New views on foams from protein solutions

Wierenga, Peter A.; Gruppen, Harry

doi:10.1016/j.cocis.2010.05.017

Cited by 172 publications

(117 citation statements)

References 93 publications

(48 reference statements)

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“…According to Henry's law, the solubility of a gas in a liquid is higher around the bubble than in bulk liquid. Consequently, the excess gas diffuses to areas of lower concentration of dissolved gas (e.g., to larger bubbles and to the atmosphere) (46). Another source of instability at liquid-liquid and gas-liquid interfaces is coalescence.…”

Section: Stability Of Gas-liquid and Liquid-liquid Interfaces: Interfmentioning

confidence: 99%

Interfacial rheology: An overview of measuring techniques and its role in dispersions and electrospinning

Pelipenko¹,

Kristl²,

Rošic³

et al. 2012

Acta Pharmaceutica

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Colloidal disperse systems represent the increasing number of modern delivery systems whose primary characteristic, a large interfacial area, causes thermodynamic instability. Therefore, the foremost challenge in dispersion design is the reduction of interface instability and an understanding of the behaviour of interfaces. Interfacial rheology is one of the most powerful tools for observing occurrences at the interphase. As previously mentioned, the stability of such systems is provided by the formation of a stable interfacial layer of surfactants around each dispersible particle. The stability of these systems can be improved by using more than one surfactant, but it must be kept in mind that different surfactants can have varying mechanisms of stabilisation, some of which can be mutually incompatible. Surfactant selection is therefore crucial and must be based on physicochemical properties, stability of the interfacial film, mobility of the molecules in the interfacial film, HLB, film formation kinetics, compatibility and interactions between molecules on the surface, CMC, etc. Interfacial rheological properties have yet to be thoroughly explored. Only recently, methods have been introduced that provide sufficient sensitivity to reliably determine viscoelastic interfacial properties. In general, interfacial rheology describes the relationship between the deformation of an interface and the stresses exerted on it.Due to the variety in deformations of the interfacial layer (shear and expansions or compressions), the field of interfacial rheology is divided into the subcategories of shear and dilatational rheology. While shear rheology is primarily linked to the long-term stability of dispersions, dilatational rheology provides information regarding short-term stability. Interfacial rheological characteristics become relevant in systems with large interfacial areas, such as emulsions and foams, and in processes that lead to a large increase in the interfacial area, such as electrospinning of nanofibers.

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Section: Stability Of Gas-liquid and Liquid-liquid Interfaces: Interfmentioning

confidence: 99%

Interfacial rheology: An overview of measuring techniques and its role in dispersions and electrospinning

Pelipenko¹,

Kristl²,

Rošic³

et al. 2012

Acta Pharmaceutica

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“…In order to improve product formulations, it would be desirable to be able to predict functional behaviour from an understanding of interfacial properties, and ideally from knowledge of molecular structure. This link is not well established [1][2][3], largely owing to the complexity of protein molecules and the interplay between many contributing factors including surface coverage/pressure, adsorption rate, electrostatic and steric repulsion, and interfacial rheology. For example, increasing the ionic strength of solution from which protein foam is formed may have the effect of increasing the measured interfacial elasticity owing to increased intermolecular interaction, however changes in surface packing, interfacial charge and bulk aggregation may, and often do, occur.…”

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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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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“…The viscosity, interfacial tension and dilatational modulus are three parameters that can be easily and rapidly determined for any solution. As a result, some protein foam researchers aim to find a relation between molecular properties and interfacial properties, while others strive to determine the relationship between interfacial properties and foam formation and stability [1].…”

Section: Introduction mentioning

confidence: 99%

“…Three main factors have an impact on foam formation: the number of surfactant molecules in the solution, the adsorption rate of those molecules onto the surface and the dilatational properties of the layer of adsorbed molecules [2]. As often mentioned, faster adsorption Proteins 2 kinetics (or at least faster decrease of surface tension) relates to a better foam forming capacity of protein solutions [1]. The foaming capacity and the stability of the foam cannot be measured independently because the destabilizing mechanisms and foam formation take place simultaneously [3].…”

Section: Introduction mentioning

confidence: 99%

“…The formation of a layer of adsorbed molecules was found to be necessary for the formation and stabilization of foams, since pure liquids do not form stable foams [1]. Three main factors have an impact on foam formation: the number of surfactant molecules in the solution, the adsorption rate of those molecules onto the surface and the dilatational properties of the layer of adsorbed molecules [2].…”

Section: Introduction mentioning

confidence: 99%

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Effect of Acid Treatment on Interfacial and Foam Properties of Soy Proteins

Abirached¹,

Medrano²,

Moyna³

et al. 2015

JFSE

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Abstract:The goal of the present work was to study the effects of acid treatment on the foaming properties of a soybean protein isolate (SPI) and its fractions, glycinin (11S) and β-conglycinin (7S). The structural characteristics, interfacial properties, foaming capacity and stability of the treated proteins were studied. Results from surface hydrophobicity and differential scanning calorimetry (DSC) showed that the acid treatment caused the complete denaturation of 11S and a partial denaturation of 7S. This protein unfolding affected their interfacial properties, which led to an improvement in the foaming properties of both protein fractions and isolate. Treated 7S showed the best behavior in the rearrangement process, probably due to its smaller size and its modified structural characteristics. All treated proteins showed stronger interfacial films. The foams of treated proteins were destabilized mostly due to gravitational drainage rather than Ostwald ripening.

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New views on foams from protein solutions

Cited by 172 publications

References 93 publications

Interfacial rheology: An overview of measuring techniques and its role in dispersions and electrospinning

Interfacial rheology: An overview of measuring techniques and its role in dispersions and electrospinning

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

Effect of Acid Treatment on Interfacial and Foam Properties of Soy Proteins

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