Assessing the potential of flaxseed protein as an emulsifier combined with whey protein isolate

The potential use of flaxseed protein isolate (FPI) as an emulsifying agent was studied in combination with whey protein isolate (WPI) or alone. All the FPI and WPI–FPI emulsions were kinetically unstable. The increase of FPI concentration (0.7% w/v) led to a higher creaming stability of the FPI emulsions due partly to a reduction in interfacial tension between aqueous and oil phases, but mainly to the gel network formation. However at this same high FPI concentration, WPI–FPI emulsions showed a decrease in droplet size and creaming stability, which could be due to the presence of flaxseed gum in the protein isolate enhancing depletion effects. A protein excess was verified in the mixed systems (0.14 or 0.7% (w/v) FPI) and the increase of FPI concentration led to an even greater surface protein content. Increasing homogenization conditions (pressure and number of passes), the creaming stability of the FPI systems increased, mainly at higher concentration (0.7% w/v). Meanwhile, in the mixed systems, the creaming stability of the emulsions containing 0.7% (w/v) FPI decreased even more, but was improved for the emulsions with 0.14% (w/v) FPI. Thus, it was observed that systems containing only FPI at higher concentration were stabilized by gel formation, while in WPI–FPI systems there was a competition by interface between biopolymers with a consequent depletion process. As a result, more stable systems were obtained with WPI addition at lower FPI concentration (0.14% w/v) and using higher homogenization pressure and number of passes (60 MPa, two passes).     

Partition and digestive stability of α-tocopherol and resveratrol/naringenin in whey protein isolate emulsions

Co-encapsulation of multiple bioactive components is an emerging field that shows promise as an approach to develop functional foods. Hydrophobic components are generally dissolved in the inner oil phase of protein-stabilised emulsions. Some components may co-adsorb to oil droplet surfaces, due to the ligand-binding properties of proteins. In this study, α-tocopherol and resveratrol/naringenin were co-encapsulated in emulsions stabilised by whey protein isolate (WPI). α-Tocopherol was totally encapsulated and its partitioning inside oil droplets was about 3.3 times that bound by free WPI in the aqueous phase. The total encapsulation efficiency for resveratrol or naringenin was 52% and 58%, respectively. Addition of resveratrol improved digestive stability of α-tocopherol, but naringenin did not. Co-encapsulation with α-tocopherol had no significant influence on the digestive stability of resveratrol/naringenin. The data gathered here should be useful for the delivery of bioactive components with different solubilities.     

The effect of chitosan on the properties of emulsions stabilized by whey proteins

The influence of the cationic amino polysaccharide chitosan content (0–0.5%) on particle size distribution, creaming stability, apparent viscosity, and microstructure of oil-in-water emulsions (40% of rapeseed oil) containing whey protein isolate (WPI) (4%) at pH 3 was investigated. The emulsifying properties, apparent viscosity and phase separation behaviour of aqueous WPI/chitosan mixture at pH 3 were also studied. The interface tension data showed that WPI/chitosan mixture had a slightly higher emulsifying activity than had whey protein alone. An increase in chitosan content resulted in a decreased average particle size, higher viscosity and increased creaming stability of emulsions. The microstructure analysis indicated that increasing concentration of chitosan resulted in the formation of a flocculated droplet network. This behaviour of acidic model emulsions containing WPI and chitosan was explained by a flocculation phenomenon.     

Physicochemical and emulsifying properties of whey protein isolate (WPI)-polydextrose conjugates prepared via Maillard reaction

In this study, whey protein isolate (WPI) and polydextrose (PDX) were used to produce WPI-PDX covalent conjugates via dry-heating Maillard reaction, and their characteristics and functional properties including abilities to emulsify and stabilise the corn germ oil/water emulsions were measured. Compared with WPI alone, the WPI-PDX conjugates had higher water solubility and DPPH radical scavenging ability, and the derived emulsions exhibited good storage stability over 60 days prepared under these conditions: reaction time 24 h, conjugate concentration 4–6%, oil fraction ratio 0.6 and emulsion system pH 3–8. Further, we found that the emulsion possessed the best storage stability under the condition of 4% WPI-PDX conjugates and 0.6% oil fraction. These results provide a potent to prepare a beneficial Maillard conjugation following an optimised reaction condition and highlight the potential use of WPI-PDX conjugates as the emulsifier in food industry.     

