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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Detalhes 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 documento: artigo
Data de publicação:2016
País:España
Recursos:Universitat Autònoma de Barcelona
Repositório:Dipòsit Digital de Documents de la UAB
Idioma:inglês
OAI Identifier:oai:ddd.uab.cat:147880
Acesso em linha:https://ddd.uab.cat/record/147880
https://dx.doi.org/urn:doi:10.1016/j.biombioe.2015.11.021
Access Level:Acceso aberto
Palavra-chave:Enginyeria
Biodiesel
Lipase
Transesterification mechanism
Free fatty acids
Lipase inactivation
Rhizopus oryzae
Descrição
Resumo: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.