Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents

Detalhes bibliográficos
Autor(a) principal: Borges, Janaina Pires [UNESP]
Data de Publicação: 2020
Outros Autores: Quilles Junior, José Carlos [UNESP], Moreno-Perez, Sônia, Fernandez-Lorente, Glória [UNESP], Boscolo, Mauricio [UNESP], Gomes, Eleni [UNESP], da Silva, Roberto [UNESP], Bocchini, Daniela Alonso [UNESP], Guisan, José Manuel
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1007/s00449-020-02399-1
http://hdl.handle.net/11449/200651
Resumo: Lipase stability in organic solvent is crucial for its application in many biotechnological processes as biocatalyst. One way to improve lipase’s activity and stability in unusual reaction medium is its immobilization on inert supports. Here, lipases from different sources and immobilized through weak chemical interactions on hydrophobic and ionic supports had their transesterification ability dramatically dependent on the support and also on the solvent that had been used. The ethanolysis of sardine oil was carried out at the presence of cyclohexane and tert-amyl alcohol, in which Duolite A568-Thermomyces lanuginosa lipase derivative achieved 49% of ethyl esters production after 24 h in cyclohexane. The selectivity of immobilized lipases was also studied and, after 3 h of synthesis, the reaction with Duolite A568-Thermomyces lanuginosa derivative in cyclohexane produced 24% ethyl ester of eicosapentaenoic acid and 1.2% ethyl ester of docosahexaenoic acid, displaying a selectivity index of 20 times the ethyl ester of eicosapentaenoic acid. Different derivatives of Candida antarctica lipases fraction B (CALB) and phospholipase Lecitase® Ultra (Lecitase) were also investigated. Along these lines, a combination between these factors may be applied to improve the activity and selectivity of immobilized lipases, decreasing the total cost of the process.
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spelling Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solventsEthanolysisImmobilizationLipases selectivityOrganic solventsLipase stability in organic solvent is crucial for its application in many biotechnological processes as biocatalyst. One way to improve lipase’s activity and stability in unusual reaction medium is its immobilization on inert supports. Here, lipases from different sources and immobilized through weak chemical interactions on hydrophobic and ionic supports had their transesterification ability dramatically dependent on the support and also on the solvent that had been used. The ethanolysis of sardine oil was carried out at the presence of cyclohexane and tert-amyl alcohol, in which Duolite A568-Thermomyces lanuginosa lipase derivative achieved 49% of ethyl esters production after 24 h in cyclohexane. The selectivity of immobilized lipases was also studied and, after 3 h of synthesis, the reaction with Duolite A568-Thermomyces lanuginosa derivative in cyclohexane produced 24% ethyl ester of eicosapentaenoic acid and 1.2% ethyl ester of docosahexaenoic acid, displaying a selectivity index of 20 times the ethyl ester of eicosapentaenoic acid. Different derivatives of Candida antarctica lipases fraction B (CALB) and phospholipase Lecitase® Ultra (Lecitase) were also investigated. Along these lines, a combination between these factors may be applied to improve the activity and selectivity of immobilized lipases, decreasing the total cost of the process.Department of Biochemistry and Chemical Technology IQ/UNESP – Rua Prof. Francisco Degni, 55 – CEPDepartment of Chemistry and Environmental Sciences IBILCE/UNESP – Rua Cristóvão Colombo, 2265 – CEPDepartment of Biotechnology and Food Microbiology Research Institute for Food Science CIAL CSIC/Campus UAMDepartment of Biology IBILCE/UNESP – Rua Cristóvão Colombo, 2265 – CEPDepartment of Catalysis CSIC/Campus UAMDepartment of Biochemistry and Chemical Technology IQ/UNESP – Rua Prof. Francisco Degni, 55 – CEPDepartment of Chemistry and Environmental Sciences IBILCE/UNESP – Rua Cristóvão Colombo, 2265 – CEPDepartment of Biology IBILCE/UNESP – Rua Cristóvão Colombo, 2265 – CEPUniversidade Estadual Paulista (Unesp)CSIC/Campus UAMBorges, Janaina Pires [UNESP]Quilles Junior, José Carlos [UNESP]Moreno-Perez, SôniaFernandez-Lorente, Glória [UNESP]Boscolo, Mauricio [UNESP]Gomes, Eleni [UNESP]da Silva, Roberto [UNESP]Bocchini, Daniela Alonso [UNESP]Guisan, José Manuel2020-12-12T02:12:25Z2020-12-12T02:12:25Z2020-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1007/s00449-020-02399-1Bioprocess and Biosystems Engineering.1615-76051615-7591http://hdl.handle.net/11449/20065110.1007/s00449-020-02399-12-s2.0-85087022232Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBioprocess and Biosystems Engineeringinfo:eu-repo/semantics/openAccess2021-10-23T14:54:23Zoai:repositorio.unesp.br:11449/200651Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T14:54:23Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
title Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
spellingShingle Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
Borges, Janaina Pires [UNESP]
Ethanolysis
Immobilization
Lipases selectivity
Organic solvents
title_short Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
title_full Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
title_fullStr Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
title_full_unstemmed Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
title_sort Ethyl esters production catalyzed by immobilized lipases is influenced by n-hexane and ter-amyl alcohol as organic solvents
author Borges, Janaina Pires [UNESP]
author_facet Borges, Janaina Pires [UNESP]
Quilles Junior, José Carlos [UNESP]
Moreno-Perez, Sônia
Fernandez-Lorente, Glória [UNESP]
Boscolo, Mauricio [UNESP]
Gomes, Eleni [UNESP]
da Silva, Roberto [UNESP]
Bocchini, Daniela Alonso [UNESP]
Guisan, José Manuel
author_role author
author2 Quilles Junior, José Carlos [UNESP]
Moreno-Perez, Sônia
Fernandez-Lorente, Glória [UNESP]
Boscolo, Mauricio [UNESP]
Gomes, Eleni [UNESP]
da Silva, Roberto [UNESP]
Bocchini, Daniela Alonso [UNESP]
Guisan, José Manuel
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
CSIC/Campus UAM
dc.contributor.author.fl_str_mv Borges, Janaina Pires [UNESP]
Quilles Junior, José Carlos [UNESP]
Moreno-Perez, Sônia
Fernandez-Lorente, Glória [UNESP]
Boscolo, Mauricio [UNESP]
Gomes, Eleni [UNESP]
da Silva, Roberto [UNESP]
Bocchini, Daniela Alonso [UNESP]
Guisan, José Manuel
dc.subject.por.fl_str_mv Ethanolysis
Immobilization
Lipases selectivity
Organic solvents
topic Ethanolysis
Immobilization
Lipases selectivity
Organic solvents
description Lipase stability in organic solvent is crucial for its application in many biotechnological processes as biocatalyst. One way to improve lipase’s activity and stability in unusual reaction medium is its immobilization on inert supports. Here, lipases from different sources and immobilized through weak chemical interactions on hydrophobic and ionic supports had their transesterification ability dramatically dependent on the support and also on the solvent that had been used. The ethanolysis of sardine oil was carried out at the presence of cyclohexane and tert-amyl alcohol, in which Duolite A568-Thermomyces lanuginosa lipase derivative achieved 49% of ethyl esters production after 24 h in cyclohexane. The selectivity of immobilized lipases was also studied and, after 3 h of synthesis, the reaction with Duolite A568-Thermomyces lanuginosa derivative in cyclohexane produced 24% ethyl ester of eicosapentaenoic acid and 1.2% ethyl ester of docosahexaenoic acid, displaying a selectivity index of 20 times the ethyl ester of eicosapentaenoic acid. Different derivatives of Candida antarctica lipases fraction B (CALB) and phospholipase Lecitase® Ultra (Lecitase) were also investigated. Along these lines, a combination between these factors may be applied to improve the activity and selectivity of immobilized lipases, decreasing the total cost of the process.
publishDate 2020
dc.date.none.fl_str_mv 2020-12-12T02:12:25Z
2020-12-12T02:12:25Z
2020-01-01
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/s00449-020-02399-1
Bioprocess and Biosystems Engineering.
1615-7605
1615-7591
http://hdl.handle.net/11449/200651
10.1007/s00449-020-02399-1
2-s2.0-85087022232
url http://dx.doi.org/10.1007/s00449-020-02399-1
http://hdl.handle.net/11449/200651
identifier_str_mv Bioprocess and Biosystems Engineering.
1615-7605
1615-7591
10.1007/s00449-020-02399-1
2-s2.0-85087022232
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Bioprocess and Biosystems Engineering
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
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