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Untangling effects of proteins as stabilizers for foam films

Gräff, Kevin ; Stock, Sebastian ; Mirau, Luca ; Bürger, Sabine ; Braun, Larissa ; Völp, Annika ; Willenbacher, Norbert ; Klitzing, Regine von (2022)
Untangling effects of proteins as stabilizers for foam films.
In: Frontiers in Soft Matter, 2022, 2
doi: 10.26083/tuprints-00022938
Artikel, Zweitveröffentlichung, Verlagsversion

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Kurzbeschreibung (Abstract)

Foam film’s properties have a high impact on the properties of the macroscopic foams. This work focusses on protein stabilized foam films. The direct comparison of three different proteins with a concentration normalized to the protein surface enables to distinguish between electrostatic, steric and network stabilization effects. In order to untangle those effects, we study and compare two globular proteins (β − lactoglobulin, BLG, and bovine serum albumin, BSA) and a disordered, flexible protein (whole casein, CN) at low ionic strengths with varying solution pH. Image intensity measurement as a recently developed image analysis method in this field allows to record spatially resolved disjoining pressure isotherms in a Thin Film Pressure Balance (TFPB). This reveals insights into the structure formation in inhomogeneous protein films. As a novel method we introduce tracking inhomogeneities (features) which enables the measurement of interfacial mobility and stiffness of foam films. Around the isoelectric point (IEP), Newton Black Films (NBF) form which are stable for the globular proteins while they are unstable for the disordered flexible one. This difference in film stability is explained by different characteristics of the network structures which is supported by findings in the bulk and at the surface of the respective protein solutions.

Typ des Eintrags: Artikel
Erschienen: 2022
Autor(en): Gräff, Kevin ; Stock, Sebastian ; Mirau, Luca ; Bürger, Sabine ; Braun, Larissa ; Völp, Annika ; Willenbacher, Norbert ; Klitzing, Regine von
Art des Eintrags: Zweitveröffentlichung
Titel: Untangling effects of proteins as stabilizers for foam films
Sprache: Englisch
Publikationsjahr: 2022
Ort: Darmstadt
Publikationsdatum der Erstveröffentlichung: 2022
Verlag: Frontiers Media S.A.
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Frontiers in Soft Matter
Jahrgang/Volume einer Zeitschrift: 2
Kollation: 18 Seiten
DOI: 10.26083/tuprints-00022938
URL / URN: https://tuprints.ulb.tu-darmstadt.de/22938
Zugehörige Links:
Herkunft: Zweitveröffentlichung DeepGreen
Kurzbeschreibung (Abstract):

Foam film’s properties have a high impact on the properties of the macroscopic foams. This work focusses on protein stabilized foam films. The direct comparison of three different proteins with a concentration normalized to the protein surface enables to distinguish between electrostatic, steric and network stabilization effects. In order to untangle those effects, we study and compare two globular proteins (β − lactoglobulin, BLG, and bovine serum albumin, BSA) and a disordered, flexible protein (whole casein, CN) at low ionic strengths with varying solution pH. Image intensity measurement as a recently developed image analysis method in this field allows to record spatially resolved disjoining pressure isotherms in a Thin Film Pressure Balance (TFPB). This reveals insights into the structure formation in inhomogeneous protein films. As a novel method we introduce tracking inhomogeneities (features) which enables the measurement of interfacial mobility and stiffness of foam films. Around the isoelectric point (IEP), Newton Black Films (NBF) form which are stable for the globular proteins while they are unstable for the disordered flexible one. This difference in film stability is explained by different characteristics of the network structures which is supported by findings in the bulk and at the surface of the respective protein solutions.

Freie Schlagworte: disjoining pressure, β-lactoglobulin, bovine serum albumin, casein, foam films, networks
Status: Verlagsversion
URN: urn:nbn:de:tuda-tuprints-229385
Sachgruppe der Dewey Dezimalklassifikatin (DDC): 500 Naturwissenschaften und Mathematik > 530 Physik
Fachbereich(e)/-gebiet(e): 05 Fachbereich Physik
05 Fachbereich Physik > Institut für Physik Kondensierter Materie (IPKM)
Hinterlegungsdatum: 02 Dez 2022 12:56
Letzte Änderung: 05 Dez 2022 09:13
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