Dataset Information

Apparent Interfacial Tension Effects in Protein Stabilized Emulsions Prepared with Microstructured Systems.

ABSTRACT: Proteins are mostly used to stabilize food emulsions; however, production of protein containing emulsions is notoriously difficult to capture in scaling relations due to the complex behavior of proteins in interfaces, in combination with the dynamic nature of the emulsification process. Here, we investigate premix membrane emulsification and use the Ohnesorge number to derive a scaling relation for emulsions prepared with whey protein, bovine serum albumin (BSA), and a standard emulsifier Tween 20, at various concentrations (0.1%, 0.5%, 1.25% and 2%). In the Ohnesorge number, viscous, inertia, and interfacial tension forces are captured, and most of the parameters can be measured with great accuracy, with the exception of the interfacial tension. We used microfluidic Y-junctions to estimate the apparent interfacial tension at throughputs comparable to those in premix emulsification, and found a unifying relation. We next used this relation to plot the Ohnesorge number versus P-ratio defined as the applied pressure over the Laplace pressure of the premix droplet. The measured values all showed a decreasing Ohnesorge number at increasing P-ratio; the differences between regular surfactants and proteins being systematic. The surfactants were more efficient in droplet size reduction, and it is expected that the differences were caused by the complex behavior of proteins in the interface (visco-elastic film formation). The differences between BSA and whey protein were relatively small, and their behavior coincided with that of low Tween concentration (0.1%), which deviated from the behavior at higher concentrations.

SUBMITTER: Guell C

PROVIDER: S-EPMC5489853 | biostudies-other | 2017 Mar

REPOSITORIES: biostudies-other

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Apparent Interfacial Tension Effects in Protein Stabilized Emulsions Prepared with Microstructured Systems.

Güell Carme C Ferrando Montserrat M Trentin Alexandre A Schroën Karin K

Membranes 20170325 2

Proteins are mostly used to stabilize food emulsions; however, production of protein containing emulsions is notoriously difficult to capture in scaling relations due to the complex behavior of proteins in interfaces, in combination with the dynamic nature of the emulsification process. Here, we investigate premix membrane emulsification and use the Ohnesorge number to derive a scaling relation for emulsions prepared with whey protein, bovine serum albumin (BSA), and a standard emulsifier Tween ...[more]

PMID: 28346335

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Project description:Emulsification is a powerful, well-known technique for mixing and dispersing immiscible components within a continuous liquid phase. Consequently, emulsions are central components of medicine, food and performance materials. Complex emulsions, including Janus droplets (that is, droplets with faces of differing chemistries) and multiple emulsions, are of increasing importance in pharmaceuticals and medical diagnostics, in the fabrication of microparticles and capsules for food, in chemical separations, in cosmetics, and in dynamic optics. Because complex emulsion properties and functions are related to the droplet geometry and composition, the development of rapid, simple fabrication approaches allowing precise control over the droplets' physical and chemical characteristics is critical. Significant advances in the fabrication of complex emulsions have been made using a number of procedures, ranging from large-scale, less precise techniques that give compositional heterogeneity using high-shear mixers and membranes, to small-volume but more precise microfluidic methods. However, such approaches have yet to create droplet morphologies that can be controllably altered after emulsification. Reconfigurable complex liquids potentially have great utility as dynamically tunable materials. Here we describe an approach to the one-step fabrication of three- and four-phase complex emulsions with highly controllable and reconfigurable morphologies. The fabrication makes use of the temperature-sensitive miscibility of hydrocarbon, silicone and fluorocarbon liquids, and is applied to both the microfluidic and the scalable batch production of complex droplets. We demonstrate that droplet geometries can be alternated between encapsulated and Janus configurations by varying the interfacial tensions using hydrocarbon and fluorinated surfactants including stimuli-responsive and cleavable surfactants. This yields a generalizable strategy for the fabrication of multiphase emulsions with controllably reconfigurable morphologies and the potential to create a wide range of responsive materials.

Dataset Information

Apparent Interfacial Tension Effects in Protein Stabilized Emulsions Prepared with Microstructured Systems.

Publications

Apparent Interfacial Tension Effects in Protein Stabilized Emulsions Prepared with Microstructured Systems.

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