Interfacial Activity and Interfacial Shear Rheology of Native β-Lactoglobulin Monomers and Their Heat-Induced Fibers

Jung, Jin-Mi; Gunes, Deniz Z.; Mezzenga, Raffaele

doi:10.1021/la102721m

Cited by 155 publications

(140 citation statements)

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“…The exact extent of cleavage to peptides, formation of fibres and deamidation is very difficult to identify and quantify, therefore the bulk composition of the system being studied is at best only qualitatively understood. This type of issue makes even the simplest of experiments difficult to interpret, as in the study by Jung et al [14], where the observed interfacial tension kinetics could not be clearly explained. Second, the interfacial composition is even more difficult to characterize than that in the bulk.…”

Section: Introductionmentioning

confidence: 96%

“…First, systems composed of natural components are often complex and difficult to characterize. For example, heat treatment of b-lactoglobulin at pH 2 to form fibres results in a mixed system of fibres, monomers, peptides and deamidated variants of each [14]. The exact extent of cleavage to peptides, formation of fibres and deamidation is very difficult to identify and quantify, therefore the bulk composition of the system being studied is at best only qualitatively understood.…”

Section: Introductionmentioning

confidence: 99%

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Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Dwyer

James

et al. 2013

J. R. Soc. Interface.

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Mixtures of a large, structured protein with a smaller, unstructured component are inherently complex and hard to characterize at interfaces, leading to difficulties in understanding their interfacial behaviours and, therefore, formulation optimization. Here, we investigated interfacial properties of such a mixed system. Simplicity was achieved using designed sequences in which chemical differences had been eliminated to isolate the effect of molecular size and structure, namely a short unstructured peptide (DAMP1) and its longer structured protein concatamer (DAMP4). Interfacial tension measurements suggested that the size and bulk structuring of the larger molecule led to much slower adsorption kinetics. Neutron reflectometry at equilibrium revealed that both molecules adsorbed as a monolayer to the air -water interface (indicating unfolding of DAMP4 to give a chain of four connected DAMP1 molecules), with a concentration ratio equal to that in the bulk. This suggests the overall free energy of adsorption is equal despite differences in size and bulk structure. At small interfacial extensional strains, only molecule packing influenced the stress response. At larger strains, the effect of size became apparent, with DAMP4 registering a higher stress response and interfacial elasticity. When both components were present at the interface, most stress-dissipating movement was achieved by DAMP1. This work thus provides insights into the role of proteins' molecular size and structure on their interfacial properties, and the designed sequences introduced here can serve as effective tools for interfacial studies of proteins and polymers.

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Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Dwyer

James

et al. 2013

J. R. Soc. Interface.

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“…In this work, we apply this paradigm to interfacial materials, specifically particle-stabilized drops and bubbles. These systems with high interfacial area have broad applicability from food formulation and processing (1,2), encapsulation (3,4), ultrasound medical technologies (5), to lowweight/high-strength materials (6). One of the key challenges in using solid stabilized emulsions and foams in applications is curtailing Ostwald ripening, which causes the growth/shrinkage of large/small bubbles and increased size heterogeneity (7).…”

mentioning

confidence: 99%

Arresting dissolution by interfacial rheology design

Beltramo

Gupta

Alicke

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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A strategy to halt dissolution of particle-coated air bubbles in water based on interfacial rheology design is presented. Whereas previously a dense monolayer was believed to be required for such an "armored bubble" to resist dissolution, in fact engineering a 2D yield stress interface suffices to achieve such performance at submonolayer particle coverages. We use a suite of interfacial rheology techniques to characterize spherical and ellipsoidal particles at an air-water interface as a function of surface coverage. Bubbles with varying particle coverages are made and their resistance to dissolution evaluated using a microfluidic technique. Whereas a bare bubble only has a single pressure at which a given radius is stable, we find a range of pressures over which bubble dissolution is arrested for armored bubbles. The link between interfacial rheology and macroscopic dissolution of ∼ 100 µm bubbles coated with ∼ 1 µm particles is presented and discussed. The generic design rationale is confirmed by using nonspherical particles, which develop significant yield stress at even lower surface coverages. Hence, it can be applied to successfully inhibit Ostwald ripening in a multitude of foam and emulsion applications.interfacial rheology | foams | yield stress | Ostwald ripening | emulsions T uning the interparticle interaction potential in bulk suspensions has long been a strategy to engineer the properties of colloidal suspensions. In this work, we apply this paradigm to interfacial materials, specifically particle-stabilized drops and bubbles. These systems with high interfacial area have broad applicability from food formulation and processing (1, 2), encapsulation (3, 4), ultrasound medical technologies (5), to lowweight/high-strength materials (6). One of the key challenges in using solid stabilized emulsions and foams in applications is curtailing Ostwald ripening, which causes the growth/shrinkage of large/small bubbles and increased size heterogeneity (7).Ripening occurs due to differences in the Laplace pressure in bubbles of different radii; large bubbles grow, while small bubbles shrink. This suggests that strategies to impart a resistance to dilation or compression of the interface would retard or entirely stop Ostwald ripening. Previously, fully covered, "jammed," particle coated bubbles were shown to fully resist dissolution of this nature (8)(9)(10)(11)(12). When the ratio of particle size to bubble size is large (a/R > 0.1), specific faceted shapes may moreover reduce the mean curvature to zero, thereby reducing the driving force to zero (10). However, stability is also observed at much smaller a/R ratios, suggesting other factors come into play. Previous work supposed the particles do not interact with each other, but since such interactions have a major role in interfacial rheology, they can potentially contribute to bulk bubble and emulsion stability as well.Here, we design and characterize model viscoplastic interfacial systems consisting of spherical and nonspherical particles at an air-water int...

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“…Jung and co-workers demonstrated that b-lactoglobulin monomers heated at pH 2 for 5 h at 90 C are more surface active than native monomers. 58 At very long times, further conformational rearrangements take place and a viscoelastic network is formed. [48][49][50] The formation of such network is confirmed by the dilatational frequency sweep after the 24 hours of adsorption.…”

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confidence: 99%

Interfacial properties of fractal and spherical whey protein aggregates

2011

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Fractal and spherical aggregates of whey globular proteins are formed under conditions that coupled heating and shear flow in a plate heat-exchanger at high temperature and for short holding time. Their properties upon adsorption and spreading at the air-water interface have been studied at neutral pH and two subphase conditions. The surface activity of mixtures of aggregates and residual proteins is enhanced and the adsorption behaviour depends strongly on the denatured native-like monomers and the charge screening. After long hours of adsorption, they form a weakly dissipative viscoelastic network, with strong interactions. When spread at the air-water interface, protein aggregates dissociate and form monolayers whose properties are described by scaling laws in the semi-dilute regime. The scaling exponents found in charge-screening subphase conditions correspond to values for polymer in q-conditions, whereas the values determined in long-range repulsion subphase conditions are intermediate between an ideal (q-conditions) chain and a chain in good solvent.

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Interfacial Activity and Interfacial Shear Rheology of Native β-Lactoglobulin Monomers and Their Heat-Induced Fibers

Cited by 155 publications

References 53 publications

Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Arresting dissolution by interfacial rheology design

Interfacial properties of fractal and spherical whey protein aggregates

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