Multiple Emulsion Stability: Pressure Balance and Interfacial Film Strength

2007 ◽  
pp. 1-27 ◽  
Author(s):  
Jim Jiao ◽  
Diane J. Burgess
Keyword(s):  
Emulsion Stability ◽  
Multiple Emulsion ◽  
Pressure Balance ◽  
Interfacial Film

Multiple Emulsion Stability: Pressure Balance and Interfacial Film Strength

2002 ◽  
Vol 250 (2) ◽  
pp. 444-450 ◽  
Author(s):  
Jim Jiao ◽  
David G. Rhodes ◽  
Diane J. Burgess
Keyword(s):  
Emulsion Stability ◽  
Multiple Emulsion ◽  
Pressure Balance ◽  
Interfacial Film

scholarly journals Effect of Surfactant Molecular Structure on Emulsion Stability Investigated by Interfacial Dilatational Rheology

Polymers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1127
Author(s):  
Yuejie Jin ◽  
Dingrong Liu ◽  
Jinhua Hu
Keyword(s):  
Emulsion Stability ◽  
Chain Structure ◽  
Interfacial Film ◽  
Future Design ◽  
Rheological Method ◽  
Viscoelastic Modulus ◽  
Hydrophobic Chain ◽  
Branched Chain ◽  
The Stability ◽  
Branched Structure

Polyglycerol polyricinolate (PGPR) and polyglycerol-2 dioleate were selected as model surfactants to construct water-in-oil (W/O) emulsions, and the effect of interfacial rheological properties of surfactant film on the stability of emulsions were investigated based on the interfacial dilatational rheological method. The hydrophobicity chain of PGPR is polyricinic acid condensed from ricinic acid, and that of polyglycerol-2 dioleate is oleic acid. Their dynamic interfacial tensions in 15 cycles of interfacial compression-expansion were determined. The interfacial dilatational viscoelasticity was analyzed by amplitude scanning in the range of 1–28% amplitude and frequency sweep in the range of 5–45 mHz under 2% amplitude. It was found that PGPR could quickly reach adsorption equilibrium and form interfacial film with higher interfacial dilatational viscoelastic modulus to resist the deformation of interfacial film caused by emulsion coalescence, due to its branched chain structure and longer hydrophobic chain, and the emulsion thus presented good stability. However, polyglycerol-2 dioleate with a straight chain structure had lower interfacial tension, and it failed to resist the interfacial disturbance caused by coalescence because of its lower interfacial dilatational viscoelastic modulus, and thus the emulsion was unstable. This study reveals profound understanding of the influence of branched structure of PGPR hydrophobic chain on the interfacial film properties and the emulsion stability, providing experimental reference and theoretical guidance for future design or improvement of surfactant.

The Influence Faction to the Crude Oil Emulsion Stability

2012 ◽  
Vol 502 ◽  
pp. 330-334
Author(s):  
Hong Jing Zhang
Keyword(s):  
Crude Oil ◽  
Emulsion Stability ◽  
Solid Particles ◽  
Stable Emulsion ◽  
Oil Emulsion ◽  
Interfacial Film ◽  
The World

At present, the exploited crude oil is about 80% in the presence of crude oil emulsion in the world. More and more research to study stability of the crude oil is developed. Firstly, the basal knowledge of the crude oil emulsion and interfacial film are introduced in this paper. The main reason that crude oil can come into being stable emulsion is it has natural emulsifiers, which can form interfacial film, then the author emphasizes on four natural emulsifiers of the crude oil’s components: asphaltenes, gelatine, paraffine and solid particles, which play very important role in the crude oil emulsion’s stability. The natural emulsifiers, such as asphaltenes, gelatine, can be absorbed between water and oil to form interfacial film that has some visco-elasticity. The stronger is interfacial film, the more stable is the crude oil emulsion.

