Interfacial composition and stability of emulsions made with mixtures of commercial sodium caseinate and whey protein concentrate

The interfacial composition and the stability of oil-in-water emulsion droplets (30% soya oil, pH 7.0) made with mixtures of sodium caseinate and whey protein concentrate (WPC) (1:1 by protein weight) at various total protein concentrations were examined. The average volume-surface diameter (d₃₂) and the total surface protein concentration of emulsion droplets were similar to those of emulsions made with both sodium caseinate alone and WPC alone. Whey proteins were adsorbed in preference to caseins at low protein concentrations (<3%), whereas caseins were adsorbed in preference to whey proteins at high protein concentrations. The creaming stability of the emulsions decreased markedly as the total protein concentration of the system was increased above 2% (sodium caseinate >1%). This was attributed to depletion flocculation caused by the sodium caseinate in these emulsions. Whey proteins did not retard this instability in the emulsions made with mixtures of sodium caseinate and WPC.     

Interfacial properties of deamidated wheat protein in relation to its ability to stabilise oil-in-water emulsions

Isolated wheat protein (IWP) is an acidic deamidated wheat protein. The deamidation process enhances the protein solubility at pHs greater than 6, and therefore its potential ability to act as a food emulsifier. The interfacial properties and the mechanism by which this protein stabilises oil-in-water emulsions were investigated by measuring the protein's absorbed layer thickness on latex particles, its interfacial rheology, and the colloidal and thermal stability of IWP stabilised emulsions. IWP forms a relatively thick interfacial layer of 18 nm upon adsorption onto latex beads, suggesting that the protein adsorbed with the long axis perpendicular to the surface, i.e. end-on, at a full protein coverage. The interfacial rheology measurement showed that IWP formed a relatively weak fluid-like interface. Similar to other protein emulsifiers, the colloidal stability of IWP emulsions is provided largely through electrostatic repulsion. Although IWP emulsions were sensitive to salt induced flocculation, the presence of excess protein in the aqueous phase (e.g. 4 wt%) was able to reduce the effect of salt screening (50 mM CaCl₂) on a 25 wt% oil-in-water emulsion completely. The emulsions underwent minimal coalescence when droplets were in close contact, e.g. flocculated, because the interfacial layer of IWP provides a barrier to droplet coalescence, even in high salt environments. IWP emulsions were resistant to thermal treatment with no changes in particle size observed when the emulsions were heated (up to 90 °C for 20 min) in the absence or the presence of 150 mM NaCl. The heat stability of IWP emulsions is thought to arise from the structure of IWP at the interface. A lack of free cysteines combined with few hydrophobic regions meant that there were minimal interactions between protein molecules adsorbed onto the same droplet or on neighbouring droplets. The unique interfacial properties of IWP, e.g. its physical layer thickness and the structure provide enhanced stability for emulsions against coalescence and heating.     

Characterisation of emulsion properties and of interface composition in O/W emulsions prepared with hen egg yolk, plasma and granules

Comprehension of hen egg yolk emulsifying properties remains incomplete because competition between its various emulsifiers (proteins and lipoproteins containing phospholipids) has not been clearly elucidated and colloidal interactions between yolk-stabilised oil droplets have not been documented. Recent studies emphasised the interest of the fractionation of yolk into plasma and granules to improve this comprehension. In the present study, we characterised, concurrently, emulsion properties (oil droplet size and stability against creaming) and interface attributes (interfacial concentrations of proteins and phospholipids, SDS-PAGE profiles of adsorbed proteins and zeta potential) in oil-in-water (O/W) emulsions prepared with yolk, plasma and granules. We observed these features at four physicochemical conditions (pH 3.0 or 7.0 and at 0.15 or 0.55 M NaCl). Emulsion properties in emulsions made with yolk or plasma varied similarly as a function of pH and NaCl concentration whereas granules emulsions exhibited distinct properties. Therefore the main contributors to yolk emulsifying properties are to be sought for among plasma constituents (proteinaceous or phospholipids). Since, in plasma emulsions, variations of emulsion stability against creaming correlated exclusively to variations of protein interfacial concentration, a driving contribution of the proteinaceous part of plasma, namely apo-LDL, was hypothesised. In the pH and ionic strength ranges studied, zeta potentials of the interfaces were low, excluding extended electrostatic repulsion between oil droplets. We deduced that steric repulsion is the main interaction opposing to droplet aggregation in food emulsions made with yolk.     

