Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule
Interest in the synthesis and application of thymol esters has increased in recent years due to the numerous applications associated with its biological activities. The enzymatic synthesis of thymol octanoate by esterification of thymol and octanoic acid was explored using soluble lipases and immobi...
Published in: | Catalysts |
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Main Authors: | , , |
Format: | Text |
Language: | English |
Published: |
Multidisciplinary Digital Publishing Institute
2023
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Subjects: | |
Online Access: | https://doi.org/10.3390/catal13030473 |
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author | Daniel Alberto Sánchez Gabriela Marta Tonetto María Luján Ferreira |
author_facet | Daniel Alberto Sánchez Gabriela Marta Tonetto María Luján Ferreira |
author_sort | Daniel Alberto Sánchez |
collection | MDPI Open Access Publishing |
container_issue | 3 |
container_start_page | 473 |
container_title | Catalysts |
container_volume | 13 |
description | Interest in the synthesis and application of thymol esters has increased in recent years due to the numerous applications associated with its biological activities. The enzymatic synthesis of thymol octanoate by esterification of thymol and octanoic acid was explored using soluble lipases and immobilized lipase biocatalysts in solvent-free systems. Candida antarctica lipase B in its soluble form was the most active biocatalyst for this reaction. Different thymol and lipase feeding strategies were evaluated to maximize thymol octanoate production. The results suggest that there could be lipase inhibition by the ester product of the reaction. In this way, the optimal reaction condition was given using a thymol/acid molar ratio of 1:4 mol/mol. Under these conditions the conversion of thymol was close to 94% and the lipase maintained more than 90% of its initial activity after the reaction, showing the potential of the enzyme to be used in successive reaction cycles. |
format | Text |
genre | Antarc* Antarctica |
genre_facet | Antarc* Antarctica |
id | ftmdpi:oai:mdpi.com:/2073-4344/13/3/473/ |
institution | Open Polar |
language | English |
op_collection_id | ftmdpi |
op_doi | https://doi.org/10.3390/catal13030473 |
op_relation | Catalysis for Pharmaceuticals https://dx.doi.org/10.3390/catal13030473 |
op_rights | https://creativecommons.org/licenses/by/4.0/ |
op_source | Catalysts; Volume 13; Issue 3; Pages: 473 |
publishDate | 2023 |
publisher | Multidisciplinary Digital Publishing Institute |
record_format | openpolar |
spelling | ftmdpi:oai:mdpi.com:/2073-4344/13/3/473/ 2025-01-16T19:33:10+00:00 Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule Daniel Alberto Sánchez Gabriela Marta Tonetto María Luján Ferreira 2023-02-24 application/pdf https://doi.org/10.3390/catal13030473 EN eng Multidisciplinary Digital Publishing Institute Catalysis for Pharmaceuticals https://dx.doi.org/10.3390/catal13030473 https://creativecommons.org/licenses/by/4.0/ Catalysts; Volume 13; Issue 3; Pages: 473 thymol octanoate enzymatic synthesis biocatalysts Candida antarctica lipase B Text 2023 ftmdpi https://doi.org/10.3390/catal13030473 2023-08-01T08:59:21Z Interest in the synthesis and application of thymol esters has increased in recent years due to the numerous applications associated with its biological activities. The enzymatic synthesis of thymol octanoate by esterification of thymol and octanoic acid was explored using soluble lipases and immobilized lipase biocatalysts in solvent-free systems. Candida antarctica lipase B in its soluble form was the most active biocatalyst for this reaction. Different thymol and lipase feeding strategies were evaluated to maximize thymol octanoate production. The results suggest that there could be lipase inhibition by the ester product of the reaction. In this way, the optimal reaction condition was given using a thymol/acid molar ratio of 1:4 mol/mol. Under these conditions the conversion of thymol was close to 94% and the lipase maintained more than 90% of its initial activity after the reaction, showing the potential of the enzyme to be used in successive reaction cycles. Text Antarc* Antarctica MDPI Open Access Publishing Catalysts 13 3 473 |
spellingShingle | thymol octanoate enzymatic synthesis biocatalysts Candida antarctica lipase B Daniel Alberto Sánchez Gabriela Marta Tonetto María Luján Ferreira Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule |
title | 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_short | Enzymatic Synthesis of Thymol Octanoate, a Promising Hybrid Molecule |
title_sort | enzymatic synthesis of thymol octanoate, a promising hybrid molecule |
topic | thymol octanoate enzymatic synthesis biocatalysts Candida antarctica lipase B |
topic_facet | thymol octanoate enzymatic synthesis biocatalysts Candida antarctica lipase B |
url | https://doi.org/10.3390/catal13030473 |