Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Free
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1007/s12010-021-03774-8 http://hdl.handle.net/11449/223304 |
Resumo: | 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. |
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Repositório Institucional da UNESP |
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Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-FreeEversa® TransformEversa® Transform 2.0Hydrophobic supportsImmobilizationLipaseSolvent-freeLipases 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.Department of Engineering of Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP), SPDepartment of Chemical and Food Engineering UFSC, SCDepartamento de Biocatálisis Instituto de Catálisis-CSIC UAM CantoblancoDepartamento de Biotecnología y Microbiología de los Alimentos Instituto de Alimentación CIAL (CSIC-UAM)Department of Engineering of Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP), SPUniversidade Estadual Paulista (UNESP)Universidade Federal de Santa Catarina (UFSC)CantoblancoCIAL (CSIC-UAM)Remonatto, Daniela [UNESP]Oliveira, J. VladimirGuisan, J. ManuelOliveira, DéboraNinow, JorgeFernandez-Lorente, Gloria2022-04-28T19:49:57Z2022-04-28T19:49:57Z2022-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1007/s12010-021-03774-8Applied Biochemistry and Biotechnology.1559-02910273-2289http://hdl.handle.net/11449/22330410.1007/s12010-021-03774-82-s2.0-85123256588Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengApplied Biochemistry and Biotechnologyinfo:eu-repo/semantics/openAccess2022-04-28T19:49:57Zoai:repositorio.unesp.br:11449/223304Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:52:31.099304Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
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 [UNESP] Eversa® Transform Eversa® Transform 2.0 Hydrophobic supports Immobilization Lipase Solvent-free |
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 |
author |
Remonatto, Daniela [UNESP] |
author_facet |
Remonatto, Daniela [UNESP] Oliveira, J. Vladimir Guisan, J. Manuel Oliveira, Débora Ninow, Jorge Fernandez-Lorente, Gloria |
author_role |
author |
author2 |
Oliveira, J. Vladimir Guisan, J. Manuel Oliveira, Débora Ninow, Jorge Fernandez-Lorente, Gloria |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) Universidade Federal de Santa Catarina (UFSC) Cantoblanco CIAL (CSIC-UAM) |
dc.contributor.author.fl_str_mv |
Remonatto, Daniela [UNESP] Oliveira, J. Vladimir Guisan, J. Manuel Oliveira, Débora Ninow, Jorge Fernandez-Lorente, Gloria |
dc.subject.por.fl_str_mv |
Eversa® Transform Eversa® Transform 2.0 Hydrophobic supports Immobilization Lipase Solvent-free |
topic |
Eversa® Transform Eversa® Transform 2.0 Hydrophobic supports Immobilization Lipase Solvent-free |
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 |
2022-04-28T19:49:57Z 2022-04-28T19:49:57Z 2022-01-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1007/s12010-021-03774-8 Applied Biochemistry and Biotechnology. 1559-0291 0273-2289 http://hdl.handle.net/11449/223304 10.1007/s12010-021-03774-8 2-s2.0-85123256588 |
url |
http://dx.doi.org/10.1007/s12010-021-03774-8 http://hdl.handle.net/11449/223304 |
identifier_str_mv |
Applied Biochemistry and Biotechnology. 1559-0291 0273-2289 10.1007/s12010-021-03774-8 2-s2.0-85123256588 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Applied Biochemistry and Biotechnology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128993634811904 |