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dc.contributor.author
Cavallaro, Valeria  
dc.contributor.author
Tonetto, Gabriela Marta  
dc.contributor.author
Ferreira, María Luján  
dc.date.available
2020-12-09T20:47:56Z  
dc.date.issued
2019-06-14  
dc.identifier.citation
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  
dc.identifier.uri
http://hdl.handle.net/11336/120059  
dc.description.abstract
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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Multidisciplinary Digital Publishing Institute  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/  
dc.subject
BIOREFINERY  
dc.subject
CALB  
dc.subject
ENZYME INHIBITION  
dc.subject
ESTERIFICATION  
dc.subject
PING-PONG BI-BI MECHANISM  
dc.subject
RSM  
dc.subject.classification
Otras Ingeniería Química  
dc.subject.classification
Ingeniería Química  
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS  
dc.title
Optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2020-11-11T18:46:54Z  
dc.identifier.eissn
2311-5637  
dc.journal.volume
5  
dc.journal.number
2  
dc.journal.pagination
1-11  
dc.journal.pais
Suiza  
dc.journal.ciudad
Basilea  
dc.description.fil
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  
dc.description.fil
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  
dc.description.fil
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  
dc.journal.title
Fermentation  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/fermentation5020048  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2311-5637/5/2/48