Protein-stabilized emulsions

McClements, David Julian

doi:10.1016/j.cocis.2004.09.003

Cited by 876 publications

(506 citation statements)

References 42 publications

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“…In such a case, BSA acted as a surface active agent. During the adsorption, the protein changes its structural conformation so that physical chemical interactions at the interface become more favorable [35,36].…”

Section: Microparticle Morphologymentioning

confidence: 99%

Drug release mechanisms of chemically cross-linked albumin microparticles: Effect of the matrix erosion

Sitta

Guilherme

Silva

et al. 2014

Colloids and Surfaces B: Biointerfaces

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A c c e p t e d M a n u s c r i p t Page 4 of 25 A c c e p t e d M a n u s c r i p tsphericity. In such a case, BSA played a role as a surface active agent, replacing PVA. For longer stirring times, BSA was unable to act as an emulsifier.These microparticles showed an uncommon release profile, consisting of a two-step release mechanism, at the pH range studied. Considering that a two-step release mechanism is occurring, the experimental data were adjusted by applying modified power law and Weibull equations in order to describe release mechanism n and release rate constant k, respectively. Each one of the release stages was related to a specific value of n and k. The second stage was driven by a super case II transport mechanism, as a result of diffusion, macromolecular relaxation, and erosion. A third model, described by Hixson-Crowell, confirmed the erosion mechanism.Vit-B 12 diffusion kinetics in aqueous solutions (i.e., without the microparticles) follows a one-step process, being k dependent on the pH, confirming that the two-step release mechanism is a characteristic profile of the developed microparticles. The microparticles released only 2.70% of their initial drug load at pH 2, and 58.53% at pH 10.

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Section: Microparticle Morphologymentioning

confidence: 99%

Drug release mechanisms of chemically cross-linked albumin microparticles: Effect of the matrix erosion

Sitta

Guilherme

Silva

et al. 2014

Colloids and Surfaces B: Biointerfaces

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“…The thick interfacial layer confers strong and long ranged steric repulsion on the freshly formed oil droplets and protects fine droplets against flocculation and hence coalescence (Dickinson, 1999;Surh, et al, 2006). Caseinate (CAS) covered emulsions are more stable to elevated temperature treatments when compared with whey protein stabilized emulsions since in contrast to the globular proteins, e.g., whey proteins, casein molecules are relatively flexible and do not develop heatinduced structural changes (McClements, 2004;Surh, et al, 2006). One drawback of CAS-stabilized emulsion is their susceptibility to droplet flocculation at pH close to the isoelectric point (pH 4.6) of the casein since this drastically reduces the electrostatic repulsion between the oil droplets (Perrechil & Cunha, 2010;Surh, et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…Upon freezing and chilling, oil-in-water emulsions are significantly destabilized, and then readily broken down after thawing (McClements, 2004). Deep under-cooling of emulsions may induce crystallization, and consequently the formation of a fat crystal network in the oil droplets.…”

Section: Introductionmentioning

confidence: 99%

“…The resultant dried emulsions either can be easily used as food ingredients, e.g., flavoring agents, or can be reconstituted with water by the consumer, e.g., dairy creamers (McClements, 2004). There is a growing interest in freeze drying of emulsions in the pharmaceutical industry since the dried emulsions are easy to handle and physically stable ingredients (Christensen, Pedersen, & Kristensen, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…There is a growing interest in freeze drying of emulsions in the pharmaceutical industry since the dried emulsions are easy to handle and physically stable ingredients (Christensen, Pedersen, & Kristensen, 2002). During the dehydration step of freeze drying process, the removal of water from the protein may lead to a loss of protein functionality and stability (McClements, 2004).…”

Section: Introductionmentioning

confidence: 99%

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Influence of pH value and locust bean gum concentration on the stability of sodium caseinate-stabilized emulsions

2013

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Sodium caseinate emulsions of 20% sunflower oil in water were prepared at various pH and Locust Bean Gum concentrations (LBG). The presence of LBG was examined to assess the stabilizing properties in relation to flocculation, creaming and coalescence, in the initial emulsions as well freezethawed and freeze-dried/reconstituted samples. We found the initial emulsions to be stable at pH 6 and 6.5, both in absence or presence of LBG, against creaming. However we found evidence for the presence of emulsion droplet aggregates in the presence of LBG. Strong shear thinning behavior, even at low shear rates, and micrographs indicated that the presence of LBG may promote flocculation by mediating depletion forces between the oil droplets. However, the absence or low concentrations of LBG resulted in creaming followed by the emulsion break-up for the freezedried/reconstituted emulsions, particularly at lower pH. We have also detected a proliferation in the number of very small sub-micron particles in the particle size distribution, for samples containing higher concentrations of LBG, following the freeze-thaw cycle. We believe these to be LBG aggregates nucleating during the freezing phase of the process as the polysaccharide solubility declines with temperature.

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Applications of High‐Pressure Homogenization and Microfluidization for Milk and Dairy Products

Tobin¹,

Heffernan²,

Mulvihill³

et al. 2015

Emerging Dairy Processing Technologies

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Protein-stabilized emulsions

Cited by 876 publications

References 42 publications

Drug release mechanisms of chemically cross-linked albumin microparticles: Effect of the matrix erosion

Drug release mechanisms of chemically cross-linked albumin microparticles: Effect of the matrix erosion

Influence of pH value and locust bean gum concentration on the stability of sodium caseinate-stabilized emulsions

Applications of High‐Pressure Homogenization and Microfluidization for Milk and Dairy Products

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