Ultra-High Pressure Homogenization enhances physicochemical properties of soy protein isolate-stabilized emulsions

The effect of Ultra-High Pressure Homogenization (UHPH, 100–300 MPa) on the physicochemical properties of oil-in-water emulsions prepared with 4.0% (w/v) of soy protein isolate (SPI) and soybean oil (10 and 20%, v/v) was studied and compared to emulsions treated by conventional homogenization (CH, 15 MPa). CH emulsions were prepared with non-heated and heated (95 °C for 15 min) SPI dispersions. Emulsions were characterized by particle size determination with laser diffraction, rheological properties using a rotational rheometer by applying measurements of flow curve and by transmission electron microscopy. The variation on particle size and creaming was assessed by Turbiscan® analysis, and visual observation of the emulsions was also carried out. UHPH emulsions showed much smaller d_3.2 values and greater physical stability than CH emulsions. The thermal treatment of SPI prior CH process did not improve physical stability properties. In addition, emulsions containing 20% of oil exhibited greater physical stability compared to emulsions containing 10% of oil. Particularly, UHPH emulsions treated at 100 and 200 MPa with 20% of oil were the most stable due to low particle size values (d_3.2 and Span), greater viscosity and partial protein denaturation. These results address the physical stability improvement of protein isolate-stabilized emulsions by using the emerging UHPH technology.     

Effect of pre- and post-heat treatments on the physicochemical,microstructural and rheological properties of milk protein concentrate-stabilised oil-in-water emulsions

The effect of heat treatment on the physical stability of milk protein concentrate (MPC) stabilised emulsions was investigated; 3% (w/w) MPC dispersions were preheated at 90 °C for 5 min at neutral pH prior to emulsification. Heat-treated (120 °C, 10 min) emulsions stabilised by preheated MPC had slightly fewer droplet–droplet interactions than that stabilised by unheated MPC because the whey proteins were pre-denatured (∼90% denaturation of the total whey proteins), which led to a reduction in subsequent heat-induced droplet–droplet and droplet–protein interactions. Emulsions stabilised by calcium-depleted MPC were also investigated. The presence of some non-micellar casein fractions gave better emulsification and may have conferred a protective stabilising effect on whey protein aggregation, in both the dispersed phase and the continuous phase during the secondary heat treatment. It was concluded that calcium manipulation and thermal modification of MPC can be utilised to control the functionality in oil-in-water emulsions.     

Emulsions stabilized by heat-treated collagen fibers

The emulsifying properties of collagen fiber were modified by heat treatment at temperatures ranging from 50 to 85 °C for 20 or 60 min. In addition to heat treatment, the influence of pH (3.5 and 9.2) and the emulsifying process (rotor-stator device and high-pressure homogenizer) were evaluated on oil-in-water emulsions stabilized by collagen fiber through visual analysis (stability), microstructure and rheological measurements. Emulsions homogenized using solely the rotor-stator device showed phase separation and a larger mean droplet size (d₃₂), except for the emulsion composed by non-heated collagen fiber. The alkaline emulsions showed lower kinetic stability, since collagen fibers have a lower net charge (zeta potential) at higher pH values, decreasing the electrostatic stability process. Heat treatment slightly decreased the protein charge and significantly reduced the insoluble protein content, suggesting a decrease in the emulsifying properties of the collagen fiber. The use of high-pressure homogenization (20-100 MPa) made it possible to produce acid emulsions with a reduced droplet size and distribution. At 20 MPa, the emulsions showed a higher d₃₂ value (between 3.17 and 1.18 μm), while at 60 and 100 MPa the emulsions presented lower d₃₂ values (between 0.74 and 0.94 μm) without any significant variation between the different heat-treated collagen fibers, but showing a noticeable decrease in emulsion viscosity and elasticity with increases in the homogenization pressure and heat treatment.     

