Monitoring Entering and Spreading of Emulsion Droplets at an Expanding Air/Water Interface: A Novel Technique

Hotrum, N.E.; Vliet, T. van; Stuart, Martien A. Cohen; Aken, George A. van

doi:10.1006/jcis.2001.8124

Cited by 31 publications

(28 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…If liquid droplets enter and spread at the interface then this will lead to bubble instability [93], but this is only likely to occur if the surface of the bubbles and/or droplets are depleted in adsorbed protein, which is unlikely if the foam and emulsion have reasonable stability separately. Schokker et al [94] introduced an elegant method for measuring the spreading of an oil droplet at the air-water interface and how this is affected by the coherence of the adsorbed protein film on the droplet.…”

Section: Particle-stabilized Systemsmentioning

confidence: 97%

Stabilization of bubbles and foams

Murray

2007

Current Opinion in Colloid & Interface Science

282

174

View full text Add to dashboard Cite

Section: Particle-stabilized Systemsmentioning

confidence: 97%

Stabilization of bubbles and foams

Murray

2007

Current Opinion in Colloid & Interface Science

282

174

View full text Add to dashboard Cite

“…This situation is an analogy to the spreading of oil-droplets at the air-water interface. In this case, a simple calculation of the spreading coefficient [51] will tell whether the oil droplet spreads or if it keeps its globular form.…”

Section: Adsorption Behaviormentioning

confidence: 99%

The adsorption and unfolding kinetics determines the folding state of proteins at the air–water interface and thereby the equation of state

Wierenga¹,

Egmond²,

Voragen³

et al. 2006

Journal of Colloid and Interface Science

View full text Add to dashboard Cite

Unfolding of proteins has often been mentioned as an important factor during the adsorption process at air-water interfaces and in the increase of surface pressure at later stages of the adsorption process. This work focuses on the question whether the folding state of the adsorbed protein depends on the rate of adsorption to the interface, which can be controlled by bulk concentration. Therefore, the adsorption of proteins with varying structural stabilities at several protein concentrations was studied using ellipsometry and surface tensiometry. For β-lactoglobulin the adsorbed amount (Γ ) needed to reach a certain surface pressure (Π) decreased with decreasing bulk concentration. Ovalbumin showed no such dependence. To verify whether this difference in behavior is caused by the difference in structural stability, similar experiments were performed with cytochrome c and a destabilized variant of this protein. Both proteins showed identical Π-Γ , and no dependence on bulk concentration. From this work it was concluded that unfolding will only take place if the kinetics of adsorption is similar or slower than the kinetics of unfolding. The latter depends on the activation energy of unfolding (which is in the order of 100-300 kJ/mol), rather than the free energy of unfolding (typically 10-50 kJ/mol).

show abstract

“…Interfacial techniques have been developed to study the interfacial behaviour of various superstructures like liposomes [20], lipid nanocapsules [21], hen egg yolk low-density lipoproteins [22] and emulsion droplets [23] at the air-water interface. Those data showed that the Langmuir balance can be used as a tool for studying the general organisation, structure and stability of such particles when spread at the air-water interface.…”

Section: Introductionmentioning

confidence: 99%