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David Julian McClements

Publications and source records attributed to David Julian McClements.

5 recordsLinked to original sources

Impact of electrostatic interactions on formation and stability of emulsions containing oil droplets coated by beta-lactoglobulin-pectin complexes.

Interfacial protein-polysaccharide complexes can be used to improve the physical stability of oil-in-water emulsions. The purpose of this study was to examine the impact of ionic strength on the formation and stability of oil-in-water emulsions containing polysaccharide-protein-coated droplets. Emulsions were prepared that contained 0.1 wt % corn oil, 0.05 wt % beta-lactoglobulin, and 0.02 wt % pectin at pH 7. The emulsions were then adjusted to pH 4 to promote electrostatic deposition of the pectin molecules onto the surfaces of the protein-coated droplets. The salt concentration of the aqueous phase (0 or 50 mM NaCl) was adjusted either before or after deposition of the pectin molecules onto the droplet surfaces. We found that stable emulsions containing polysaccharide-protein-coated droplets could be formed when the salt was added after pectin adsorption but not when it was added before pectin adsorption. This phenomenon was attributed to the ability of NaCl to promote droplet flocculation in the protein-coated droplets so that the pectin molecules adsorbed onto the surfaces of flocs rather than individual droplets when salt was added before pectin adsorption. We also found that polysaccharide-protein-coated droplets had a much improved stability to salt-induced flocculation than protein-coated droplets with the same droplet charge (zeta-potential). Theoretical predictions indicated that this was due to the ability of the adsorbed polysaccharide layer to strongly diminish the van der Waals attraction between the droplets.

Adsorption↗

Non-covalent interactions between proteins and polysaccharides.

Foods with novel or improved properties can be created by utilizing non-covalent interactions between proteins and polysaccharides. In solution, either attractive or repulsive interactions between proteins and polysaccharides can be used to create microstructures that give foods novel textural and sensory properties. At interfaces, attractive electrostatic interactions can be used to create food emulsions with improved stability to environmental stresses or with novel encapsulation-release characteristics.

Biopolymers↗

Theoretical prediction of emulsion color.

The perceived quality of many commercial products that are based on emulsions is determined by their color. In this article, a theory is presented to relate the color of emulsions to their composition and microstructure. First, the scattering characteristics (Qs and g) of individual droplets are calculated using Mie Theory. Second, the scattering (S) and absorption (K) coefficients of a concentrated emulsion are calculated using radiative transfer theory. Third, the reflectance spectrum (R) of the emulsion is calculated using Kubelka-Munk Theory. Finally, the tristimulus coordinates (XYZ, or L*a*b*) of the emulsion are calculated using color theory. There is excellent agreement between theoretical predictions and experimental measurements of the influence of droplet and chromophore characteristics on the tristimulus coordinates of concentrated oil-in-water emulsions.

Journal Article↗

Influence of oil polarity on droplet growth in oil-in-water emulsions stabilized by a weakly adsorbing biopolymer or a nonionic surfactant.

The influence of oil type (n-hexadecane, 1-decanol, n-decane), droplet composition (hexadecane:decanol), and emulsifier type (Tween 20, gum arabic) on droplet growth in oil-in-water emulsions was studied. Droplet size distributions of emulsions were measured over time (0-120 h) by laser diffraction and ultrasonic spectroscopy. Emulsions containing oil molecules of low polarity and low water solubility (hexadecane) were stable to droplet growth, irrespective of the emulsifier used to stabilize the droplets. Emulsions containing oil molecules of low polarity and relatively high water solubility (decane) were stable to coalescence, but unstable to Ostwald ripening, irrespective of emulsifier. Droplet growth in emulsions containing oil molecules of relatively high polarity and high water solubility (decanol) depended on emulsifier type. Decanol droplets stabilized by Tween 20 were stable to droplet growth in concentrated emulsions but unstable when the emulsions were diluted. Decanol droplets stabilized by gum arabic exhibited rapid and extensive droplet growth, probably due to a combination of Ostwald ripening and coalescence. We proposed that coalescence was caused by the relatively low interfacial tension at the decanol-water boundary, which meant that the gum arabic did not absorb strongly to the droplet surfaces and therefore did not prevent the droplets from coming into close proximity.

Journal Article↗

Modulation of globular protein functionality by weakly interacting cosolvents.

Globular proteins are utilized in food, pharmaceutical, and health-care products because of their unique functional attributes, for example, enzyme catalysis, ligand binding and transport, surface activity and self-association. The expression of these functional attributes in a particular product depends on the molecular structure, chemical environment and thermal-mechanical history of the proteins. The optimization of the design and operation of processing technologies used to manufacture protein-containing materials depends on a thorough understanding of the influence of processing conditions and material composition on protein properties. This paper focuses on the impact of weakly interacting neutral cosolvents (such as sugars and polyols) on the structural, thermodynamic and functional properties of globular proteins in foods. The physicochemical mechanisms by which these cosolvents can modulate protein functionality are highlighted, that is, differential interactions and steric exclusion. Previous studies of the impact of cosolvents on protein functionality that are relevant to foods are reviewed, for example, water solubility, stabilization, emulsification, foaming, gelation, enzyme catalysis, and flavor binding.

Dietary Proteins↗