Effects of ultrasound power on the properties of non-salt chicken myofibrillar protein emulsions

The present study was designed to investigate the effects of different ultrasonic powers (0–600 W) on the storage stability, rheological properties and microstructure of non-salt chicken myofibrillar protein (MP) emulsions. The Turbiscan stability index (TSI) values, storage modulus (G′) values, loss modulus (G″) values, viscosity values and droplet size of the MP emulsions first increased and then decreased with an increase in ultrasonic power. The results of the creaming index and TSI values showed that ultrasonic treatment effectively improved the storage stability of the emulsions compared with non-ultrasonic treatment. Meanwhile, sonication decreased the oil droplet size and the contact angles accompanied by an increase in G′ and G″ values and the viscosity. The oil droplets became smaller and more uniform distribution observed through the different kinds of microscopic analysis. The physical stability of non-salt MP emulsions treated with different ultrasonic powers was significantly enhanced, and ultrasonic treatment with 450 W power had the optimal efficiency for the stability of the emulsions.     

Emulsifying properties of pea protein/guar gum conjugates and mayonnaise application

Modified plant protein may be used as a healthy and more functional emulsifier in food products. The objective of this study was to evaluate the emulsifying properties of functionally enhanced pea protein (i.e. pea protein conjugated with guar gum, G-PPI) and its potential application to mayonnaise, compared with unmodified pea protein. Emulsions containing G-PPI were prepared at different pH, salt concentrations, protein concentrations and oil/water ratios. Mayonnaise samples were prepared using the pea proteins or egg yolk powder. Various characteristics of the emulsions, including droplet size, apparent viscosity, viscoelasticity and microstructure, were analysed. The emulsions with G-PPI had significantly increased stability of up to 89.4% and apparent viscosity of up to 48.62 mPa.s. The G-PPI emulsion had a smaller average droplet size of 934.4 nm at pH 7 compared with the PPI emulsion (stability 62.7%, apparent viscosity 22.8 mPa.s and droplet size 1664.8 nm). The pH, NaCl concentration, protein concentration and oil/water ratio greatly affected the emulsifying properties. The G-PPI mayonnaise at higher protein concentrations (6 or 8%) exhibited excellent emulsifying and rheological properties. The modified pea protein through the green modification process with natural polysaccharides could be used as a safe and functional emulsifier in different emulsified foods.     

Utilization of layer-by-layer interfacial deposition technique to improve freeze–thaw stability of oil-in-water emulsions

The freeze–thaw stability of 5 wt% hydrogenated palm oil-in-water emulsions (pH 3) containing droplets stabilized by sodium dodecyl sulfate (SDS)–chitosan–pectin membranes was studied. The multilayered interfacial membranes were created using an electrostatic layer-by-layer deposition method. The ζ-potential, mean particle diameter, fat destabilization, apparent viscosity and microstructure of the emulsions were used to examine the influence of freezing on their stability. Emulsions containing oil droplets stabilized only by SDS were highly unstable to droplet coalescence when either the oil phase became partially crystallized or the water phase crystallized. Emulsions containing oil droplets stabilized by SDS–chitosan membranes were stable to droplet coalescence, but unstable to droplet flocculation. Emulsions containing droplets stabilized by SDS–chitosan–pectin membranes were stable to both droplet coalescence and flocculation. The interfacial engineering technology utilized in this study could lead to the creation of food emulsions with improved stability to freeze–thaw cycling.     

Rheological and microstructural characterization of WPI-stabilized O/W emulsions exhibiting time-dependent flow behavior

The rheological behavior of oil-in-water (O/W) emulsions stabilized by whey protein isolate (WPI) and its relationship with the microstructural changes caused by shearing was studied. O/W emulsions (50, 55, and 60 g oil/100 g) were made using ultrasound and their rheological properties were determined by: flow curve test, constant shear rate test, and hysteresis loop test. Microstructural changes were evaluated in terms of droplet size and droplet size distribution. Emulsions containing 50 and 55 g oil/100 g showed a Newtonian behavior, whereas those with 60 g oil/100 g exhibited shear-thinning behavior. Under constant deformation, the apparent viscosity of the emulsions decreased with time. The hysteresis loop test revealed that increasing oil content increased the degree of thixotropy of the emulsions. Moreover, before and after the constant deformation test droplet size distributions did not show differences, indicating that the decrease in the apparent viscosity may be promoted by breakdown and further deformation and/or reorganization of oil droplets flocs. In turn, experimental data obtained from the constant shear rate test was fitted to a structural kinetic model. The rate constant values showed no particular trend with oil content and shear rate, implying that probably wall slip occurred at high shear rates and high oil contents.     

