Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Free

dc.contributor.authorRemonatto, Daniela [UNESP]
dc.contributor.authorOliveira, J. Vladimir
dc.contributor.authorGuisan, J. Manuel
dc.contributor.authorOliveira, Débora
dc.contributor.authorNinow, Jorge
dc.contributor.authorFernandez-Lorente, Gloria
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUniversidade Federal de Santa Catarina (UFSC)
dc.contributor.institutionCantoblanco
dc.contributor.institutionCIAL (CSIC-UAM)
dc.date.accessioned2022-04-28T19:49:57Z
dc.date.available2022-04-28T19:49:57Z
dc.date.issued2022-01-01
dc.description.abstractLipases 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.en
dc.description.affiliationDepartment of Engineering of Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP), SP
dc.description.affiliationDepartment of Chemical and Food Engineering UFSC, SC
dc.description.affiliationDepartamento de Biocatálisis Instituto de Catálisis-CSIC UAM Cantoblanco
dc.description.affiliationDepartamento de Biotecnología y Microbiología de los Alimentos Instituto de Alimentación CIAL (CSIC-UAM)
dc.description.affiliationUnespDepartment of Engineering of Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP), SP
dc.identifierhttp://dx.doi.org/10.1007/s12010-021-03774-8
dc.identifier.citationApplied Biochemistry and Biotechnology.
dc.identifier.doi10.1007/s12010-021-03774-8
dc.identifier.issn1559-0291
dc.identifier.issn0273-2289
dc.identifier.scopus2-s2.0-85123256588
dc.identifier.urihttp://hdl.handle.net/11449/223304
dc.language.isoeng
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.sourceScopus
dc.subjectEversa® Transform
dc.subjectEversa® Transform 2.0
dc.subjectHydrophobic supports
dc.subjectImmobilization
dc.subjectLipase
dc.subjectSolvent-free
dc.titleImmobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Freeen
dc.typeArtigo
unesp.author.orcid0000-0002-0756-439X[6]

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