Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free

Lipases are an important group of biocatalysts for many industrial applications. Two new commercial low-cost lipases Eversa® Transform and Eversa® Transform 2.0 was immobilized on four different hydrophobic supports: Lewatit-DVB, Purolite-DVB, Sepabeads-C18, and Purolite-C18. The performance of immo...

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Detalles Bibliográficos
Autores: Remonatto, Daniela, Oliveira, J. Vladimir de, Guisán, José Manuel, Oliveira, Débora de, Ninow, Jorge, Fernández-Lorente, Gloria
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/279162
Acceso en línea:http://hdl.handle.net/10261/279162
Access Level:acceso abierto
Palabra clave:Lipase
Eversa® transform
Solvent-free
Hydrophobic supports
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spelling Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-freeRemonatto, DanielaOliveira, J. Vladimir deGuisán, José ManuelOliveira, Débora deNinow, JorgeFernández-Lorente, GloriaLipaseEversa® transformSolvent-freeHydrophobic supportsLipases are an important group of biocatalysts for many industrial applications. Two new commercial low-cost lipases Eversa® Transform and Eversa® Transform 2.0 was immobilized on four different hydrophobic supports: Lewatit-DVB, Purolite-DVB, Sepabeads-C18, and Purolite-C18. The performance of immobilized lipases was investigated in the transesterification of sunflower oil solvent-free in an anhydrous medium. Interesting results were obtained for both lipases and the four supports, but with Sepabeads support the lipases Eversa showed high catalytic activity. However, the more stable and efficient derivative was Eversa® Transform immobilized on Sepabeads C-18. A 98 wt% of ethyl ester of fatty acid (FAEE) was obtained, in 3 h at 40ºC, ethanol/sunflower oil molar ratio of 3:1 and a 10 wt% of the immobilized biocatalyst. After 6 reaction cycles, the immobilized biocatalyst preserved 70 wt% of activity. Both lipases immobilized in Sepabeads C-18 were highly active and stable in the presence of ethanol. The immobilization of Eversa Transform and Eversa Transform 2.0 in hydrophobic supports described in this study appears to be a promising alternative to the immobilization and application of these news lipases still unexplored.Open Access funding provided thanks to the CRUE-CSIC agreement with Springer Nature.This work was sponsored by the Spanish Ministry of Science and Innovation (projects AGL-2009-07526 and BIO2012- 36861). The authors thank CNPq and CAPES for the scholarships and financial support of this work.Peer reviewedSpringer NatureConsejo Superior de Investigaciones Científicas (España)Conferencia de Rectores de las Universidades EspañolasMinisterio de Ciencia e Innovación (España)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202220222022info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/279162reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO//AGL2009-07526info:eu-repo/grantAgreement/MINECO//BIO2012-36861https://doi.org/10.1007/s12010-021-03774-8Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2791622026-05-22T06:33:51Z
dc.title.none.fl_str_mv Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free
title Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free
spellingShingle Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free
Remonatto, Daniela
Lipase
Eversa® transform
Solvent-free
Hydrophobic supports
title_short Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free
title_full Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free
title_fullStr Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free
title_full_unstemmed Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free
title_sort Immobilization of Eversa lipases on hydrophobic supports for ethanolysis of sunflower oil solvent-free
dc.creator.none.fl_str_mv Remonatto, Daniela
Oliveira, J. Vladimir de
Guisán, José Manuel
Oliveira, Débora de
Ninow, Jorge
Fernández-Lorente, Gloria
author Remonatto, Daniela
author_facet Remonatto, Daniela
Oliveira, J. Vladimir de
Guisán, José Manuel
Oliveira, Débora de
Ninow, Jorge
Fernández-Lorente, Gloria
author_role author
author2 Oliveira, J. Vladimir de
Guisán, José Manuel
Oliveira, Débora de
Ninow, Jorge
Fernández-Lorente, Gloria
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas (España)
Conferencia de Rectores de las Universidades Españolas
Ministerio de Ciencia e Innovación (España)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Lipase
Eversa® transform
Solvent-free
Hydrophobic supports
topic Lipase
Eversa® transform
Solvent-free
Hydrophobic supports
description Lipases are an important group of biocatalysts for many industrial applications. Two new commercial low-cost lipases Eversa® Transform and Eversa® Transform 2.0 was immobilized on four different hydrophobic supports: Lewatit-DVB, Purolite-DVB, Sepabeads-C18, and Purolite-C18. The performance of immobilized lipases was investigated in the transesterification of sunflower oil solvent-free in an anhydrous medium. Interesting results were obtained for both lipases and the four supports, but with Sepabeads support the lipases Eversa showed high catalytic activity. However, the more stable and efficient derivative was Eversa® Transform immobilized on Sepabeads C-18. A 98 wt% of ethyl ester of fatty acid (FAEE) was obtained, in 3 h at 40ºC, ethanol/sunflower oil molar ratio of 3:1 and a 10 wt% of the immobilized biocatalyst. After 6 reaction cycles, the immobilized biocatalyst preserved 70 wt% of activity. Both lipases immobilized in Sepabeads C-18 were highly active and stable in the presence of ethanol. The immobilization of Eversa Transform and Eversa Transform 2.0 in hydrophobic supports described in this study appears to be a promising alternative to the immobilization and application of these news lipases still unexplored.
publishDate 2022
dc.date.none.fl_str_mv 2022
2022
2022
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/10261/279162
url http://hdl.handle.net/10261/279162
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO//AGL2009-07526
info:eu-repo/grantAgreement/MINECO//BIO2012-36861
https://doi.org/10.1007/s12010-021-03774-8
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Springer Nature
publisher.none.fl_str_mv Springer Nature
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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