Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule

Autores
Sanchez, Daniel Alberto; Tonetto, Gabriela Marta; Ferreira, María Luján
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Interest in the synthesis and application of thymol esters has increased in recent years dueto the numerous applications associated with its biological activities. The enzymatic synthesis ofthymol octanoate by esterification of thymol and octanoic acid was explored using soluble lipasesand immobilized lipase biocatalysts in solvent-free systems. Candida antarctica lipase B in its solubleform was the most active biocatalyst for this reaction. Different thymol and lipase feeding strategieswere evaluated to maximize thymol octanoate production. The results suggest that there could belipase inhibition by the ester product of the reaction. In this way, the optimal reaction condition wasgiven using a thymol/acid molar ratio of 1:4 mol/mol. Under these conditions the conversion ofthymol was close to 94% and the lipase maintained more than 90% of its initial activity after thereaction, showing the potential of the enzyme to be used in successive reaction cycles.
Fil: Sanchez, Daniel Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Ingeniería Química; Argentina
Fil: Tonetto, Gabriela Marta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Ingeniería Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Química; Argentina
Materia
THYMOL OCTANOATE
ENZYMATIC SYNTHESIS
BIOCATALYSTS
CANDIDA ANTARTICTICA LIPASE B
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/231094
Acceder
id CONICETDig_e285799c87125d1b39c033315f7b146d
oai_identifier_str oai:ri.conicet.gov.ar:11336/231094
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid MoleculeSanchez, Daniel AlbertoTonetto, Gabriela MartaFerreira, María LujánTHYMOL OCTANOATEENZYMATIC SYNTHESISBIOCATALYSTSCANDIDA ANTARTICTICA LIPASE Bhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Interest in the synthesis and application of thymol esters has increased in recent years dueto the numerous applications associated with its biological activities. The enzymatic synthesis ofthymol octanoate by esterification of thymol and octanoic acid was explored using soluble lipasesand immobilized lipase biocatalysts in solvent-free systems. Candida antarctica lipase B in its solubleform was the most active biocatalyst for this reaction. Different thymol and lipase feeding strategieswere evaluated to maximize thymol octanoate production. The results suggest that there could belipase inhibition by the ester product of the reaction. In this way, the optimal reaction condition wasgiven using a thymol/acid molar ratio of 1:4 mol/mol. Under these conditions the conversion ofthymol was close to 94% and the lipase maintained more than 90% of its initial activity after thereaction, showing the potential of the enzyme to be used in successive reaction cycles.Fil: Sanchez, Daniel Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Ingeniería Química; ArgentinaFil: Tonetto, Gabriela Marta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Ingeniería Química; ArgentinaFil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Química; ArgentinaMDPI2023-02-24info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/231094Sanchez, Daniel Alberto; Tonetto, Gabriela Marta; Ferreira, María Luján; Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule; MDPI; Catalysts; 13; 3; 24-2-2023; 1-152073-4344CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4344/13/3/473info:eu-repo/semantics/altIdentifier/doi/10.3390/catal13030473info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:22:11Zoai:ri.conicet.gov.ar:11336/231094instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:22:11.448CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
title Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
spellingShingle Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
Sanchez, Daniel Alberto
THYMOL OCTANOATE
ENZYMATIC SYNTHESIS
BIOCATALYSTS
CANDIDA ANTARTICTICA LIPASE B
title_short Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
title_full Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
title_fullStr Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
title_full_unstemmed Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
title_sort Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
dc.creator.none.fl_str_mv Sanchez, Daniel Alberto
Tonetto, Gabriela Marta
Ferreira, María Luján
author Sanchez, Daniel Alberto
author_facet Sanchez, Daniel Alberto
Tonetto, Gabriela Marta
Ferreira, María Luján
author_role author
author2 Tonetto, Gabriela Marta
Ferreira, María Luján
author2_role author
author
dc.subject.none.fl_str_mv THYMOL OCTANOATE
ENZYMATIC SYNTHESIS
BIOCATALYSTS
CANDIDA ANTARTICTICA LIPASE B
topic THYMOL OCTANOATE
ENZYMATIC SYNTHESIS
BIOCATALYSTS
CANDIDA ANTARTICTICA LIPASE B
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Interest in the synthesis and application of thymol esters has increased in recent years dueto the numerous applications associated with its biological activities. The enzymatic synthesis ofthymol octanoate by esterification of thymol and octanoic acid was explored using soluble lipasesand immobilized lipase biocatalysts in solvent-free systems. Candida antarctica lipase B in its solubleform was the most active biocatalyst for this reaction. Different thymol and lipase feeding strategieswere evaluated to maximize thymol octanoate production. The results suggest that there could belipase inhibition by the ester product of the reaction. In this way, the optimal reaction condition wasgiven using a thymol/acid molar ratio of 1:4 mol/mol. Under these conditions the conversion ofthymol was close to 94% and the lipase maintained more than 90% of its initial activity after thereaction, showing the potential of the enzyme to be used in successive reaction cycles.
Fil: Sanchez, Daniel Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Ingeniería Química; Argentina
Fil: Tonetto, Gabriela Marta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Ingeniería Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina. Universidad Nacional del Sur. Departamento de Química; Argentina
description Interest in the synthesis and application of thymol esters has increased in recent years dueto the numerous applications associated with its biological activities. The enzymatic synthesis ofthymol octanoate by esterification of thymol and octanoic acid was explored using soluble lipasesand immobilized lipase biocatalysts in solvent-free systems. Candida antarctica lipase B in its solubleform was the most active biocatalyst for this reaction. Different thymol and lipase feeding strategieswere evaluated to maximize thymol octanoate production. The results suggest that there could belipase inhibition by the ester product of the reaction. In this way, the optimal reaction condition wasgiven using a thymol/acid molar ratio of 1:4 mol/mol. Under these conditions the conversion ofthymol was close to 94% and the lipase maintained more than 90% of its initial activity after thereaction, showing the potential of the enzyme to be used in successive reaction cycles.
publishDate 2023
dc.date.none.fl_str_mv 2023-02-24
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/231094
Sanchez, Daniel Alberto; Tonetto, Gabriela Marta; Ferreira, María Luján; Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule; MDPI; Catalysts; 13; 3; 24-2-2023; 1-15
2073-4344
CONICET Digital
CONICET
url http://hdl.handle.net/11336/231094
identifier_str_mv Sanchez, Daniel Alberto; Tonetto, Gabriela Marta; Ferreira, María Luján; Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule; MDPI; Catalysts; 13; 3; 24-2-2023; 1-15
2073-4344
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4344/13/3/473
info:eu-repo/semantics/altIdentifier/doi/10.3390/catal13030473
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846083368950693888
score 13.22299

Publicaciones similares