Characterisation of fish oil emulsions stabilised by sodium caseinate

Fish oil emulsions varying in sodium caseinate concentration (25% w/w oil and 0.1–1.0% w/w protein, giving oil-to-protein ratios of 250–25) were investigated in terms of their creaming stability, rheological properties, the mobility of oil droplets and the oil/protein interaction at the interface. The presence of excessive protein in an emulsion (i.e., at 1% w/w) caused the aggregation of oil droplets through depletion flocculation, resulting in low creaming stability and high low-shear viscosity. At a lower protein concentration (0.1% w/w), when protein was limited, the emulsion droplets were stabilised by bridging flocculation and showed good stability to creaming. Shear-thinning behaviour was observed for both flocculated emulsions. A reduction in the low-shear viscosity and a Newtonian flow was obtained for the emulsion containing an intermediate concentration of protein (0.25% w/w). At this concentration, there was relatively little excess unadsorbed protein in the continuous phase; thus the emulsion was most stable to creaming. NMR was used to characterise these emulsion systems without dilution. Shorter T₂ values (by low-field ¹H NMR), for the emulsions containing both high (1% w/w) and low (0.1% w/w) amounts of protein, indicated increased restricted mobility of oils, caused by depletion or bridging flocculation. The line broadening in oil signals in the high-field NMR spectra (¹H, ¹³C) indicated increased interaction between oil molecules and proteins at the interface with increasing protein concentration in emulsions. In addition, ³¹P NMR spectra, which reflect the mobility of the casein component only, showed increased line broadening, with reduction in protein content due to the relatively higher proportion of the protein being adsorbed to the interface of the oil droplets, compared to that in the continuous phase (i.e., as the oil-to-protein ratio was increased). The T₂ values of resonances of the individual groups on oil molecules, obtained using high-field ¹H NMR, reflected their different environments within the oil droplet.     

Formation of nanostructured colloidosomes using electrostatic deposition of solid lipid nanoparticles onto an oil droplet interface

This study describes the assembly of colloidosomes by adsorbing solid lipid nanoparticles (SLN) onto the interfaces of oil-in-water emulsion droplets via electrostatic deposition technique. Oil-in-water emulsions (10% w/w corn oil, 1% w/w whey protein isolate in water) and SLN (10% octadecane, 1% sodium dodecyl sulfate in water) were prepared using a microfluidizer. The surface saturation concentration (C_sat) of negatively charged SLN adsorbed onto the positively charged oil-in-water emulsions (at oil droplet concentration of 0.5%) at pH 3 was investigated by measuring ζ-potential, and particle size, as well as assessing the microstructure by optical microscopy. Each of these methods depicted C_sat between 1.1–1.5% (w/w). The results were explained by calculating theoretical C_sat using molecular forces acting between the adsorbed droplets as described by the DLVO theory. We demonstrated that the surface saturation of SLN on emulsion droplets depends on the particle size population.     

Crosslinking of interfacial layers in multilayered oil-in-water emulsions using laccase: Characterization and pH-stability

The enzymatic crosslinking of polymer layers adsorbed at the interface of oil-in-water emulsions was investigated. A sequential two step process, based on the electrostatic deposition of pectin onto a fish gelatin interfacial membrane was used to prepare emulsions containing oil droplets stabilized by fish gelatin-beet pectin membranes (citrate buffer, 10 mM, pH 3.5). First, a fine dispersed primary emulsion (5% soybean oil (w/v), 1% (w/w) gelatin solution) (citrate buffer, 10 mM, pH 3.5) was produced using a high pressure homogenizer. Second, a series of secondary emulsions were formed by diluting the primary emulsion into pectin solutions (0 - 0.4% (w/w)) to coat the droplets. Oil droplets of stable emulsions with different oil droplet concentrations (0.1%, 0.5%, 1.0% (w/v)) were subjected to enzymatic crosslinking. Laccase was added to the fish gelatin-beet pectin emulsions and emulsions were incubated for 15 min at room temperature. The pH- and storage stability of primary, secondary and secondary, laccase-treated emulsions was determined. Results indicated that crosslinking occurred exclusively in the layers and not between droplets, since no aggregates were formed. Droplet size increased from 350 to 400 nm regardless of oil droplet concentrations within a matter of minutes after addition of laccase suggesting formation of covalent bonds between pectin adsorbed at interfaces and pectin in the aqueous phase in the vicinity of droplets. During storage, size of enzymatically treated emulsions decreased, which was found to be due to enzymatic hydrolysis. Results suggest that biopolymer-crosslinking enzymes could be used to enhance stability of multilayered emulsions.     