Emulsifying Properties of Legume Proteins Compared to β‐Lactoglobulin and Tween 20 and the Volatile Release from Oil‐in‐Water Emulsions

The emulsifying properties of plant legume protein isolates (soy, pea, and lupin) were compared to a milk whey protein, β‐lactoglobulin (β‐lg), and a nonionic surfactant (Tween 20). The protein fractional composition was characterized using sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis. The following emulsion properties were measured: particle diameter, shear surface ζ‐potential, interfacial tension (IT), and creaming velocity. The effect of protein preheat treatment (90 °C for 10 min) on the emulsifying behavior and the release of selected volatile organic compounds (VOCs) from emulsions under oral conditions was also investigated in real time using proton transfer reaction‐mass spectrometry. The legume proteins showed comparable results to β‐lg and Tween 20, forming stable, negatively charged emulsions with particle diameter d_3,2 < 0.4 μm, and maintained stability over 50 d. The relatively lower stability of lupin emulsions was significantly correlated with the low protein surface hydrophobicity and IT of the emulsion. After heating the proteins, the droplet size of pea and lupin emulsions decreased. The VOC release profile was similar between the protein‐stabilized emulsions, and greater retention was observed for Tween 20‐stabilized emulsions. This study demonstrates the potential application of legume proteins as alternative emulsifiers to milk proteins in emulsion products.     

Physical Stability of Whey Protein-stabilized Oil-in-water Emulsions at pH 3: Potential ω-3 Fatty Acid Delivery Systems (Part A)

ABSTRACT: The oxidative stability of polyunsaturated lipids can be improved by incorporating them in oil droplets surrounded by positively charged whey protein isolate (WPI) membranes. This study dealt with the factors that influence the physical properties of WPI-stabilized oil-in-water emulsions at pH 3. Emulsions containing 5 to 50 wt% corn oil and 0.5 to 5.0 wt% WPI (protein-to-oil ratio of 1:10) were prepared at pH 3. The apparent viscosity of the emulsions increased appreciably at oil concentrations ≥ 35 wt%; however, the particle size was relatively independent of oil concentration. The influence of NaCl (0 to 250 m M ) on the physical properties of 28 wt% emulsions was examined. Significant increases in mean particle size, apparent viscosity, and creaming instability occurred at ≥150 m M NaCl, which were attributed to flocculation induced by screening of the electrostatic repulsion between droplets. The influence of heat treatment (30°C to 90°C for 30 min) on 28 wt% emulsions was examined in the absence and presence of salt, respectively. At 0 m M NaCl, heating had little effect on the physical properties of the emulsions, presumably because the electrostatic repulsion between the droplets prevented droplet aggregation. At 150 m M NaCl, the mean particle diameter, apparent viscosity, and creaming instability of the emulsions increased considerably when they were heated above a critical temperature, which was 70°C when salt was added before heating and 90°C when salt was added after heating. These results have important implications for the design of WPI-stabilized emulsions that could be used to incorporate functional lipids that are sensitive to oxidation, for example, ω-3 fatty acids.     

Chia protein hydrolysates: characterisation and emulsifying properties

The evaluation of functional properties of different chia protein hydrolysates (CPH) and their application in O/W emulsions were studied. Enzymatic treatments with pepsin, pancreatin or the sequential action of pepsin–pancreatin were applied to hydrolyse a chia protein concentrate (CPC). Oil-in-water emulsions stabilised with CPC or these CPHs, with or without chia mucilage, were prepared at pH 7 or 10. Particle size, global stability, ζ-potential and rheological measurement of emulsions were determined. CPH presented higher (P ≤ 0.05) solubility and surface hydrophobicity levels, exhibiting better emulsifying properties than CPC. Emulsions with CPH presented smaller (P ≤ 0.05) droplet sizes than those with CPC. Regarding to physicochemical stability, emulsions at pH 7 were less stable than those at pH 10, showing destabilisation by creaming and coalescence. The addition of chia mucilage increased the apparent viscosity of emulsions and led to modifications in their fluid behaviour, exhibiting an interesting role as a thickening agent.     

