Biomedical subjects

David J McClements

Publications and source records attributed to David J McClements.

5 recordsLinked to original sources

PubMed2006

Stabilization of model beverage cloud emulsions using protein-polysaccharide electrostatic complexes formed at the oil-water interface.

The potential of utilizing interfacial complexes, formed through the electrostatic interactions of proteins and polysaccharides at oil-water interfaces, to stabilize model beverage cloud emulsions has been examined. These interfacial complexes were formed by mixing charged polysaccharides with oil-in-water emulsions containing oppositely charged protein-coated oil droplets. Model beverage emulsions were prepared that consisted of 0.1 wt % corn oil droplets coated by beta-lactoglobulin (beta-Lg), beta-Lg/alginate, beta-Lg/iota-carrageenan, or beta-Lg/gum arabic interfacial layers (pH 3 or 4). Stable emulsions were formed when the polysaccharide concentration was sufficient to saturate the protein-coated droplets. The emulsions were subjected to variations in pH (from 3 to 7), ionic strength (from 0 to 250 mM NaCl), and thermal processing (from 30 or 90 degrees C), and the influence on their stability was determined. The emulsions containing alginate and carrageenan had the best stability to ionic strength and thermal processing. This study shows that the controlled formation of protein-polysaccharide complexes at droplet surfaces may be used to produce stable beverage emulsions, which may have important implications for industrial applications.

Alginates↗

PubMed2006

Influence of pH and ionic strength on formation and stability of emulsions containing oil droplets coated by beta-lactoglobulin-alginate interfaces.

Emulsions of 0.1 wt % corn oil-in-water containing oil droplets coated by beta-lactoglobulin (0.009 wt % beta-Lg, 5 mM phosphate buffer, pH 7.0) were prepared in the absence and presence of sodium alginate (0 or 0.004 wt %). The pH (3-7) and ionic strength (0-250 mM NaCl) of these emulsions were adjusted, and the particle charge, particle size, and creaming stability were measured. Alginate adsorbed to the beta-Lg-coated droplets from pH 3 to 6, which was attributed to electrostatic attraction between the anionic polymer and cationic patches on the droplet surfaces. Droplets coated by beta-Lg-alginate had better stability to flocculation than those coated by beta-Lg alone, especially around the isoelectric point of the adsorbed proteins and at low ionic strengths (< 100 mM NaCl). At pH 5, alginate molecules desorbed from the droplet surfaces at high salt concentrations due to weakening of the electrostatic attraction.

Alginates↗

PubMed2004

Effect of surfactant type on surfactant-maltodextrin interactions: isothermal titration calorimetry, surface tensiometry, and ultrasonic velocimetry study.

Isothermal titration calorimetry (ITC), surface tensiometry, and ultrasonic velocimetry were used to characterize surfactant-maltodextrin interactions in buffer solutions (pH 7.0, 10 mM NaCl, 20 mM Trizma base, 30.0 degrees C). Experiments were carried out using three surfactants with similar nonpolar tail groups (C12) but different charged headgroups: anionic (sodium dodecyl sulfate, SDS), cationic (dodecyl trimethylammonium bromide, DTAB), and nonionic (polyoxyethylene 23 lauryl ether, Brij35). All three surfactants bound to maltodextrin, with the binding characteristics depending on whether the surfactant headgroup was ionic or nonionic. The amounts of surfactant bound to 0.5% w/v maltodextrin (DE 5) at saturation were < 0.3 mM Brij35, approximately 1-1.6 mM SDS, and approximately 1.5 mM DTAB. ITC measurements indicated that surfactant binding to maltodextrin was exothermic. Surface tension measurements indicated that the DTAB-maltodextrin complex was more surface active than DTAB alone but that SDS- and Brij35- maltodextrin complexes were less surface active than the surfactants alone.

Calorimetry, Differential Scanning↗

PubMed2004

Two-dimensional rotating-frame Overhauser spectroscopy (ROESY) and (13)C NMR study of the interactions between maltodextrin and an anionic surfactant.

Rotational frame nuclear Overhauser effect spectroscopy (ROESY) and (13)C NMR measurements were carried out to study the molecular interaction between maltodextrin, a digestive byproduct of starch, and an anionic surfactant. Significant differences in chemical shifts were observed when sodium dodecyl sulfate (SDS) was introduced into the maltodextrin (DE 10) solutions. (13)C NMR measurement indicated that there were downfield shifts and broadening of peaks, especially in the region of 75-81 and 100-103 ppm, which were assigned to carbons 1 and 4 of the d-glucopyranose residues of maltodextrin, respectively. ROESY spectra indicated cross-peaks between the SDS and maltodextrin protons. These peaks can arise only in the case of the designated SDS protons and maltodextrin protons being less than 0.5 nm apart for a substantial period of time. The most intense cross-peaks are those between the central CH(2) protons of SDS near 1.2 ppm and the maltodextrin protons ranging from 3.5 to 3.9 ppm. The SDS-H3 CH(2) protons were resolved from the bulk of the SDS protons, with peaks and shoulders at 1.25 ppm, which indicated an especially strong interaction of the SDS hydrophobic tail with MD6 and some less intense interactions with MD2, 4, and 5.

Anions↗

PubMed2003

Influence of sucrose on droplet flocculation in hexadecane oil-in-water emulsions stabilized by beta-lactoglobulin.

The influence of sucrose on the flocculation stability of hydrocarbon oil-in-water emulsions stabilized by a globular protein was examined using laser diffraction. Salt (150 mM NaCl) and sucrose (0-40 wt %) were added to n-hexadecane oil-in-water emulsions stabilized by beta-lactoglobulin (beta-Lg, pH 7.0) either before or after isothermal heat treatment (30-95 degrees C for 20 min). When salt was added to emulsions before heat treatment, appreciable droplet flocculation was observed below the thermal denaturation temperature of the adsorbed beta-Lg (T(m) approximately 70 degrees C), and more extensive flocculation was observed above T(m). On the other hand, when salt was added to emulsions after heat treatment, appreciable droplet flocculation still occurred below T(m), but little flocculation was observed above T(m). Addition of sucrose to the emulsions increased T(m) and either promoted or suppressed droplet flocculation depending on whether it was added before or after heat treatment. These results are interpreted in terms of the influence of sucrose on protein conformational stability, protein-protein interactions, and the physiochemical properties of aqueous solutions. This study has important implications for the formulation and production of protein stabilized oil-in-water emulsions.

Adsorption↗