Physical characteristics of submicron emulsions upon partial displacement of whey protein by a small molecular weight surfactant and pectin addition

O/W emulsions (6 wt.% olive oil) were prepared at pH 3.3 using different WPI:Tween 20 weight ratios (1:0, 3:1, 1:1, 1:3, 0:1) at 1 wt.% total concentration. The emulsion droplet size was found to decrease with an increase in Tween 20. A minimum droplet size of d_3,2 300 nm was found for Tween systems alone, similar to that found (360 nm) for a 1:1 WPI:Tween 20 combination (p < 0.05). This specific composition showed a value for the interfacial tension close to that of Tween 20 alone. However, the emulsions presented low stability regardless of the WPI:Tween 20 ratio. To increase their stability, pectin was added, in various concentrations (0.2, 0.4 and 0.6 wt.%), using the Layer by Layer technique. In the presence of pectin, the ζ-potential of the oil droplets became negative; indicating that negatively charged pectin was absorbed onto the positively-charged droplet surface forming a secondary layer. The additional layer resulted in a wide range of emulsion stability. For all pectin concentrations, the 1:1 ratio of WPI:Tween 20 showed the highest stability. In most emulsions, extensive aggregation of oil droplets was observed, and their viscosity increased. Insufficient amounts of pectin to form the secondary layers led to bridging flocculation phenomena of oppositely charged pectin and proteins, leading to aggregation of the oil droplets. The higher the concentration of pectin, the greater the stability of the emulsion due to higher viscosity. All in all, the addition of a second layer consisting of pectin can be used to increase the stability of an emulsion containing emulsion droplets in the sub-micron range.     

Influence of chitosan and NaCl on physicochemical properties of low-acid tuna oil-in-water emulsions stabilized by non-ionic surfactant

An influence of low molecular weight (LMW) chitosan on physicochemical properties and stability of low-acid (pH 6) tuna oil-in-water emulsion stabilized by non-ionic surfactant (Tween 80) was studied. The mean droplet diameter, droplet charge (ζ-potential), creaming stability and microstructure of emulsions (5 wt% oil) were evaluated. The added chitosan was adsorbed on the surface of oil droplets stabilized by Tween 80 through electrostatic interactions. Such addition of chitosan at different concentrations (0–10 wt%) to emulsions showed slight effect on the mean droplet diameter. However, the degree of flocculation was a function of chitosan concentration assessed by emulsions' microstructure and creaming index. The impact of chitosan on the strength of the colloidal interaction between the emulsion droplets increased with increasing chitosan concentration. The mean diameter of droplet in emulsions increased with increasing NaCl because of the electrostatic screening effect. The addition of LMW chitosan could be performed to create tuna oil emulsions with low-acid to neutral character, as well as various physicochemical and stability properties suitable for health food products.     

Pea protein exhibits a novel Pickering stabilization for oil-in-water emulsions at pH 3.0

In this paper we reported that pea protein isolate (PPI) at pH 3.0 exhibits a novel Pickering stabilization for oil-in-water emulsions. At pH 3.0, most of the proteins in PPI were present in the nanoparticle form, with the hydrodynamic diameter of 134–165 nm depending on the concentration (c; 0.25–3.0 g/100 mL). For the emulsions formed at a specific oil fraction of 0.2, increasing the c from 0.25 to 3.0 g/100 mL resulted in a considerable reduction in the emulsion size, while their creaming stability progressively increased, and especially at c values higher than 2 g/100 mL, no creaming occurred even after storage of 20 days. Confocal laser scanning microscopy observations showed that increasing the c resulted in a progressive increase in extent of droplet flocculation, and at higher c values, a network consisting of flocculated droplets could be formed. The emulsions formed at c values above 1.0 g/100 mL exhibited extraordinary stability against coalescence. The flocculated droplet network formation was closely associated with the increased amount of adsorbed proteins at the interface. The results suggest that pea proteins exhibit a good potential to act as a kind of Pickering stabilizers for oil-in-water emulsions at acidic pHs.     