Interfacial and emulsifying properties of lentil protein isolate

The dynamic interfacial tension (DIFT) at oil–water interface, diffusion coefficients, surface hydrophobicity, zeta potential and emulsifying properties, including emulsion activity index (EAI), emulsion stability index (ESI) and droplet size of lentil protein isolate (LPI), were measured at different pH and LPI concentration, in order to elucidate its emulsifying behaviour. Sodium caseinate (NaCas), whey protein isolate (WPI), bovine serum albumin (BSA) and lysozyme (Lys) were used as benchmark proteins and their emulsifying property was compared with that of LPI. The speed of diffusion-controlled migration of these proteins to the oil/water interface, was in the following order: NaCas > LPI > WPI > BSA > Lys, while their surface hydrophobicity was in the following order: BSA > LPI > NaCas > WPI > Lys. The EAI of emulsions stabilised by the above proteins ranged from 90.3 to 123.3 m²/g and it was 93.3 ± 0.2 m²/g in LPI-stabilised emulsion. However, the stability of LPI-stabilised emulsions was slightly lower compared to that of WPI and NaCas-stabilised emulsions at the same protein concentration at pH 7.0. The ESI of LPI emulsions improved substantially with decrease in droplet size when protein concentration was increased (20–30 mg/ml). Reduction of disulphide bonds enhanced both the EAI and ESI compared to untreated samples. Heat treatment of LPI dispersions resulted in poor emulsion stability due to molecular aggregation. The stability of LPI-stabilised emulsions was found to decrease in the presence of NaCl. This study showed that LPI can be as effective emulsifiers of oil-in-water emulsions as are WPI and NaCas at ?20 mg/ml concentrations both at low and neutral pH. The emulsifying property of LPI can be improved by reducing the intra and inter-disulphide bond by using appropriate reducing agents.     

Comparative study of the emulsifying and foaming properties of defatted coriander (Coriandrum sativum) seed flour and protein concentrate

Emulsifying and foaming properties were determined for coriander protein products (defatted flour and protein concentrate) at pH 4.0, 7.0 and 9.0 and the results compared with those obtained for defatted soybean flour. Mean oil droplet size and interfacial protein concentration was smallest for emulsions (∼17% oil, v/v) stabilized by the coriander protein concentrate, when compared to the coriander and soybean flours. Polypeptide composition of the interfacial protein membrane of the emulsions was different from the polypeptide composition present in the respective coriander flour and protein concentrate. In contrast, soybean flour-stabilized emulsions contained similar polypeptide composition to that of the flour. Soybean flour formed the greatest amount of foams at pH 4.0, 7.0 and 9.0 followed by the coriander flour, which had greater amounts of foam at pH 4.0 and 5.0. The foam stability of both the coriander flour and protein concentrate were significantly (P⩽0.05) less than those of the soybean flour. It was concluded that the reduced level of non-protein components in the coriander protein concentrate favoured increased surface activity at the oil–water interface but not at the air–water interface.     

Oil-in-Water Emulsions Stabilized by Sodium Caseinate or Whey Protein Isolate as influenced by Glycerol Monostearate

Competitive adsorption between glycerol monostearate (GMS) and whey protein isolate (WPI) or sodium caseinate was studied in oil-in-water emulsions (20 wt % soya oil, deionized water, pH 7). Addition of GMS resulted in partial displacement of WPI or sodium caseinate from the emulsion interface. SDS-PAGE showed that GMS altered the adsorbed layer composition in sodium caseinate stabilized emulsions containing < 1.0 wt % protein. Predominance of β-casein at the interface in the absence of surfactant was reduced in the presence of GMS. The distribution of α-lactalbumin and β-lactoglobulin between the aqueous bulk phase and the fat surface in emulsions stabilized with WPI was independent of the concentration of added protein or surfactant.     

