Lipase-catalysed transesterification

A series of lipase-catalysed transesterification experiments were carried out to study the effect of the presence of free fatty acids on synthesis reaction rate and the stability of the biocatalyst, and also to elucidate the underlying mechanism, which remains a subject of debate. Based on the resul...

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Detalles Bibliográficos
Autores: Canet, Albert|||0009-0000-8487-8176, Bonet-Ragel, Kírian|||0000-0002-0041-7493, Benaiges, M. Dolors|||0000-0002-6840-1981, Valero, Francisco|||0000-0003-0429-9620
Tipo de recurso: artículo
Fecha de publicación:2016
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:147880
Acceso en línea:https://ddd.uab.cat/record/147880
https://dx.doi.org/urn:doi:10.1016/j.biombioe.2015.11.021
Access Level:acceso abierto
Palabra clave:Enginyeria
Biodiesel
Lipase
Transesterification mechanism
Free fatty acids
Lipase inactivation
Rhizopus oryzae
Descripción
Sumario:A series of lipase-catalysed transesterification experiments were carried out to study the effect of the presence of free fatty acids on synthesis reaction rate and the stability of the biocatalyst, and also to elucidate the underlying mechanism, which remains a subject of debate. Based on the results, the reaction rate and biocatalyst stability increased with increasing content in free fatty acids of the reaction mixture. Also, tests carried out with a mixture of triolein and linoleic acid revealed that the transesterification mechanism is a combination of direct alcoholysis of triacylglycerols and a twostep reaction involving hydrolysis of acylglycerols and further esterification of previously released free fatty acids. The time course of triacylglycerols and diacylglycerols revealed that the enzyme is similarly selective for both types of substrate.