491
url http://hdl.handle.net/10261/82491
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
KBBE-2010-4-265397
http://dx.doi.org/10.1002/bit.24904
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)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.81155

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