Microstructure of β-lactoglobulin-stabilized emulsions containing non-ionic surfactant and excess free protein: Influence of heating

Kerstens, Sven; Murray, Brent S.; Dickinson, Eric

doi:10.1016/j.jcis.2005.08.046

Cited by 47 publications

(47 citation statements)

References 53 publications

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“…Then we describe the effects of the addition of (1) anionic SDS and (2) cationic cetyl trimethyl ammonium bromide (CTAB) on the properties of the same heat-set emulsion gel system (no added salt). Finally, we compare the results for the emulsions containing these charged surfactants with those previously reported 41 for analogous emulsions containing the nonionic Tween 20.…”

Section: Introductionmentioning

confidence: 87%

“…A concentrated oil-in-water emulsion (45 vol% oil, 2.7 wt% β-lg in the aqueous phase) was made as described previously 41 using a laboratory-scale jet homogenizer operating at a constant pressure of 300 bar. This stock emulsion was divided into several aliquots.…”

Section: Methodsmentioning

confidence: 99%

“…40 To improve understanding of the relationship between emulsion microstructure and protein−surfactant interactions during thermal processing, the technique of confocal microscopy has emerged as a powerful tool. 37,41 In β-lgstabilized emulsions containing substantial excess protein, we have recently found 41 no evidence in the confocal images for displacement of β-lg from the oil-water interface at ambient temperature upon addition of the nonionic surfactant Tween 20 at surfactant/protein ratios up to R = 2. Rather, such competitive displacement was observed to be induced only on heating, so that finally the surfactantcoated droplets became phase-separated inactive filler particles within the heat-set protein gel network.…”

Section: Introductionmentioning

confidence: 98%

“…By analyzing the fluorescence intensities within different regions in the sample, we were able to describe the migration of protein during thermal processing in a semiquantitative way. 41 In this paper, we first present some new data on the same β-lg-stabilized emulsion system containing excess protein (no added surfactant) in the presence of added sodium chloride. Then we describe the effects of the addition of (1) anionic SDS and (2) cationic cetyl trimethyl ammonium bromide (CTAB) on the properties of the same heat-set emulsion gel system (no added salt).…”

Section: Introductionmentioning

confidence: 99%

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Influence of Ionic Surfactants on the Microstructure of Heat-Set β-Lactoglobulin-Stabilized Emulsion Gels

et al. 2006

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Using confocal microscopy, we studied the effect of heating (up to 85°C) on the microstructure of β-lactoglobulin-stabilized emulsions (20 vol% oil, pH 6.8) containing excess protein (total protein content 13.2%). Two different fluorescent dyes were used to separately visualize the oil droplets and the protein. In overlay micrographs, their location with respect to each other could then be determined. In the presence of a low salt concentration, flocculation of the emulsion without surfactant was inhibited, by a mechanism analogous to the "salting-in" of aqueous protein solutions. Addition of the anionic surfactant sodium dodecyl sulfate (SDS) caused weak flocculation, probably as a result of the formation of protein−SDS complexes. The final heat-set emulsion contained distinct pores for a surfactant/protein ratio of R = 1, but no pores for R = 2. Addition of the cationic surfactant cetyl trimethyl ammonium bromide (CTAB) caused strong aggregation, as indicated by microscopic observation of the concentrated emulsion and light scattering of the diluted emulsion. For R = 1 with CTAB, there were aggregates consisting of oil droplets and excess protein. At R = 2, almost all the excess protein was aggregated into separate protein flakes. In the final emulsion gels containing CTAB, the protein was more spread out. Differing structural behavior with anionic and cationic surfactants has been interpreted in terms of different protein−surfactant interactions in aqueous solution and at the oil−water interface, both before and after protein denaturation.

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Section: Introductionmentioning

confidence: 87%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Influence of Ionic Surfactants on the Microstructure of Heat-Set β-Lactoglobulin-Stabilized Emulsion Gels

et al. 2006

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“…Low molecular weight surfactants are much smaller in size than biopolymers; thus they can reduce interfacial tension more efficiently and quickly by adsorbing a large number of molecules within the same surface area. If both are present at high enough bulk concentrations they are likely to dominate at the interface after equilibration [69][70][71][72].…”

Section: Selection Of Surface Active Agentmentioning

confidence: 99%

Improving Product Quality with Entrapped Stable Emulsions: From Theory to Industrial Application

Panagiotou

Fisher

2012

Challenges

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Entrapment of sub-micron scale emulsions containing active ingredients into macro-scale matrices has exhibited great potential as a delivery vehicle with controlled release capabilities, however optimization remains unrealized. Reported here are methods used to improve product quality by optimizing the emulsion formation steps. These methods are in conjunction with the precepts of Process Intensification (PI). Success with pharmaceutics and chemical reacting systems provides a strategy for a wide range of applications; the emphasis here being nutraceutics. Use of a nano-technology platform assists in: (a) product quality improvements through better nutrient dispersion, and thus bio-efficacy; and (b) production efficiencies through implementation of PI concepts. A continuous methodology, utilizing these PI concepts, that approximates a bottom-up approach to the creation of sub-micron and nano-emulsions is the basis of the technology presented here. Note that solid particles may result during post-processing. The metrics of successful processing include obtainment of nano-scale species with minimal input energy, reduced processing steps at higher throughput rates, and improved quality without over-usage of key ingredients. In addition to flavor and wellness characteristics, product stability for extended shelf life along with an appreciable cargo load in the entrapped emulsion is a major concern. Experimental protocols and path forward recommendations to overcome challenges and meet expectations in these emerging opportunities are also presented.

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Double emulsions of immiscible polymer blends stabilized by interfacially active nanoparticles

Huang

et al. 2013

AIChE Journal

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The stability of particle‐stabilized double emulsions under flow is of great scientific and technical interest in many fields. In this work, a two‐step mixing procedure was adopted to produce double emulsions based on viscous polyisobutylene (PIB)/polydimethylsiloxane (PDMS) blends and a small amount of interfacially active hydrophobic silica nanoparticles were used to stabilize the morphology. The structures of nanoparticle‐stabilized double emulsions with varying blend ratios and nanoparticle concentrations were investigated via optical microscopy and rheology technique. It was found that increasing the nanoparticle content effectively facilitated the formation of double emulsion droplets under shear flow and improved their stabilities. Rheology results suggested that these nanoparticle‐stabilized double emulsions displayed a slower relaxation dynamics. Decreasing the concentration of dispersed phase was in favor of the generation of more stable double emulsions, possibly due to the higher particle coverage at the interface between two phases. © 2013 American Institute of Chemical Engineers AIChE J, 59: 4373–4382, 2013

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Microstructure of β-lactoglobulin-stabilized emulsions containing non-ionic surfactant and excess free protein: Influence of heating

Cited by 47 publications

References 53 publications

Influence of Ionic Surfactants on the Microstructure of Heat-Set β-Lactoglobulin-Stabilized Emulsion Gels

Influence of Ionic Surfactants on the Microstructure of Heat-Set β-Lactoglobulin-Stabilized Emulsion Gels

Improving Product Quality with Entrapped Stable Emulsions: From Theory to Industrial Application

Double emulsions of immiscible polymer blends stabilized by interfacially active nanoparticles

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