Characterization of β-lactoglobulin adsorption on silica membrane pore surfaces and its impact on membrane emulsification processes

dc.contributor.authorGiefer, Patrick
dc.contributor.authorBäther, Sabrina
dc.contributor.authorKaufmes, Nadine
dc.contributor.authorKieserling, Helena
dc.contributor.authorHeyse, Anja
dc.contributor.authorWagemans, Wiebe
dc.contributor.authorBarthel, Lars
dc.contributor.authorMeyer, Vera
dc.contributor.authorSchneck, Emanuel
dc.contributor.authorFritsching, Udo
dc.contributor.authorWagemans, Anja Maria
dc.date.accessioned2023-11-15T10:40:50Z
dc.date.available2023-11-15T10:40:50Z
dc.date.issued2023-08-18
dc.description.abstractProtein adsorption plays a key role in membrane fouling in liquid processing, but the specific underlying molecular mechanisms of β-lactoglobulin adsorption on ceramic silica surfaces in premix membrane emulsification have not been investigated yet. In this study, we aimed to elucidate the β-lactoglobulin adsorption and its effect on the premix membrane emulsification of β-lactoglobulin-stabilized oil-in-water emulsions. In particular, the conformation, molecular interactions, layer thickness, surface energy of the adsorbed β-lactoglobulin and resulting droplet size distribution are investigated in relation to the solvent properties (aggregation state of β-lactoglobulin) and the treatment of the silica surface (hydrophilization). The β-lactoglobulin adsorption is driven by attractive electrostatic interactions between positively charged amino acid residues, i.e., lysin and negatively charged silanol groups, and is stabilized by hydrophobic interactions. The strong negative charges of the treated silica surfaces result in a high apparent layer thickness of β-lactoglobulin. Although the conformation of the adsorbed β-lactoglobulin layer varies with membrane treatment and the solvent properties, the β-lactoglobulin adsorption offsets the effect of hydrophilization of the membrane so that the surface energies after β-lactoglobulin adsorption are comparable. The resulting droplet size distribution of oil-in-water emulsions produced by premix membrane emulsification are similar for treated and untreated silica surfaces.en
dc.description.sponsorshipDFG, 273937032, SPP 1934: Dispersitäts-, Struktur- und Phasenänderungen von Proteinen und biologischen Agglomeraten in biotechnologischen Prozessen
dc.identifier.eissn1095-7103
dc.identifier.issn0021-9797
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/20637
dc.identifier.urihttps://doi.org/10.14279/depositonce-19435
dc.language.isoen
dc.publisherElsevier BV
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.subject.ddc500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften
dc.subject.otherprotein adsorptionen
dc.subject.otherconformationen
dc.subject.othermolecular interactionsen
dc.subject.otherfoulingen
dc.subject.otherceramic membranesen
dc.titleCharacterization of β-lactoglobulin adsorption on silica membrane pore surfaces and its impact on membrane emulsification processes
dc.typeArticle
dc.type.versionacceptedVersion
dcterms.bibliographicCitation.doi10.1016/j.jcis.2023.08.103
dcterms.bibliographicCitation.issuePart A
dcterms.bibliographicCitation.journaltitleJournal of Colloid and Interface Science
dcterms.bibliographicCitation.originalpublishernameElsevier
dcterms.bibliographicCitation.originalpublisherplaceAmsterdam
dcterms.bibliographicCitation.pageend1084
dcterms.bibliographicCitation.pagestart1074
dcterms.bibliographicCitation.volume652
dcterms.rightsHolder.reference§ 38 (4) UrhG
tub.accessrights.dnbembargoed*
tub.affiliationFak. 3 Prozesswissenschaften::Inst. Lebensmitteltechnologie und Lebensmittelchemie::FG Lebensmittelbiowissenschaften
tub.publisher.universityorinstitutionTechnische Universität Berlin

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