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Lipozyme® TL IM Biocatalyst for Castor Oil FAME and Triacetin Production by Interesterification: Activity, Stability, and Kinetics

dc.contributor.authorGómez-Calvo, Alba
dc.contributor.authorGallardo, María Esther
dc.contributor.authorLadero Galán, Miguel
dc.date.accessioned2023-06-22T11:08:57Z
dc.date.available2023-06-22T11:08:57Z
dc.date.issued2022
dc.description.abstractGlobal climate change and present geopolitical tensions call for novel, renewable, and, ideally, sustainable resources and processes that, in the end, will be integrated in the natural cycles of carbon and water, progressively replacing non-renewable feedstocks. In this context, the production of biofuels and, in consequence, of biodiesel plays a notable role. This work is focused on the production of fatty acid methyl esters (FAME) from castor oil, an abundant non-edible oil, using a sustainable technology approach based on industrial lipases and methyl acetate as a methylating reagent to reduce biocatalyst inactivation. We have selected a stable industrial enzyme preparation to determine its suitability for FAME production: Lipozyme® TL IM (an inexpensive lipase from Thermomyces lanuginosus immobilized by agglomeration in silica gel). Several operational variables affecting the enzyme activity have been studied: methanol excess (6:1 to 13:1), temperature (from 40 to 60 °C), and enzyme concentration (10 and 30% w/w). At all temperatures and reagent ratios, we have also tested the enzyme stability for six cycles, showing its low to negligible inactivation under operational conditions. Finally, a novel multivariable kinetic model has been proposed and fitted to experimental data obtained in a wide experimental range for the first time, showing that direct and reverse in-series reactions are present. We have estimated the values of the kinetic constants and their standard errors, and goodness-of-fit parameters, observing that the kinetic model fitted very reasonably to all retrieved experimental data at the same time
dc.description.departmentDepto. de Ingeniería Química y de Materiales
dc.description.facultyFac. de Ciencias Químicas
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Ciencia, Innovación
dc.description.sponsorshipInstituto de Salud Carlos III (ISCIII)
dc.description.sponsorshipEuropean Union to MEG
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/78030
dc.identifier.doi10.3390/catal12121673
dc.identifier.issn2073-4344
dc.identifier.officialurlhttps://doi.org/10.3390/catal12121673
dc.identifier.urihttps://hdl.handle.net/20.500.14352/72152
dc.journal.titleCatalysts
dc.language.isoeng
dc.publisherMDPI
dc.relation.projectIDCTQ2017-84963-C2-1-R and PID2020-114365RB-C21
dc.relation.projectIDPI15/00484, CP16/00046 and PI18/00151
dc.relation.projectIDPI21/00162 and CPII21/00011
dc.rightsAtribución 3.0 España
dc.rights.accessRightsopen access
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/es/
dc.subject.cdu66.0
dc.subject.keywordcastor oil
dc.subject.keywordFAME
dc.subject.keywordricinoleic acid
dc.subject.keywordlipase
dc.subject.keywordscreening
dc.subject.keywordkinetic model
dc.subject.ucmIngeniería química
dc.subject.unesco3303 Ingeniería y Tecnología Químicas
dc.titleLipozyme® TL IM Biocatalyst for Castor Oil FAME and Triacetin Production by Interesterification: Activity, Stability, and Kinetics
dc.typejournal article
dc.volume.number12
dspace.entity.typePublication
relation.isAuthorOfPublication24473ce5-8582-4e7e-b28a-cd5f91d1aeab
relation.isAuthorOfPublication.latestForDiscovery24473ce5-8582-4e7e-b28a-cd5f91d1aeab

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