2026-04-19T03:39:25Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/45832022-04-20T12:51:06Zcom_10259_4244com_10259_5086com_10259_2604col_10259_4569

Comparison of glycerolysis of sardine oil by Lipozyme 435 in solvent free and SC-CO2 media García Solaesa, Ángela Melgosa Gómez, Rodrigo Sanz Díez, Mª Teresa Beltrán Calvo, Sagrario Illera Gigante, Alba Ester Ingeniería química Chemical engineering Ponencia presentada en: 16th European Meeting on Supercritical Fluids, 25 a 28 de abril de 2017, Lisboa The efficiency of lipase catalyzed glycerolysis of sardine oil in solvent free and supercritical carbon dioxide media has been investigated. The immiscibility between substrates, glycerol and oil, is an important drawback to reach good high conversions of triglycerides (TAG) into monoglycerides (MAG) and diglycerides (DAG) in short reaction times. To improve mass transfer rates, emulsification of both reactants as reverse micelles (glycerol-in-oil) has been carried out. Enzyme-catalyzed reaction is an attractive alternative since the reaction can be carried out under mild conditions avoiding the oxidation of omega-3 fatty acids. In this work, a commercial immobilized lipase (Lipozyme 435) was employed as biocatalyst. The effects of SC-CO2 density on reaction rates and oxidation stability has been compared with those obtained in solvent free system at atmospheric pressure. The effect of temperature and pressure on reaction yield, oxidation state of reaction products and enzyme stability was studied. Good stability of Lipozyme 435 has been observed in both systems proving no thermal deactivation at temperatures higher than its optimum. MINECO (CTQ2012‐39131‐C02‐01 and CTQ2015-64396-R) for financial support. Ángela García Solaesa acknowledges University of Burgos for a pre‐doctoral fellowship. Rodrigo Melgosa acknowledges MINECO for a predoctoral grant (reference BES‐2013‐063937). 2017-09-05T10:23:28Z 2017-09-05T10:23:28Z 2017 info:eu-repo/semantics/conferenceObject http://hdl.handle.net/10259/4583 eng info:eu-repo/semantics/openAccess application/pdf