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dc.contributor.authorValiño Llamazares, Virginia 
dc.contributor.authorSan Román San Emeterio, María Fresnedo 
dc.contributor.authorIbáñez Mendizábal, Raquel 
dc.contributor.authorBenito Moreno, José Manuel
dc.contributor.authorEscudero Barbero, María Isabel
dc.contributor.authorOrtiz Uribe, Inmaculada 
dc.contributor.otherUniversidad de Cantabriaes_ES
dc.date.accessioned2017-02-16T07:46:33Z
dc.date.available2017-02-16T07:46:33Z
dc.date.issued2014-10-15
dc.identifier.issn1383-5866
dc.identifier.issn1873-3794
dc.identifier.otherCTQ2011-2526es_ES
dc.identifier.otherCTM2011-23912es_ES
dc.identifier.otherCTQ2012-31639es_ES
dc.identifier.urihttp://hdl.handle.net/10902/10343
dc.description.abstractThe aim of this work is to accurately measure fundamental surface properties, i.e., zeta potential, isoelectric point and protein size that determine the optimal separation conditions of Bovine serum albumin and lactoferrin, two high added value food proteins whose similarity in weight makes their separation a scientific and technical challenge. The systematic study of these proteins’ surface properties was performed under different conditions: (i) 3.0 < pH < 10.0, (ii) electrolyte type: KCl, NaCl and CaCl2 and concentration (0.01–0.1 M KCl) and (iii) protein concentration in the range of 0.04–4.0 g L-1 for BSA and 0.01–1.0 g L-1 for LF with the objective of establishing the optimal separation conditions. Finally, the comparison of the experimental and theoretically calculated values revealed significant deviations under specific conditions, highlighting the simplicity of the theoretical assumptions and leading to the conclusion that the use of experimental surface properties is still needed for the correct design of food protein separation processes.es_ES
dc.description.sponsorshipFinancial support from the Projects CTQ2011-25262, CTM2011- 23912 and CTQ2012- 31639 (Ministerio de Economía y Competitividad-MINECO/SPAIN and Fondo Europeo de Desarrollo Regional-FEDER) is gratefully acknowledged.es_ES
dc.format.extent38 p.es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.rights© 2014, Elsevier. Licensed under the Creative Commons Reconocimiento-NoComercial-SinObraDerivadaes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.sourceSeparation and Purification Technology, 2014, 135, 145–157es_ES
dc.subject.otherDynamic light scatteringes_ES
dc.subject.otherZeta potentiales_ES
dc.subject.otherBovine serum proteinses_ES
dc.subject.otherBioprocess designes_ES
dc.titleAccurate determination of key surface properties that determine the efficient separation of bovine milk BSA and LF proteinses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherVersionhttp://dx.doi.org/10.1016/j.seppur.2014.07.051es_ES
dc.rights.accessRightsopenAccesses_ES
dc.identifier.DOI10.1016/j.seppur.2014.07.051
dc.type.versionacceptedVersiones_ES


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© 2014, Elsevier. Licensed under the Creative Commons Reconocimiento-NoComercial-SinObraDerivadaExcept where otherwise noted, this item's license is described as © 2014, Elsevier. Licensed under the Creative Commons Reconocimiento-NoComercial-SinObraDerivada