Publication:
Biocatalytic Synthesis of Polyglycerol Polyricinoleate: A Comparison of Different Commercial Lipases

dc.contributor.authorOrtega Requena, Salvadora
dc.contributor.authorGómez, José Luis
dc.contributor.authorBastida Rodríguez, Josefa
dc.contributor.authorMáximo Martín, María Fuensanta
dc.contributor.authorMontiel Morte, María Claudia
dc.contributor.authorGómez, María
dc.contributor.departmentIngeniería Química
dc.date.accessioned2021-04-16T09:50:49Z
dc.date.available2021-04-16T09:50:49Z
dc.date.created2013-04-19
dc.date.issued2013-10
dc.description.abstractIn this work, the studies were carried out to select the most suitable lipase as catalyst for the esterification of polyglycerol with polyricinoleic acid to yield polyglicerol polyricinoleate (PGPR), a valued-added, biobased food emulsifier are described. The enzymes assayed were lipases from Rhizopus arrhizus, Rhizopus oryzae and Mucor javanicus, previously selected because of their suitable activity and moderate cost. First, reaction was catalyzed by free lipases in a batch reactor and the influence of different operating conditions (initial water content, amount of enzyme and temperature) on the progress of the reaction was studied. Next, the three lipases were immobilized by physical adsorption on the anion exchange resin, Lewatit MonoPlus MP 64, providing derivatives with a high activity and stability. Recovery of the immobilized derivative from the reaction medium was conducted with very good yields (up 99%) and no loss of activity of the derivative with successive uses was proved. Finally, a high performance reactor, which operates at low pressure and with a dry atmosphere, was used to synthesise PGPR using the immobilized enzymes. Both Rhizopus arrhizus and Rhizopus oryzae lipases allowed the production of a PGPR which fulfils the “specific purity criteria on food additives other than colours and sweeteners” established by the Commission of the European Communities, with an acid value of 4.91 and 5.31 mg KOH/g respectively.es
dc.formatapplication/pdfes
dc.format.extent39es
dc.identifier.citationChemical and Biochemical Engineering Quaterly, 2013, 27 (4) 439–448
dc.identifier.doihttps://doi.org/10.15255/CABEQ.2014.19
dc.identifier.urihttp://hdl.handle.net/10201/106685
dc.languageenges
dc.publisherAssoc. of Chemists and Chemical Engineers of Croatiaes
dc.relationÁmbito del proyecto (Europeo, nacional o regional): Nacional Agencia/entidad financiadora: Unión Europea (FEDER) and MICINN Convocatoria: Ayudas para la realización de proyectos de investigación (Subprograma de Proyectos de Investigación Fundamental no Orientada, convocatoria 2011). Nombre del proyecto: Biosíntesis de emulsionantes con aplicaciones alimentarias y cosméticas, en sistemas “solvent free”, utilizando lipasas comerciales. Código: CTQ2011-24091es
dc.relation.ispartofNombre del proyecto: Biosíntesis de emulsionantes con aplicaciones alimentarias y cosméticas, en sistemas “solvent free”, utilizando lipasas comerciales. Código: CTQ2011-24091es
dc.relation.publisherversionhttp://silverstripe.fkit.hr/cabeq/assets/Uploads/Cabeq-2013-04-07.pdfes
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectPolyglycerol polyricinoleatees
dc.subjectlipasees
dc.subjectimmobilized enzymeses
dc.subjectheterogeneous reactiones
dc.subjectenzyme biocatalysises
dc.subjectvacuum reactores
dc.subject.otherCDU::6 - Ciencias aplicadases
dc.titleBiocatalytic Synthesis of Polyglycerol Polyricinoleate: A Comparison of Different Commercial Lipaseses
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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