Interfacial rheology of protein–surfactant mixtures

Maldonado-Valderrama, Julia; Patino, Juan M. Rodrı́guez

doi:10.1016/j.cocis.2009.12.004

Cited by 241 publications

(117 citation statements)

References 87 publications

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“…At this stage, however, the concentration of LMWSs is not high enough to provide dispersion stabilisation by the Gibbs-Marangoni effect. As the concentration of LMWSs increases, they displace the proteins from the surface and ultimately stabilise the dispersion by their own mechanism (19,38). Molecules of LMWS at the interface squeeze together more tightly than proteins; thus, in most cases, LMWSs replace proteins at the interface, given a sufficient concentration in the bulk phase.…”

Section: Dispersions Stabilised With Proteins Low-molecular-weight Smentioning

confidence: 99%

“…Distribution of proteins and LMWSs at the interface is determined by the competitive adsorption of both types of surfactants and by the nature of the protein-LMWS interactions, both of which have a distinct impact on the rheological properties of the interface (19). Furthermore, the interfacial viscosity and complex modulus values for adsorbed proteins have been often shown to be much higher than those for LMWSs (43).…”

Section: Dispersions Stabilised With Proteins Low-molecular-weight Smentioning

confidence: 99%

“…Furthermore, the interfacial viscosity and complex modulus values for adsorbed proteins have been often shown to be much higher than those for LMWSs (43). Therefore, the interactions between surfactants, displacement of proteins by LMWSs, structures at the interface, incompatibilities of surfactants, film composition and the mechanism of interfacial film formation can all be analysed using interfacial rheological methods (19,20,31).…”

Section: Dispersions Stabilised With Proteins Low-molecular-weight Smentioning

confidence: 99%

“…Shear interfacial rheological methods involve inducing shear in the adsorbed film without changing the area. These methods provide information on the structures formed at the interface (3,8,19). These techniques are most commonly used for the adsorption layers of protein or combinations of protein and low-molecular-weight surfactants and can be divided into direct and indirect methods.…”

Section: Shear Measuring Techniquesmentioning

confidence: 99%

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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: Dispersions Stabilised With Proteins Low-molecular-weight Smentioning

confidence: 99%

Section: Dispersions Stabilised With Proteins Low-molecular-weight Smentioning

confidence: 99%

Section: Dispersions Stabilised With Proteins Low-molecular-weight Smentioning

confidence: 99%

Section: Shear Measuring Techniquesmentioning

confidence: 99%

See 2 more Smart Citations

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

Pelipenko¹,

Kristl²,

Rošic³

et al. 2012

Acta Pharmaceutica

View full text Add to dashboard Cite

show abstract

“…The addition of surfactants can modify the microstructure, equilibrium and dynamic adsorption values, and the rheological characteristics of interfacial layers 3,10,11,55 and the interfacial properties of the mixed protein/surfactant system are also quite different from the bulk. Studies of the microstructure at the interface using Brewster Angle Microscopy or Fluorescence Microscopy [56][57][58] or by evaluating local dynamics using micro-rheology reveal the presence of considerable interfacial phase separation with localized surfactant-rich and protein-rich regions 3,4,36 .…”

Section: Protein-surfactant Mixturesmentioning

confidence: 99%

Interfacial viscoelasticity, yielding and creep ringing of globular protein–surfactant mixtures

2011

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Protein-surfactant mixtures arise in many industrial and biological systems, and indeed, blood itself is a mixture of serum albumins along with various other surface-active components. Bovine serum albumin (BSA) solutions, and globular proteins in general, exhibit an apparent yield stress in bulk rheological measurements at surprisingly low concentrations. By contrasting interfacial rheological measurements with corresponding interface-free data obtained using a microfluidic rheometer, we show that the apparent yield stress exhibited by these solutions arises from the presence of a viscoelastic layer formed due to the adsorption of protein molecules at the air-water interface. The coupling between instrument inertia and surface elasticity in a controlled stress device also results in a distinctive damped oscillatory strain response during creep experiments known as"creep ringing". We show that this response can be exploited to extract the interfacial storage and loss moduli of the protein interface. The interfacial creep response at small strains can be described by a simple second order system, such as the linear Jeffreys model, however the interfacial response rapidly becomes nonlinear beyond strains of order 1%. We use the two complementary techniques of interfacial rheometry and microfluidic rheometry to examine the systematic changes in the surface and bulk material functions for mixtures of a common non-ionic surfactant, Polysorbate 80, and BSA. It is observed that the nonlinear viscoelastic properties of the interface are significantly suppressed by the presence of even a relatively small amount of surfactant (c surf > 10 −3 wt.%).

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Interfacial Phenomena in Structured Foods

Golding

2012

Food Materials Science and Engineering

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Interfacial rheology of protein–surfactant mixtures

Cited by 241 publications

References 87 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

Interfacial viscoelasticity, yielding and creep ringing of globular protein–surfactant mixtures

Interfacial Phenomena in Structured Foods

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