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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
Article, Secondary publication, Publisher's Version

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Item Type: Article
Type of entry: Secondary publication
Title: Untangling effects of proteins as stabilizers for foam films
Language: English
Date: 2 December 2022
Place of Publication: Darmstadt
Year of primary publication: 2022
Publisher: Frontiers Media S.A.
Journal or Publication Title: Frontiers in Soft Matter
Volume of the journal: 2
Collation: 18 Seiten
DOI: 10.26083/tuprints-00022938
Corresponding Links:
Origin: Secondary publication DeepGreen
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.

Uncontrolled Keywords: disjoining pressure, β-lactoglobulin, bovine serum albumin, casein, foam films, networks
Status: Publisher's Version
URN: urn:nbn:de:tuda-tuprints-229385
Classification DDC: 500 Science and mathematics > 530 Physics
Divisions: 05 Department of Physics > Institute for Condensed Matter Physics
Date Deposited: 02 Dec 2022 12:56
Last Modified: 14 Nov 2023 19:05
SWORD Depositor: Deep Green
URI: https://tuprints.ulb.tu-darmstadt.de/id/eprint/22938
PPN: 502480114
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