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- W2094559968 abstract "This work presents a linear and nonlinear interfacial rheological characterization of viscoelastic protein adsorption layers formed by β-lactoglobulin fibrils, β-lactoglobulin peptides, and native β-lactoglobulin (called monomers) at the water–oil interface at pH 2. The fibril and peptide solution presented a similar surface density, whereas β-lactoglobulin monomers lower the interfacial tension more efficiently. The interfacial tension/dilatational rheology response to drop area amplitude sweeps showed pronounced differences, as the β-lactoglobulin fibrils and monomer react nonlinear at high frequencies and area strains, an effect not observed for β-lactoglobulin peptides. Step strain experiments in combination with frequency sweeps present the material response: In the low frequency regime, β-lactoglobulin peptides and β-lactoglobulin monomers can be characterized by the behavior of irreversibly adsorbed molecules. At high frequencies, both peptides and monomers behaved like reversibly adsorbed molecules, while β-lactoglobulin fibrils showed a mixed behavior at all frequencies. The observed dilatational rheological responses can be described using two different adsorption models, the Maxwell model and a modified Lucassen and van den Temple model. In interfacial shear rheology, the pH increase led to highly nonlinear behavior. A large amplitude oscillatory shear analysis in combination with subphase pH changes showed strain stiffening occurring at the isoelectric point, which was quantified by the strain-stiffening index S." @default.
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- W2094559968 date "2013-05-01" @default.
- W2094559968 modified "2023-10-17" @default.
- W2094559968 title "Shear and dilatational linear and nonlinear subphase controlled interfacial rheology of β-lactoglobulin fibrils and their derivatives" @default.
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- W2094559968 doi "https://doi.org/10.1122/1.4802051" @default.
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