Behaviour of oil droplets during spray drying of milk-protein-stabilised oil-in-water emulsions

The effects of spray drying on the behaviour of oil droplets in oil-in-water emulsions (12.0%, w/w, maltodextrin; 20.0%, w/w, soya oil) stabilised with either sodium caseinate or whey protein isolate (WPI) were examined as a function of protein concentration (0.5–5.0%, w/w). Spray drying and redispersion caused a shift in the droplet size distribution to larger values for all emulsions made using low protein concentrations (0.5–2.0%, w/w), in comparison with their respective parent emulsions. However, the droplet size distribution was affected only very slightly by spray drying when the protein concentration was above 2.0% (w/w). The effects of maltodextrin concentration (1.0–25.0%, w/w) on the behaviour of WPI-stabilised emulsions (0.5–10.0%, w/w, WPI, 20.0%, w/w, soya oil) were also examined. Emulsions containing low levels of maltodextrin showed marked re-coalescence during spray drying and redispersion even at a WPI concentration of 10.0% (w/w).     

Influence of EDTA and citrate on thermal stability of whey protein stabilized oil-in-water emulsions containing calcium chloride

The influence of calcium ions and chelating agents on the thermal stability of model nutritional beverages was examined. Oil-in-water emulsions (6.94% (w/v) soybean oil, 0.35% (w/v) WPI, 0.02% (w/v) sodium azide, 20 mM Tris buffer, 0–10 mM CaCl₂, and 0–40 mM EDTA or citrate, pH 7.0) were stored at temperatures between 30 and 120 °C for 15 min. The particle size, particle charge, creaming stability, rheology, and free-calcium concentration of the emulsions were then measured. In the absence of chelating agents, appreciable droplet aggregation occurred in emulsions held at temperatures from 80 to 120 °C, which led to increased emulsion particle diameter, shear-thinning behavior, apparent viscosity, and creaming instability. Addition of chelating agents to the emulsions prior to heating decreased, but did not prevent, droplet aggregation in the emulsions. EDTA was more effective than citrate in decreasing droplet aggregation. Heat treatment increased the amount of chelating agents required to prevent droplet aggregation in the emulsions. Free-calcium concentration and droplet surface potential was independent of heat-treatment temperature, indicating that the performance of the chelating agents in binding calcium ions was not affected by the heat treatment. It was suggested that increased hydrophobic attractive interactions between the droplets occurred during heating, which induced droplet aggregation.     

Influence of calcium-binding salts on heat stability and fouling of whey protein isolate dispersions

The effect of the calcium-binding salts (CBS), trisodium citrate (TSC), tripotassium citrate (TPC) and disodium hydrogen phosphate (DSHP) at concentrations of 1–45 mm on the heat stability and fouling of whey protein isolate (WPI) dispersions (3%, w/v, protein) was investigated. The WPI dispersions were assessed for heat stability in an oil bath at 95 °C for 30 min, viscosity changes during simulated high-temperature short-time (HTST) and fouling behaviour using a lab-scale fouling rig. Adding CBS at levels of 5–30 mm for TSC and TPC and 25–35 mm for DSHP improved thermal stability of WPI dispersions by decreasing the ionic calcium (Ca²⁺) concentration; however, lower or higher concentrations destabilised the systems on heating. Adding CBS improved heat transfer during thermal processing, and resulted in lower viscosity and fouling. This study demonstrates that adding CBS is an effective means of increasing WPI protein stability during HTST thermal processing.     