Influence of tragacanth gum exudates from specie of Astragalus gossypinus on rheological and physical properties of whey protein isolate stabilised emulsions

The aim of this work was to investigate the effects of Iranian tragacanth gum (Astragalus gossypinus) (0.5, 1 wt.%), Whey protein isolate (WPI) (2, 4 wt.%) and acid oleic‐phase volume fraction (5, 10% v/v) on droplet size distribution, creaming index and rheological properties of emulsions with various compositions. Rheological investigations showed that both loss and storage modules increased with gum and oil contents. However, the viscoelastic behaviour was mainly governed by the gum concentration. Delta degree (storage and loss modules ratio) increased with frequency indicated that liquid like viscose behaviour dominates over solid like elastic behaviour. The shear‐thinning behaviour of all dispersions was successfully modelled with power law and Ellis models and Ellis model was founded as the better model to describe the flow behaviour of dispersions. Droplet size distribution was measured by light scattering; microscopic observations revealed a flocculated system. Increase in gum, WPI and oil contents resulted in decrease in creaming index of emulsions with dominant effect of gum concentration.     

热处理对大豆分离蛋白稳定乳液包埋特性的影响

本实验通过喷雾干燥前对SPI溶液95℃1 5 min热处理及形成乳液后加入乳糖溶液制备粉末样品,并将部分干粉储存于RH 75%环境中记录其7 d内等温吸湿线,待吸湿稳定后得到湿粉样品,测定原始乳液及干、湿粉末复溶乳液的粒径大小分布,干、湿粉末的水分含量、包埋效率(ME)、溶解速率并用扫描电镜(SEM)观察其微观结构。结果表明热处理和加糖处理能显著提高喷雾干燥SPI稳定乳液的包埋效率,高达98.68%,相对于未经处理的SPI乳液包埋效率高出1倍以上,此外含糖粉末表现出良好的溶解性,但潮湿环境对其溶解性、包埋效率及微观结构有较大影响。     

Emulsifying properties of sweet potato protein: Effect of protein concentration and oil volume fraction

The effect of protein concentrations (0.1, 0.25, 0.5, 1.0, 1.5 and 2.0% w/v) and oil volume fractions (5, 15, 25, 35 and 45% v/v) on properties of stabilized emulsions of sweet potato proteins (SPPs) were investigated by use of the emulsifying activity index (EAI), emulsifying stability index (ESI), droplet size, rheological properties, interfacial properties and optical microscopy measurements at neutral pH. The protein concentration or oil volume fraction significantly affected droplet size, interfacial protein concentration, emulsion apparent viscosity, EAI and ESI. Increasing of protein concentration greatly decreased droplet size, EAI and apparent viscosity of SPP emulsions; however, there was a pronounced increase in ESI and interfacial protein concentration (P < 0.05). In contrast, increasing of oil volume fraction greatly increased droplet size, EAI and emulsion apparent viscosity of SPP emulsions, but decreased ESI and interfacial protein concentration significantly (P < 0.05). The rheological curve suggested that SPP emulsions were shear-thinning non-Newtonian fluids. Optical microscopy clearly demonstrated that droplet aggregates were formed at a lower protein concentration of <0.5% (w/v) due to low interfacial protein concentration, while at higher oil volume fractions of >25% (v/v) there was obvious coalescence. In addition, the main components of adsorbed SPP at the oil–water interface were Sporamin A, Sporamin B and some high-molecular-weight aggregates formed by disulfide linkage.     