Factors Influencing the Freeze‐Thaw Stability of Emulsion‐Based Foods

Many of the sauces used in frozen meals are oil‐in‐water emulsions that consist of fat droplets dispersed within an aqueous medium. This type of emulsion must remain physically and chemically stable throughout processing, freezing, storage, and defrosting conditions. Knowledge of the fundamental physicochemical mechanisms responsible for the stability of emulsion‐based sauces is needed to design and fabricate high‐quality sauces with the desired sensory attributes. This review provides an overview of the current understanding of the influence of freezing and thawing on the stability of oil‐in‐water emulsions. In particular, it focuses on the influence of product composition (such as emulsifiers, biopolymers, salts, and cryoprotectants), homogenization conditions, and freezing/thawing conditions on the stability of emulsions. The information contained in this review may be useful for optimizing the design of emulsion‐based sauces for utilization in commercial food products.     

Aspects of milk-protein-stabilised emulsions

Milk proteins are widely used as ingredients in prepared foods, in which they perform a wide range of key functions, including emulsification, thickening, gelling and foaming. An important functionality of milk proteins in food colloids is their ability to facilitate the formation and stabilisation of oil droplets in emulsions. The ability of milk proteins to adsorb at the oil–water interface and to stabilise emulsions has been exploited by the food industry in the manufacture of nutritional products, specialised medical foods, dietary formulations, cream liqueurs and dairy desserts. This article provides an overview of the properties and functionalities of food emulsions formed with milk proteins, focusing on the structure and composition of adsorbed protein layers, competition between proteins and the physical and chemical stability of emulsion droplets. Of particular importance is the understanding of the behaviour of milk-protein-based emulsions under the conditions relevant to digestion in the human gastrointestinal tract. Recent relevant research in this area is reviewed and discussed.     

Heat stability of oil-in-water emulsions formed with intact or hydrolysed whey proteins: influence of polysaccharides

The heat stability of emulsions (4 wt% corn oil) formed with whey protein isolate (WPI) or extensively hydrolysed whey protein (WPH) products and containing xanthan gum or guar gum was examined after a retort treatment at 121 °C for 16 min. At neutral pH and low ionic strength, emulsions stabilized with both 0.5 and 4 wt% WPI (intact whey protein) were stable against retorting. The amount of β-lactoglobulin (β-lg) at the droplet surface increased during retorting, especially in the emulsion containing 4 wt% protein, whereas the amount of adsorbed α-lactalbumin (α-la) decreased markedly. Addition of xanthan gum or guar gum caused depletion flocculation of the emulsion droplets, but this flocculation did not lead to their aggregation during heating. In contrast, the droplet size of emulsions formed with WPH increased during heat treatment, indicating that coalescence had occurred. The coalescence during heating was enhanced considerably with increasing concentration of polysaccharide in the emulsions, up to 0.12% and 0.2% for xanthan gum and guar gum, respectively; whey peptides in the WPH emulsions formed weaker and looser, mobile interfacial structures than those formed with intact whey proteins. Consequently, the lack of electrostatic and steric repulsion resulted in the coalescence of flocculated droplets during retort treatment. At higher levels of xanthan gum or guar gum addition, the extent of coalescence decreased gradually, apparently because of the high viscosity of the aqueous phase.     

Emulsification by the phase inversion temperature method: the role of self-bodying agents and the influence of oil polarity

Oil-in-water emulsions stabilized with nonionic emulsifiers change to water-in-oil emulsions as the temperature rises when the hydrophilic and lipophilic properties of the mixed emulsifier are just balanced. Preparation above the phase inversion temperature followed by rapid cooling yields emulsions that exhibit very fine droplet size and extreme long-term stability. Cosmetic emulsions were prepared by this phase inversion temperature (PIT) method using typical raw materials such as polar oils, e.g. decyl oleate, 2-octyl dodecanol or isopropyl myristate, and nonionic emulsifiers, e.g. ceteareth-12 or polyoxyethylene eicosyl/docosyl ether combined with cetostearyl alcohol as a co-emulsifier. The phase inversion temperature was measured as a function of the oil polarity and the concentration of mixed emulsifier. The relationship between phase inversion temperature, droplet size and emulsion stability was investigated. In addition, self-bodying agents such as cetostearyl alcohol or monoglycerides were added to these thin, fine disperse emulsions to adjust the consistency. The influence of these ingredients on phase inversion temperature, droplet size, yield value and emulsion stability was studied.     

