Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support
The term biorefinery is related to the sustainable production of value-added bioproducts and bioenergy from biomass. Esters from fatty acids are important compounds synthesized from by-products of the oleochemical industry. In agreement with the biorefinery concept, it is important to search for cat...
Published in: | Fermentation |
---|---|
Main Authors: | , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Multidisciplinary Digital Publishing Institute
|
Subjects: | |
Online Access: | http://hdl.handle.net/11336/120059 |
_version_ | 1821749870515453952 |
---|---|
author | Cavallaro, Valeria Tonetto, Gabriela Marta Ferreira, María Luján |
author_facet | Cavallaro, Valeria Tonetto, Gabriela Marta Ferreira, María Luján |
author_sort | Cavallaro, Valeria |
collection | CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
container_issue | 2 |
container_start_page | 48 |
container_title | Fermentation |
container_volume | 5 |
description | The term biorefinery is related to the sustainable production of value-added bioproducts and bioenergy from biomass. Esters from fatty acids are important compounds synthesized from by-products of the oleochemical industry. In agreement with the biorefinery concept, it is important to search for catalysts that reduce the consumption of energy and water, using moderate operation conditions and low reaction times. In this work, response surface methodology (RSM) was used to optimize the enzymatic synthesis of pentyl oleate using Candida antarctica lipase B (CALB) immobilized on a polyethylene-aluminum structured support. A factorial design was employed to evaluate the effects of several parameters on the ester yield. To obtain a model with a good fit, an approach to reaction mechanism and enzyme kinetics was taken into consideration. Experimental findings were correlated and explained using equations of a ping-pong bi-bi kinetic model and considering the inhibitory effects of both substrates. The developed model was consistent with the experimental data predicting an increase in pentyl oleate production with increasing temperature and a decrease with higher oleic acid amounts and alcohol to acid molar ratios. This model could be useful in a future industrial application of CALB/LLDPE/Al to minimize the costs in oleochemical biorefineries. Fil: Cavallaro, Valeria. 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 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. ... |
format | Article in Journal/Newspaper |
genre | Antarc* Antarctica |
genre_facet | Antarc* Antarctica |
geographic | Argentina Ferreira |
geographic_facet | Argentina Ferreira |
id | ftconicet:oai:ri.conicet.gov.ar:11336/120059 |
institution | Open Polar |
language | English |
long_lat | ENVELOPE(-62.050,-62.050,-64.600,-64.600) |
op_collection_id | ftconicet |
op_doi | https://doi.org/10.3390/fermentation5020048 |
op_relation | info:eu-repo/semantics/altIdentifier/doi/10.3390/fermentation5020048 info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2311-5637/5/2/48 http://hdl.handle.net/11336/120059 Cavallaro, Valeria; Tonetto, Gabriela Marta; Ferreira, María Luján; Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support; Multidisciplinary Digital Publishing Institute; Fermentation; 5; 2; 14-6-2019; 1-11 2311-5637 CONICET Digital CONICET |
op_rights | info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
publisher | Multidisciplinary Digital Publishing Institute |
record_format | openpolar |
spelling | ftconicet:oai:ri.conicet.gov.ar:11336/120059 2025-01-16T19:20:49+00:00 Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support Cavallaro, Valeria Tonetto, Gabriela Marta Ferreira, María Luján application/pdf http://hdl.handle.net/11336/120059 eng eng Multidisciplinary Digital Publishing Institute info:eu-repo/semantics/altIdentifier/doi/10.3390/fermentation5020048 info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2311-5637/5/2/48 http://hdl.handle.net/11336/120059 Cavallaro, Valeria; Tonetto, Gabriela Marta; Ferreira, María Luján; Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support; Multidisciplinary Digital Publishing Institute; Fermentation; 5; 2; 14-6-2019; 1-11 2311-5637 CONICET Digital CONICET info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ BIOREFINERY CALB ENZYME INHIBITION ESTERIFICATION PING-PONG BI-BI MECHANISM RSM https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.3390/fermentation5020048 2023-09-24T19:13:44Z The term biorefinery is related to the sustainable production of value-added bioproducts and bioenergy from biomass. Esters from fatty acids are important compounds synthesized from by-products of the oleochemical industry. In agreement with the biorefinery concept, it is important to search for catalysts that reduce the consumption of energy and water, using moderate operation conditions and low reaction times. In this work, response surface methodology (RSM) was used to optimize the enzymatic synthesis of pentyl oleate using Candida antarctica lipase B (CALB) immobilized on a polyethylene-aluminum structured support. A factorial design was employed to evaluate the effects of several parameters on the ester yield. To obtain a model with a good fit, an approach to reaction mechanism and enzyme kinetics was taken into consideration. Experimental findings were correlated and explained using equations of a ping-pong bi-bi kinetic model and considering the inhibitory effects of both substrates. The developed model was consistent with the experimental data predicting an increase in pentyl oleate production with increasing temperature and a decrease with higher oleic acid amounts and alcohol to acid molar ratios. This model could be useful in a future industrial application of CALB/LLDPE/Al to minimize the costs in oleochemical biorefineries. Fil: Cavallaro, Valeria. 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 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. ... Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Ferreira ENVELOPE(-62.050,-62.050,-64.600,-64.600) Fermentation 5 2 48 |
spellingShingle | BIOREFINERY CALB ENZYME INHIBITION ESTERIFICATION PING-PONG BI-BI MECHANISM RSM https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 Cavallaro, Valeria Tonetto, Gabriela Marta Ferreira, María Luján Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support |
title | Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support |
title_full | Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support |
title_fullStr | Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support |
title_full_unstemmed | Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support |
title_short | Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support |
title_sort | optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support |
topic | BIOREFINERY CALB ENZYME INHIBITION ESTERIFICATION PING-PONG BI-BI MECHANISM RSM https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 |
topic_facet | BIOREFINERY CALB ENZYME INHIBITION ESTERIFICATION PING-PONG BI-BI MECHANISM RSM https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 |
url | http://hdl.handle.net/11336/120059 |