Heat Gelation of Oil-in-Water Emulsions Stabilized by Whey Protein

The conditions under which a high volume fraction of oil can be trapped in whey protein gels were studied. Oil-in-water emulsions of whey protein and vegetable oil were subjected to heat treatment. Such emulsions, depending on their protein and oil content, on their pH and on the emulsification technique used, gelled or remained liquid. Homogenization was the major factor to achieve gelation and the firmness of heat-induced gels increased with increasing emulsion fineness and homogeneity. Emulsions with a high gelation capacity were characterized by a single droplet family of relatively narrow size distribution and a mean droplet diameter ranging from roughly 300–700 nanometers. The pH range suitable for gelation extended from 3.5–8.0.     

The rheological behaviour of low fat soy‐based salad dressing

Low fat soy‐based salad dressings were formulated with different oil levels (3%, 13% and 23%) and emulsifiers (whey protein concentrate, soy‐lecithin and sodium caseinate) using either blender or ultra‐turrax (UT) homogeniser. Results showed that the rheological behaviour of these samples were highly dependent on the oil content, emulsifiers and blending methods. The UT method produced samples with better viscosity and have droplet size of 2–100 μm. Samples containing higher oil level have higher viscosity, smaller droplet size, larger G′ and G″ values. All samples show a shear‐thinning effect and larger G′ than G″, indicating the elastic nature of the samples. A quantity Q(t)% was applied to estimate the elasticity and the values were found to be in the range 22.8–85.2%. G′ and G″ were found to decrease with increased temperature. However, tan δ increased slightly with temperature; the values ranged from 0.2 to 0.4 at 5 °C to 0.3–0.5 at 25 °C. Current results demonstrated that the formulated samples have good stability compared with commercial products.     

Physical properties of emulsion gels formulated with sonicated soy protein isolate

This study aimed to determine the effect of high-intensity ultrasound (HIU) on physical properties of soy protein isolate dispersions (SPI) and their addition to emulsion gels (EG) containing soybean oil (SBO), inulin (IN) and carrageenan (CAR). Sonicated and non-sonicated SPI dispersions were mixed with CAR, IN and SBO and heated at 90 °C for 30 min to gel the emulsion. An increase in solubility and oil binding capacity was observed in sonicated SPI dispersions (S-SPI) compared to the non-sonicated ones. HIU changed the molecular weight of SPI and decreased apparent viscosity in the dispersions. The use of S-SPI in the EG reduced the droplet size and increased the hardness and G′ values. The use of S-SPI allowed a reduction of 75% of carrageenan in the EG without affecting the hardness of the gel. The results suggest that HIU can be used to improve rheological properties of functional EG.     

Interactions between Whey Protein Isolate and Soy Protein Fractions at Oil–Water Interfaces: Effects of Heat and Concentration of Protein in the Aqueous Phase

ABSTRACT:  The 2 main storage proteins of soy—glycinin (11S) and β-conglycinin (7S)—exhibit unique behaviors during processing, such as gelling, emulsifying, or foaming. The objective of this work was to observe the interactions between soy protein isolates enriched in 7S or 11S and whey protein isolate (WPI) in oil–water emulsion systems. Soy oil emulsion droplets were stabilized by either soy proteins (7S or 11S rich fractions) or whey proteins, and then whey proteins or soy proteins were added to the aqueous phase. Although the emulsifying behavior of these proteins has been studied separately, the effect of the presence of mixed protein systems at interfaces on the bulk properties of the emulsions has yet to be characterized. The particle size distribution and viscosity of the emulsions were measured before and after heating at 80 and 90 °C for 10 min. In addition, SDS-PAGE electrophoresis was carried out to determine if protein adsorption or exchanges at the interface occurred after heating. When WPI was added to soy protein emulsions, gelling occurred with heat treatment at WPI concentrations >2.5%. In addition, whey proteins were found adsorbed at the oil–water interface together with 7S or 11S proteins. When 7S or 11S fractions were added to WPI-stabilized emulsions, no gelation occurred at concentrations up to 2.5% soy protein. In this case also, 7S or 11S formed complexes at the interface with whey proteins during heating.     