Influence of Thermal Treatment and Soy Bean Protein Characteristics on Muscle Protein Emulsion Stability

2006 ◽  
Vol 12 (3) ◽  
pp. 195-204 ◽  
Author(s):  
M. P. Rodríguez ◽  
C. Regue ◽  
A. Bonaldo ◽  
C. Carrara ◽  
L. G. Santiago
Keyword(s):  
Heat Treatment ◽  
Soy Protein ◽  
Emulsion Stability ◽  
Muscle Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Stable Emulsion ◽  
Protein Isolates ◽  
Interfacial Film ◽  
Soy Protein Isolates

The effects of heat treatment on the interaction of salt soluble muscle protein and soy protein isolate in model emulsions were studied. Three soy protein isolates (SPI) were used: a commercial one (CSPI) and two pilot plant samples: a native soy protein isolate (NSPI) and an acid treated soy protein isolate (ASPI). Emulsions were prepared with muscle protein (MP), NSPI, ASPI, CSPI and mixtures of MP and the different SPIs, and then treated at 20, 55, 70, 80 and 90°C. Coalescence, soluble protein and electrophoresis of the aqueous phase of the emulsions were evaluated for each temperature. At 20°C the more native soy protein (NSPI) was compatible with MP, producing a stable emulsion that became more stable during heat treatment. CSPI alone could not form a stable interfacial film through the temperature range, however emulsion stabilisation was achieved at 55°C and 70°C when adding MP. Emulsions prepared with MP ASPI were highly unstable at 20°C, while as the emulsion temperature increased, coalescence decreased abruptly and maintained low values at every temperature. MP, NSPI, ASPI and MP NSPI produced stable emulsions both at 20°C and higher temperatures.

Investigation of multiple emulsion stability using rheological measurements

1994 ◽  
Vol 91 ◽  
pp. 215-225 ◽  
Author(s):  
C. Py ◽  
J. Rouvière ◽  
P. Loll ◽  
M.C. Taelman ◽  
Th.F. Tadros
Keyword(s):  
Emulsion Stability ◽  
Multiple Emulsion ◽  
Rheological Measurements

Interaction of Soy Protein Isolate and Meat Protein in a Model Emulsion System. Effect of Emulsification Order and Characteristics of Soy Isolate Used

2005 ◽  
Vol 11 (2) ◽  
pp. 79-88 ◽  
Author(s):  
L. G. Santiago ◽  
C. Carrara ◽  
R. J. González
Keyword(s):  
Soy Protein ◽  
Emulsion Stability ◽  
Surface Hydrophobicity ◽  
Soy Proteins ◽  
Emulsion System ◽  
System Effect ◽  
Interfacial Film ◽  
Meat Protein ◽  
Soy Isolate ◽  
Meat Proteins

The compatibility of soy proteins with meat protein (MP) in an emulsion system was examined. Three types of soy protein were employed: a commercial soy isolate (CSPI) and two pilot plant samples, an acid treated (ASPI) and a native soy isolate (NSPI). The incorporation of different isolates and the emulsification order affect in a different way the coalescence stability of emulsions prepared with meat proteins. Physicochemical characteristics (surface hydrophobicity, sulfhydryl content, solubility) of the soy proteins cannot explain the different behaviours towards emulsion stability, although the more native sample (NSPI) performed better than the more denature samples (ASPI or CSPI). The addition of NSPI did not modify the high coalescence stability of meat protein emulsion and the effect of the emulsification order was not significant (p 0.05), which suggested compatibility between both proteins. However, the addition of ASPI or CSPI impaired the emulsion stability. When ASPI was emulsified before MP, ASPI inhibited meat protein adsorption and emulsion became highly stable; while when MP was emulsified before or together with ASPI, meat proteins could be displaced from the interfacial film by the ASPI and the emulsion stability was deteriorated. As regards CSPI, all emulsions were highly unstable to coalescence although fractions of both proteins were found in the interfacial film. It could be suggested a mechanism of competitive adsorption when MP is emulsified together with ASPI or CSPI.(

Correlation Between Nature of Emulsifier and Multiple Emulsion Stability

1985 ◽  
Vol 11 (4) ◽  
pp. 791-798 ◽  
Author(s):  
S. Magdassi ◽  
M. Frenkel ◽  
N. Garti
Keyword(s):  
Emulsion Stability ◽  
Multiple Emulsion
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