Dynamics of mixed protein–surfactant layers adsorbed at the water/air and water/oil interface

Krägel, J.; O’Neill, M.; Makievski, A. V.; Michel, Martin; Leser, Martin E.; Miller, R.

doi:10.1016/s0927-7765(03)00047-x

Cited by 75 publications

(75 citation statements)

References 12 publications

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“…In these studies the globular protein β-lactoglobulin (BLG), which is the major protein in the whey of ruminant milk [2] and plays important function in the binding and transportation of retinol, has attracted more and more attention [3][4][5][6][7][8][9][10]. The reported studies were focused on the interaction of BLG with single surfactants [9][10][11][12][13][14][15][16][17][18][19][20], but rarely with the mixture of surfactants [21].…”

Section: Introductionmentioning

confidence: 99%

Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures

Cao

Lai

et al. 2006

Journal of Colloid and Interface Science

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Section: Introductionmentioning

confidence: 99%

Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures

Cao

Lai

et al. 2006

Journal of Colloid and Interface Science

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“…18,20 The β-lg−SDS complex is more hydrophobic and has a higher surface activity than the native protein, making it more difficult to displace from the interface. 39,51 Hence, for R = 1, it is possible that most, if not all, of the SDS present is bound to the protein. This implies that the droplets would be stabilized by adsorbed β-lg-SDS complexes, rather than by pure β-lg alone, and that the excess β-lg-SDS complexes prefer the vicinity of the complex-coated oil droplets above that of the surrounding solvent.…”

Section: Discussionmentioning

confidence: 98%

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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“…Another reason may be the fact that minor components only present in the unrefined corn germ oil form complexes that lead to a higher surface tension. It is known that in liquid-liquid systems with proteins, the addition of a small amount of a surfactant can increase the interfacial tension [14].…”

Section: Interfacial Tensionmentioning

confidence: 99%

Interfacial tension and density measurement of the system corn germ oil – carbon dioxide at low temperatures

Dittmar

Arevalo

Beckmann

et al. 2005

Eur. J. Lipid Sci. Technol.

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In this article, the physical properties of corn germ oil at high pressures of up to 30 MPa and at low temperatures from −10 °C to 22 °C are presented. We measured the interfacial tension of the commercially available corn germ oil Mazola® and of unrefined corn germ oil in contact with carbon dioxide, as well as the density of carbon dioxide‐saturated corn germ oil. The interfacial tension of refined and unrefined corn germ oil in contact with gaseous carbon dioxide at temperatures above −10 °C depends on time, while at higher pressures the equilibrium value of the interfacial tension is reached immediately after the formation of the drops or bubbles. The interfacial tension of unrefined corn germ oil in contact with carbon dioxide is higher than the interfacial tension of refined corn germ oil. This fact is explained in this article. The interfacial tension of refined and of unrefined corn germ oil in contact with carbon dioxide decrease with rising pressure and can be described as a function of the carbon dioxide density for the examined temperature range. The density of carbon dioxide‐saturated corn germ oil is linearly dependent on pressure, with a high slope if carbon dioxide is gaseous and with a low slope if carbon dioxide is liquid.

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Dynamics of mixed protein–surfactant layers adsorbed at the water/air and water/oil interface

Cited by 75 publications

References 12 publications

Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures

Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures

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

Interfacial tension and density measurement of the system corn germ oil – carbon dioxide at low temperatures

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