Cold,gel-like soy protein emulsions by microfluidization: Emulsion characteristics,rheological and microstructural properties,and gelling mechanism

In this paper we reported the rheological and microstructural properties of a kind of novel cold, gel-like soy protein isolate (SPI) emulsions obtained by means of microfluidization. These gel-like emulsions were formed from untreated and preheated (95 °C, 15 min) SPI at a protein concentration of 6% (w/v), and various oil volume fractions (Φ; 0.2–0.6) and NaCl concentrations (0–500 mM). The rheological properties and microstructure were characterized using steady viscosity and dynamic oscillatory measurements, as well as confocal laser scanning microscopy (CLSM). The characteristics (e.g. droplet size distribution and creaming stability) of the emulsions, formed at lower protein concentrations (e.g. 0.5–4.0%), were also characterized, aiming to reveal the mechanism of the gel-like network formation. The dynamic oscillatory data indicated that both untreated and preheated SPI emulsions exhibited gel-like rheological properties, but the specific apparent viscosity (η) and storage modulus (G′) of the latter ones were much higher at a comparable Φ. Both η and G′ progressively increased upon Φ increasing, indicating enhanced inter-droplet interactions. At a given Φ value (0.3), increasing NaCl concentration progressively increased η and G′ of the preheated SPI emulsions, indicating the importance of electrostatic screening for the gel-like network formation. The CLSM analyses confirmed formation of the gel-like network, mainly composed of aggregated oil droplets, which was closely dependent on the Φ and NaCl concentration. The gel-like network was formed by bridging flocculation of oil droplets, mainly through inter-droplet hydrophobic interactions between the proteins adsorbed at the interface. These results suggested that soy proteins exhibit excellent potential to produce cold, gel-like emulsions, especially through a heat pretreatment followed by microfluidization, which might be of vital importance for the development of soy protein-based formulations, especially as carriers for heat-labile ingredients with health effects.     

Catastrophic inversion and rheological behavior in soy lecithin and Tween 80 based food emulsions

Emulsions inversion occurs in many industrial processes and may be influenced by the formulation conditions, composition and emulsification protocols. In this work, the influence of emulsifiers and stirring on catastrophic inversion (O/W to W/O) was evaluated. Emulsions were prepared with different stirring rates, using soy lecithin and Tween 80, at 2 and 5 wt%. The aqueous phase was distilled water with 1 wt% NaCl and the oil phase was soy oil. These emulsions were analyzed by conductivity, stability, microscopy and rheology assays. The most stable emulsions presented inversion with a smaller amount of the external phase. Rheological analysis showed that, with a higher concentration of emulsifier, it is better to use Tween 80 when lower viscosity is desired, while soy lecithin is more appropriate for higher viscosity products. The oscillatory tests showed that while the emulsions prepared using Tween 80 exhibited concentrated solution behavior, those prepared with soy lecithin exhibited strong gel behavior.     

STABILITY OF OIL-IN-WATER EMULSIONS. 2. Effects of Oil Phase Volume, Stability Test, Viscosity, Type of Oil and Protein Additive

SUMMARY –Stability of oil-in-water emulsions stabilized in sodium caseinate, gelatin and soy sodium proteinate was found to be increased by either an increase in the aqueous phase protein concentration (0.5–2.5%) or oil phase volume (20–50%). Both factors were significantly interrelated. Emulsions stabilized by soy sodium proteinate were generally higher in stability as compared to those stabilized by gelatin or sodium caseinate. With emulsions containing gelatin, greater stability occurred when the stability testing temperature was increased from 37–70°C and when the time interval was decreased from 24 hr to 90 min. Maximum relative viscosities of emulsions stabilized by gelatin and sodium caseinate were 2.0 and 2.5, respectively. Emulsions stabilized by soy sodium proteinate were quite viscous, with relative viscosity from 1.5–30 depending on both protein concentration and oil phase volume. Interchanging the emulsified oil among corn, soybean, safflower and peanut oils did not alter emulsion stability when examined at three concentrations of soy sodium proteinate. Changing the oil to olive oil significantly increased emulsion stability at each soy sodium proteinate level with oil phase volumes of 30, 40 and 50%.