Lipid and water crystallization in protein-stabilised oil-in-water emulsions

Phase and state transitions occurring during freezing and thawing of oil-in-water emulsions with different water phase formulations, interfacial compositions and two lipid types were studied as crucial factors affecting emulsion stability. Emulsions containing 0–40% (w/w) sucrose in the water phase at pH 7, and 10, 20, 30, 40% (w/w) dispersed lipid phase (sunflower oil, SO or hydrogenated palm kernel oil, HPKO) with whey protein isolate, WPI, or sodium caseinate, NaCAS, (protein:lipid = 1:10 and 2:10) as emulsifier were prepared. Phase/state behaviour of the continuous and dispersed phases was determined by differential scanning calorimetry (DSC). Emulsion stability and morphology were derived from DSC data, gravitational separation and particle size analysis during 4 freeze-thaw cycles. Systems were stable when only lipid crystallization occurred. DSC data showed that lipid crystallization prior to water crystallization (i.e. emulsions containing HPKO) caused destabilisation at low sucrose concentrations (0, 2.5 and 5% w/w). Emulsions were stable if the dispersed oil phase crystallized after the dispersing water phase (i.e. emulsions containing SO). A concentration of sucrose ≥10% (w/w) in the aqueous phase gave stable emulsions. At 10:1 lipid to protein ratio, WPI showed better stabilising properties than NaCAS at 2.5 and 5% (w/w) sucrose. Double concentration of WPI (lipid:protein = 10:2) at 0% (w/w) sucrose significantly improved systems stability, whereas no positive effect was observed when the concentration of NaCAS was increased. From morphology study, in addition to lipid destabilisation, thickening and flocculation caused instability of the systems. These were extensive in systems containing WPI and were ascribed to interactions between whey proteins during thermal cycling.     

Tuna oil and Mentha piperita oil emulsions and microcapsules stabilised by whey protein isolate and inulin: characterisation and stability

Whey protein isolate (WPI) and its polysaccharide complexes have been widely used to prepare oil‐in‐water emulsions. The aim of this study was to evaluate the emulsions and spray‐dried microcapsules containing tuna oil and/or mint oil and stabilised by combination of WPI with inulin in terms of physicochemical characteristics and storage stability. Stable emulsions were formed before drying. Tuna oil + Mentha piperita oil emulsions had smaller viscosity, surface tension and size than did tuna oil emulsions. Surface morphology showed that spray‐dried microcapsules were spheres but had many dents and apparent shrinkage. During storage, tuna oil and tuna oil + M. piperita oil microcapsules became larger. In the blend oil microcapsules, menthone was reduced to form menthol, loss of DHA and EPA was slightly less, the degree of oxidation characterised using peroxide value and headspace propanal was less but basically greater than half of that of WTI microcapsules.     

Heat Stability of Oil-in-Water Emulsions Containing Milk Proteins: Effect of Ionic Strength and pH

Emulsions (20 wt% soybean oil; 2 wt% protein) made with caseinate at pH 7 and with whey protein isolate (WPI) at pH 7 and 3 were stable to heating at 90 and 121°C. WPI emulsions destabilized at pH values between 3.5 and 4.0. In the presence of KCI (12.5–200 mM), large particles were formed in WPI emulsions at pH 3 and the emulsions were viscous. At pH 7, moderate concentrations of KCI decreased the heat stability and gels were formed. KCI had less effect on WPI emulsions made at pH 3. Combining the emulsions with caseinate allowed some control of the heat-induced gelation.     

