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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/231094
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:24:59Zoai: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:34982025-09-29 10:24:59.404CONICET 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 |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614247961591808 |
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13.070432 |