Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support
- Autores
- Cavallaro, Valeria; Tonetto, Gabriela Marta; Ferreira, María Luján
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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. 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
-
BIOREFINERY
CALB
ENZYME INHIBITION
ESTERIFICATION
PING-PONG BI-BI MECHANISM
RSM - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/120059
Ver los metadatos del registro completo
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Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured supportCavallaro, ValeriaTonetto, Gabriela MartaFerreira, María LujánBIOREFINERYCALBENZYME INHIBITIONESTERIFICATIONPING-PONG BI-BI MECHANISMRSMhttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2The 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; 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; ArgentinaMultidisciplinary Digital Publishing Institute2019-06-14info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/120059Cavallaro, 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; 1-112311-5637CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/fermentation5020048info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2311-5637/5/2/48info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-29T11:58:55Zoai:ri.conicet.gov.ar:11336/120059instacron: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:34982025-10-29 11:58:56.071CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
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 |
| spellingShingle |
Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support Cavallaro, Valeria BIOREFINERY CALB ENZYME INHIBITION ESTERIFICATION PING-PONG BI-BI MECHANISM RSM |
| title_short |
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_sort |
Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support |
| dc.creator.none.fl_str_mv |
Cavallaro, Valeria Tonetto, Gabriela Marta Ferreira, María Luján |
| author |
Cavallaro, Valeria |
| author_facet |
Cavallaro, Valeria 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 |
BIOREFINERY CALB ENZYME INHIBITION ESTERIFICATION PING-PONG BI-BI MECHANISM RSM |
| topic |
BIOREFINERY CALB ENZYME INHIBITION ESTERIFICATION PING-PONG BI-BI MECHANISM RSM |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 |
| dc.description.none.fl_txt_mv |
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. 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 |
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. |
| publishDate |
2019 |
| dc.date.none.fl_str_mv |
2019-06-14 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
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 |
| url |
http://hdl.handle.net/11336/120059 |
| identifier_str_mv |
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 |
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eng |
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eng |
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info:eu-repo/semantics/altIdentifier/doi/10.3390/fermentation5020048 info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2311-5637/5/2/48 |
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openAccess |
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application/pdf application/pdf |
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Multidisciplinary Digital Publishing Institute |
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Multidisciplinary Digital Publishing Institute |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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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 |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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