Ability of whey protein isolate and/or fish gelatin to inhibit physical separation and lipid oxidation in fish oil-in-water beverage emulsion

The effect of pH on the capability of whey protein isolate (WPI) and fish gelatin (FG), alone and in conjugation, to form and stabilize fish oil-in-water emulsions was examined. Using layer-by-layer interfacial deposition technique for WPI–FG conjugate, a total of 1% protein was used to prepare 10% fish oil emulsions. The droplets size distributions and electrical charge, surface protein concentration, flow and dynamic rheological properties and physiochemical stability of emulsions were characterize at two different pH of 3.4 and 6.8 which were selected based on the ranges of citrus and milk beverages pHs, respectively. Emulsions prepared with WPI–FG conjugate had superior physiochemical stability compare to the emulsions prepared with individual proteins. Higher rate of coalescence was associated with reduction in net charge and consequent decrease of the repulsion between coated oil droplets due to the proximity of pH to the isoelectric point of proteins. The noteworthy shear thinning viscosity, as an indication of flocculation onset, was associated with whey protein stabilized fish oil emulsion prepared at pH of 3.4 and gelatin stabilized fish oil emulsion made at pH of 6.8. At pH 3.4, it appeared that lower surface charge and higher surface area of WPI stabilized emulsions promoted lipid oxidation and production of hexanal.     

Effects of protein concentration and oil-phase volume fraction on the stability and rheology of menhaden oil-in-water emulsions stabilized by whey protein isolate with xanthan gum

The influences of protein concentration (0.2, 1, 2 wt%) and oil-phase volume fraction (5%, 20%, 40% v/v) on emulsion stability and rheological properties were investigated in whey protein isolate (WPI)-stabilized oil-in-water emulsions containing 0.2 wt% xanthan gum (XG). The data of droplet size, surface charge, creaming index, oxidative stability, and emulsion rheology were obtained. The results showed that increasing WPI concentration significantly affected droplet size, surface charge, and oxidative stability, but had little effect on creaming stability and emulsion rheology. At 0.2 wt% WPI, increasing oil-phase volume fraction greatly increased droplet size but no significant effect on surface charge. At 1 or 2 wt% WPI, increasing oil-phase volume fraction had less influence on droplet size but led to surface charge more negative. Increasing oil-phase volume fraction facilitated the inhibition of lipid oxidation. Meanwhile, oil-phase volume fraction played a dominant role in creaming stability and emulsion viscosity. The rheological data indicated the emulsions may undergo a behavior transition from an entropic polymer gel to an enthalpic particle gel when oil-phase volume fraction increased from 20% to 40% v/v.     

Characterization of Chemically and Thermally Treated Oil‐in‐Water Heteroaggregates and Comparison to Conventional Emulsions

Heteroaggregated oil‐in‐water (O/W) emulsions formed by targeted combination of oppositely charged emulsion droplets were proposed to be used for the modulation of physical properties of food systems, ideally achieving the formation of a particulate 3‐dimensional network at comparably low‐fat content. In this study, rheological properties of Quillaja saponins (QS), sugar beet pectin (SBP), and whey protein isolate (WPI) stabilized conventional and heteroaggregated O/W emulsions at oil contents of 10% to 60% (w/w) were investigated. Selected systems having an oil content of 30% (w/w) and different particle sizes (d₄₃ ≤ 1.1 or ≥16.7 μm) were additionally subjected to chemical (genipin or glutaraldehyde) and thermal treatments, aiming to increase network stability. Subsequently, their rheological properties and stability were assessed. Yield stresses (τ₀) of both conventional and heteroaggregated O/W emulsions were found to depend on emulsifier type, oil content, and initial droplet size. For conventional emulsions, high yield stresses were only observed for SBP‐based emulsions (τ₀,_SBP approximately 157 Pa). Highest yield stresses of heteroaggregates were observed when using small droplets stabilized by SBP/WPI (approximately 15.4 Pa), being higher than those of QS/WPI (approximately 1.6 Pa). Subsequent treatments led to significant alterations in rheological properties for SBP/WPI systems, with yield stresses increasing 29‐fold (glutaraldehyde) and 2‐fold (thermal treatment) compared to untreated heteroaggregates, thereby surpassing yield stresses of similarly treated conventional SBP emulsions. Genipin‐driven treatments proved to be ineffective. Results should be of interest to food manufacturers wishing to design viscoelastic food emulsion based systems at lower oil droplet contents.     