Utilisation of pectin coating to enhance spray-dry stability of pea protein-stabilised oil-in-water emulsions

In this study, development of pea (Pisum sativum) protein stabilised dry and reconstituted emulsions is presented. Dry emulsions were prepared by spray-drying liquid emulsions in a laboratory spray-dryer. The effect of drying on the physical stability of oil-in-water emulsions containing pea protein-coated and pea protein/pectin-coated oil droplets has been studied. Oil-in-water emulsions (5 wt.% Miglyol 812 N, 0.25 wt.% pea protein, 11% maltodextrin, pH 2.4) were prepared that contained 0 (primary emulsion) or 0.2 wt.% pectin (secondary emulsion). The emulsions were then subjected to spray-drying and reconstitution (pH 2.4). The stability of the emulsions to dry processing was then analysed using oil droplet size, microstructure, Zeta potential, and creaming measurements. Obtained results showed that the secondary emulsions had better stability to droplet aggregation after drying than primary emulsions. To interpret these results, we propound that pectin, an anionic polysaccharide, formed a less charged protective layer around the protein interfacial film surrounding the oil droplets that improved their stability to spray-drying mainly by increasing steric effects.     

乳状液成分对O/W乳状液性质的影响

采用单因素实验设计,通过机械搅拌方法制备O/W乳状液。通过乳状液的离心稳定性、粘度和乳状液的显微结构,研究不同HLB值的复合乳化剂及含量、脱脂乳粉溶液的浓度以及油和水比例对乳状液性质的影响,最终确定较佳的乳状液成分。实验结果表明:当以Span-80和Tween-80为复合乳化剂,其HLB值为9.6、复合乳化剂含量为16%(w/w)、脱脂乳粉溶液浓度为25%(w/v)、油与水比为1∶1(w/w)时,可以获得状态较好的乳状液,此时乳状液的离心稳定性最高,可以达到97.5%。     

Colloidal stability and interactions of milk-protein-stabilized emulsions in an artificial saliva

Oil-in-water emulsions (20 wt% soy oil) with lactoferrin or β-lactoglobulin (β-lg) as the interfacial layer were prepared using a two-stage valve homogenizer. At pH 6.8, lactoferrin produces a stable cationic emulsion whereas β-lg forms an anionic emulsion. These emulsions were mixed with an artificial saliva that contained a range of mucin concentrations and salts. Negatively charged mucin was shown to interact readily with the positively charged lactoferrin-stabilized emulsion droplets to provide a mucin coverage of approximately 1 mg/m². As expected, the negatively charged β-lg-stabilized emulsion droplets had lower mucin coverage (0.6 mg/m² surface load) under the same conditions. The β-lg-stabilized emulsions were stable but showed depletion flocculation at higher mucin levels (≥1.0 wt%). In contrast, lactoferrin-stabilized emulsion droplets showed considerable aggregation in the presence of salts but in the absence of mucin. This salt-induced aggregation was reduced in the presence of mucin, possibly because of its binding to the positively charged lactoferrin-stabilized emulsion droplets and thus a reduction in the positive charge at the lactoferrin-coated droplet surface. However, at higher mucin concentration (≥2.0 wt%), lactoferrin-stabilized emulsions also showed droplet aggregation.     

Monitoring air/liquid partition of mastic gum oil volatiles in model alcoholic beverage emulsions: Effect of emulsion composition and oil droplet size

The purpose of this work was to study the impact of the structure and composition of hydroalcoholic emulsions on the air–liquid partition of aroma compounds of the essential oil of Pistacia lentiscus var. chia, commonly known as mastic gum oil (mainly consists of terpenes). Oil-in-water emulsions (φ = 0.17), containing 15% (v/v) ethanol, stabilized by three different emulsifiers (sodium caseinate, whey protein isolate and Tween 40), were prepared by using two different lipid phases (sunflower oil and anhydrous butter fat). The homogenization conditions were varied to obtain emulsions with different volume–surface mean diameters. The partition of the volatile compounds between air phase and emulsions at three different temperatures (25, 37 and 50 °C) was monitored by applying the Headspace Solid Phase Microextraction technique, followed by gas chromatography–mass spectrometry (GC–MS) analysis. In general, the results obtained showed that sodium caseinate was the most effective in retaining mastic aroma compounds, while WPI was the least effective. This could partly be explained by the different structure of the two proteins which, when adsorbed at the interface, form a membrane that acts as a barrier and influences the partition of the aroma compounds between the air and the liquid. At the same time interactions of aroma compounds with the two proteins in the bulk phase may also play a role. The retention of the aroma compounds depended on the oil droplet size only in the case of sodium caseinate containing emulsions at 37 and 50 °C. This behaviour could be due to the substantial increase in the thickness of the adsorbed casein layer when moving from a fine sized emulsion to one with a much larger size as well as to differences in the ratio of free to adsorbed emulsifier. The composition of the lipid phase also appeared to have a significant impact on the concentration of volatile compounds in the headspace of mastic gum oil containing emulsions stabilized by proteins. This was lower in the case of butter fat probably due to differences in composition with regard to fatty acid degree of saturation as well as to volatile absorption by the liquid lipid at 40 °C and subsequent entrapment in the semisolid fat at 25 °C.     

