Shear localisation in interfacial particle layers and its influence on Lissajous-plots

Birbaum, Fabian C.; Haavisto, Sanna; Koponen, Antti; Windhab, Erich J.; Fischer, Peter

doi:10.1007/s00397-016-0912-0

Cited by 11 publications

(3 citation statements)

References 46 publications

(65 reference statements)

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“…The loss tangents for these interfaces tend to be low (≤0.1), and in large amplitude dilatational studies they often show asymmetries in Lissajous-Bowditch plots, displaying softening in extension, and hardening in compression 22,30 . In surface shear they may display yielding behavior at a critical surface stress 31 . All these are indicators of soft disordered solid behavior.…”

Section: Resultsmentioning

confidence: 99%

Dynamic heterogeneity in complex interfaces of soft interface-dominated materials

Sagis

Liu

et al. 2019

Sci Rep

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Complex interfaces stabilized by proteins, polymers or nanoparticles, have a much richer dynamics than those stabilized by simple surfactants. By subjecting fluid-fluid interfaces to step extension-compression deformations, we show that in general these complex interfaces have dynamic heterogeneity in their relaxation response that is well described by a Kohlrausch-Williams-Watts function, with stretch exponent β between 0.4–0.6 for extension, and 0.6–1.0 for compression. The difference in β between expansion and compression points to an asymmetry in the dynamics. Using atomic force microscopy and simulations we prove that the dynamic heterogeneity is intimately related to interfacial structural heterogeneity and show that the dominant mode for stretched exponential relaxation is momentum transfer between bulk and interface, a mechanism which has so far largely been ignored in experimental surface rheology. We describe how its rate constant can be determined using molecular dynamics simulations. These interfaces clearly behave like disordered viscoelastic solids and need to be described substantially different from the 2d homogeneous viscoelastic fluids typically formed by simple surfactants.

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Section: Resultsmentioning

confidence: 99%

Dynamic heterogeneity in complex interfaces of soft interface-dominated materials

Sagis

Liu

et al. 2019

Sci Rep

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“…Only a limited works have been done on the LAOS behavior of the air-water interfaces [39][40][41][42] . Therefore, there is still a need for the advancement of this topic.…”

Section: Introductionmentioning

confidence: 99%

Nonlinear Viscoelastic Behavior of Air-Water Interface Containing Surfactant-Laden Nanoparticles

Vishal

Ghosh

2020

J. Soc. Rheol., Jpn

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Foams have a large number of applications in our daily life. Their stability depends on the thin liquid film, which consists of an aqueous phase bound by two air-water interfaces. During its processing, foam is exposed to a large deformation. Therefore, the study of the air-water interface under large amplitude oscillatory shear (LAOS) flow is highly relevant for foam stability. In this article, the LAOS behavior of the air-water interface was investigated. The interface was formed by 0.1 mol m −3 hexadecyltrimethylammonium bromide and 0.5% w/v silica nanoparticles. The LAOS study was performed by analyzing the intracycle stress waveforms and Lissajous-Bowditch curves. The Fourier transform rheology and Chebyshev polynomial approaches were used to describe the LAOS flow of the interface. The air-water interface exhibited intracycle strain-hardening and shear thickening behavior under the LAOS flow. However, at very large strain amplitude (i.e. 45%), the interface displayed intracycle shear thinning behavior.

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“…It could be argued that such behaviour is caused by inertia effects of the measuring device, as seen by Birbaum et al ( 2016) for interfacial rheology. Oscillations were observed at higher strains and they appeared to be highly reproducible, also when particles on the interface were absent [164] . The oscillations in Fig 4 .4A are more regular however, and also correspond with intersections in the viscous Lissajous curves shown in Fig…”

Section: Large Amplitude Oscillatory Shear (Laos)mentioning

confidence: 92%

Pea protein functionality : Tailor-made through fractionation

Kornet¹

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Some studies have shown that mild fractionation may result in similar or even better functional properties, than those of highly purified ingredients. This study aimed to relate the level of aqueous purification to the composition, solubility and viscosity of yellow pea fractions. A seldomly used method of cryo-planing combined with Cryo-SEM revealed the presence of protein bodies and starch granules in the seeds and flour, with sizes of ~ 3 µm and ~20 µm, respectively. Fractions with protein purities ranging from 40 to 85 wt. % were obtained from the flour and characterized. These fractions were also compared to commerially available pea protein isolate. The fractions that were only exposed to a solubilisation step contained high quantities of carbohydrates (23.6 wt. %), which were mostly present as oligosaccharides. Subsequent fractionation steps increased the protein content and changed the ratio between the different pea proteins to some extent.We found that more fractionation steps reduced the solubility of the fractions. The most purified fraction contained 17 wt. % insoluble protein aggregates with radii ≥ 100 nm. This fraction showed a substantial thickening capacity, with a viscosity of up to 10 3 mPa.s at a concentration of 23 wt. %. The impurities (i.e. sugars, starch granules) present in the fractions only had a small effect on viscosity. Based on the protein specific volume fraction and particle size analysis, it was concluded that pea protein can form aggregates with a rarefied structure responsible for its thickening capacity.

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Shear localisation in interfacial particle layers and its influence on Lissajous-plots

Cited by 11 publications

References 46 publications

Dynamic heterogeneity in complex interfaces of soft interface-dominated materials

Dynamic heterogeneity in complex interfaces of soft interface-dominated materials

Nonlinear Viscoelastic Behavior of Air-Water Interface Containing Surfactant-Laden Nanoparticles

Pea protein functionality : Tailor-made through fractionation

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