Coalescence Index of Protein-Stabilized Emulsions

A simple method is proposed to estimate coalescence stability of protein-stabilized emulsions. Coalescence was accelerated through agitation and measured by change in emulsion turbidity over time. A coalescence index (CI) was determined and used to compare emulsions stabilized with casein, whey (WPI) and soy protein isolates (SPI). CI increased when stirring rate increased. Casein produced more stable emulsions, followed by WPI and SPI. High homogenization pressure increased coalescence stability of WPI and SPI-stabilized emulsions and decreased coalescence stability of casein-stabilized emulsions. Microscopic examination, showed agitation of the emulsion had clearly induced formation of large oil droplets which acted as coalescence nuclei.     

Antioxidant properties of caseins and whey proteins in model oil-in-water emulsions

The oxidative stabilities of both wheyproteinisolate (WPI)- and sodiumcaseinate-stabilized linoleic acid emulsions with different droplet sizes, protein concentrations and protein concentrations in the continuous phase were examined by determining lipid hydroperoxide and hexanal in the headspace. Emulsions with small droplet size had greater oxidative stability than emulsions with large droplet size in both WPI and sodiumcaseinate-stabilized emulsions. Lipid oxidation was in general lowered by an increase in the protein concentration. At high protein concentrations, the antioxidative effect of the protein in the emulsions appeared to offset the effects of emulsion droplet size and protein type. Replacing the unadsorbed protein in the continuous phase with water markedly decreased the oxidative stability of the emulsions. In contrast, the oxidative stability of the emulsions increased with increasing protein concentration in the continuous phase. This suggests that the antioxidative mechanism of protein in the interfacial region, such as binding trace metal ions from the lipid phase and free-radical-scavenging activity, may involve a dynamic exchange process with protein molecules from the continuous phase.     

Iron-Catalyzed Oxidation of Menhaden Oil as Affected by Emulsifiers

The ability of Tween 20 and whey protein isolate (WPI) to influence lipid oxidation was investigated by evaluating the effects of emulsifier concentration and physical location on iron-catalyzed oxidation of emulsified Menhaden oil. Addition of Tween 20 or WPI to the aqueous phase of a 0.5 wt% Tween 20 stabilized emulsion increased lipid oxidation as determined by both thiobarbituric acid reactive substances (TBARS) and lipid peroxides. Tween 20 (2.0 wt%) and WPI (0.05–1.0 wt%) combinations inhibited TBARS formation 23–60%. Oxidation of a WPI-stabilized emulsion decreased with decreasing pH (3–7) but in a Tween 20 stabilized emulsion oxidation increased with decreasing pH. The low oxidation rate for the WPI-stabilized emulsion at pH 3 was increased when Tween 20 displaced WPI from the droplet interface. Results indicate that the oxidative stability of emulsifed Menhaden oil could be increased by controlling emulsifier type, location and concentration.     

Impact of whey protein isolates and concentrates on the formation of protein nanoparticles‐stabilised Pickering emulsions

Whey protein nanoparticles (NPs) were prepared by heat‐induced method. The influences of whey protein isolates (WPIs) and concentrates (WPCs) on the formation of NPs were first investigated. Then Pickering emulsions were produced by protein NPs and their properties were evaluated. After heat treatment, WPC NPs showed larger particle size, higher stability against NaCl, lower negative charge and contact angle between air and water. Dispersions of WPC NPs appeared as higher turbidity and viscosity than those of WPI NPs. The interfacial tension of WPC NPs (~7.9 mN/m at 3 wt% NPs) was greatly lower than that of WPI NPs (~12.1 mN/m at 3 wt% NPs). WPC NPs‐stabilised emulsions had smaller particle size and were more homogeneous than WPI NPs‐stabilised emulsions. WPC NPs‐stabilised emulsions had higher stability against NaCl, pH and coalescence during storage.