Aqueous and enzymatic extraction processes for the production of food-grade proteins and industrial oil from dehulled yellow mustard flour

Aqueous extraction is an emerging alternative to hexane-based oilseed extraction since it eliminates the dangers associated with processing, and allows the simultaneous recovery of high-quality protein products and vegetable oils. Five different successive non-enzymatic and enzymatic aqueous extraction processes (AEPs/EAEPs) were developed for dehulled yellow mustard flour with the aim of producing food-grade protein and yellow mustard oil for industrial applications. The oil released in these processes was tied up in oil-in-water emulsions that must be destabilized to recover free oil prior to industrial utilization. This study endeavored to ascertain the extraction parameters that increase oil and protein extraction yields and reduce emulsion stability during successive AEPs/EAEPs for dehulled yellow mustard flour. The remarkable stability of the emulsions was due to the presence of protein emulsifiers of high molecular weight along with the mixed phospholipid–oleosin layer. pH adjustment for emulsion destabilization was relatively inefficient; therefore, enzymatic demulsification treatments with different proteases and phospholipases were evaluated for their ability to release free oil by hydrolyzing the targeted emulsifiers. Although protease treatments with Protex 6 L at a concentration of 2.5 wt.% were effective in recovering over 91% of the oil in the emulsions, phospholipase treatments did not modify the free oil recovery from the emulsions. The results indicated that the enzymatic aqueous extraction of dehulled yellow mustard flour did not offer sufficient improvement in usable protein recovery to warrant the extra effort and cost.     

Conversion of aqueous extracts from thermochemical treatment of bagasse into functional emulsifiers

Synthetic emulsifiers in food industries are being replaced with a customer-friendly food ingredient that is derived from biomass using sustainable green technologies. After hydrothermal liquefaction treatment, raw bagasse (21%), pith (26%), and rind portions (25%) were obtained with reduced ash contents. As aqueous extracts, with oligosaccharides and lignin residues, it was used in the preparation of oil-in-water emulsions with 5% soybean oil. Results showed that the emulsions stabilised the oil droplets with particle size between 11 and 17 µm by steric repulsion with raw bagasse-stabilised emulsion showing a better stability at 25 °C (31 days). It was demonstrated that raw bagasse extracts, without alteration, maybe a potential unconventional source for food-grade emulsifiers by integrating a versatile thermochemical conversion of waste without the use of chemicals.     

Study of emulsions stabilized with Phaseolus vulgaris or Phaseolus coccineus with the addition of Arabic gum, locust bean gum and xanthan gum

The properties of o/w emulsions stabilized with 1%w/v common bean (Phaseolus vulgaris L.), V or scarlet runner bean (P. coccineus L.), Coc extracted by isoelectric precipitation or ultrafiltration, at pH 7.0 and 5.5, with the addition of Arabic gum, locust bean gum, xanthan gum and a mixture of xanthan gum–locust bean gum (0.1 %w/v and 0.25 %w/v) are studied. The stability of emulsions was evaluated on the basis of oil droplet size, creaming, viscosity and protein adsorption measurements. The addition of Arabic gum, caused an increase in D[4,3] values and a decrease in the amount of protein adsorbed at the interface. The addition of locust bean gum in some emulsions reduced the amount of protein adsorbed. The addition of xanthan and to a less extend of the polysaccharide mixture, promoted a decrease in D[4,3]. So, emulsion stability was affected by the polysaccharide nature. Differences were also observed with respect to the protein nature, the method of its preparation and emulsion's pH. All polysaccharides enhanced the emulsions viscosity with xanthan and xanthan–locust bean gum exhibiting the higher values. V isolates and isoelectricaly precipitated isolates of both V, Coc showed higher viscosity values. The stability was enhanced by the increase of the viscosity of the continuous phase and the creation of a network, which prevents the oil droplets from coalescence.