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1.
《Food research international (Ottawa, Ont.)》2000,33(1):21-25
The influence of pH and CaC12 on the rheology and physical stability of emulsions stabilized by whey protein isolate (WPI) has been studied. The particle size, creaming index and shear viscosity of 10 wt% soy bean oil-in-water emulsions (d=0.55 μm) were measured with varying pH (3, 5 and 7) and CaC12 concentration (0–150 mM). In the absence of CaCl2 extensive droplet aggregation occurred around the isoelectic point of the whey proteins (4<pH<6) because of their low electrical charge. In the presence of CaC12, extensive droplet aggregation, viscosity enhancement and creaming instability occurred at pH 7 for CaC12>3 mM. These effects were much less pronounced in emulsions at pH 3 even at 150 mM CaC12. Droplet aggregation, creaming and viscosity of emulsions at pH 5 were fairly independent of CaC12 concentration. Droplet aggregation was induced by CaC12 probably because of the reduction in electrostatic repulsion between droplets. Re-stabilization of oil-in-water emulsions at high CaC12 concentrations was not observed in this study. 相似文献
2.
Corn oil-in-water emulsions (20 wt%, d32~ 0.6 μm) stabilized by 2 wt% whey protein isolate were prepared with a range of pH (3–7) and salt concentrations (0–100 mM NaCl), and particle size, rheology and creaming were measured at 30°C. Appreciable droplet flocculation occurred near the isoelectric point of whey protein (pH 4–6), especially at higher NaCl concentrations. Droplet flocculation increased emulsion viscosity and decreased stability to creaming. Results are related to the influence of environmental conditions on electrostatic and other interactions between droplets. 相似文献
3.
Electrostatic interactions between polysaccharides and proteins at oil–water interfaces alter the physicochemical properties and stability of emulsions. In this research, we studied the influence of chitosan addition on the properties of oil-in-water emulsions containing whey protein-coated lipid droplets. Experiments were carried out under conditions where the protein and polysaccharide had similar charges (pH 3.0) or opposite charges (pH 6.5). At pH 3.0, chitosan addition (0–0.025%) had little influence on droplet charge, aggregation, creaming stability or shear viscosity of whey protein emulsions, which was attributed to the fact that the cationic chitosan molecules did not adsorb to the cationic droplet surfaces due to electrostatic repulsion. At pH 6.5, chitosan addition caused a decrease in particle negative charge, an increase in particle size, a decrease in creaming stability, and an increase in viscosity. These effects were attributed to droplet aggregation caused by charge neutralization and bridging resulting from attraction of cationic chitosan molecules to anionic patches on the protein-coated droplet surfaces. Addition of cationic polyelectrolytes to protein-stabilized emulsions may be utilized to control their physicochemical properties, stability and biological fate, which may be useful for developing commercial products with novel or improved functional properties. 相似文献
4.
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. 相似文献
5.
《Food research international (Ottawa, Ont.)》2006,39(2):230-239
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. 相似文献
6.
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. 相似文献
7.
Vilma Speiciene Fabien Guilmineau Ulrich Kulozik Daiva Leskauskaite 《Food chemistry》2007,102(4):1048-1054
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. 相似文献
8.
Formulation and properties of model beverage emulsions stabilized by sucrose monopalmitate: Influence of pH and lyso-lecithin addition 总被引:1,自引:0,他引:1
Seung Jun Choi Eric Andrew Decker Lulu Henson L. Michael Popplewell Hang Xiao David Julian McClements 《Food research international (Ottawa, Ont.)》2011,44(9):3006-3012
There is a growing trend toward utilizing more label friendly ingredients in foods and beverages. In this study, we focused on the utilization of sucrose monopalmitate (SMP) as a non-ionic surfactant for stabilizing acidic beverages. Orange oil-in-water emulsions (5% (w/w) oil) stabilized by SMP were prepared using high pressure homogenization (pH 7). The minimum droplet diameter was around 130 nm, while the minimum mass ratio of SMP-to-oil required to produce small droplets was 0.1-to-1. Extensive droplet aggregation occurred when the pH of the emulsions was reduced from pH 7 to 3, with the mean particle diameter increasing from around 0.13 to 7.25 μm. This effect was attributed to an appreciable reduction in droplet charge when the pH was reduced (ζ ≈− 35 mV at pH 3 and − 2 mV at pH 3) thereby decreasing the electrostatic repulsion between droplets. It was proposed that the negative charge on the SMP-coated droplets was due to the presence of anionic substances within the droplets, such as palmitic acid (pKa ≈ 4.9). Palmitic acid may have been an impurity in the original ingredient or it may have been generated due to degradation of SMP during storage. The addition of anionic lyso-lecithin markedly improved the stability of the emulsions to droplet aggregation and phase separation at low pH, which was attributed to an increased electrostatic repulsion between the droplets. This study has important consequences for the formulation of acidic beverage emulsions with improved stability and physicochemical performance. 相似文献
9.
《Food research international (Ottawa, Ont.)》2006,39(1):78-86
Coconut cream protein (CCP) fractions were isolated from coconuts using two different isolation procedures: isoelectric precipitation (CCP1-fraction) and freeze–thaw treatment (CCP2-fraction). The ability of these protein fractions to form and stabilize oil-in-water emulsions was compared with that of whey protein isolate (WPI). Protein solubility was a minimum at ∼pH 4, 4.5 and 5 for CCP1, CCP2, and WPI, respectively, and decreased with increasing salt concentration (0–200 mM NaCl) for the coconut proteins. All of the proteins studied were surface active, but WPI was more surface active than the two coconut cream proteins. The two coconut cream proteins were used to prepare 10 wt% corn oil-in-water emulsions (pH 6.2, 5 mM phosphate buffer). CCP2 emulsions had smaller mean droplet diameters (d32 ≈ 2 μm) than CCP1 emulsions (d32 ≈ 5 μm). Corn oil-in-water emulsions (10 wt%) stabilized by 0.2 wt% CCP2 and WPI were prepared with different pH values (3–8), salt concentrations (0–500 mM NaCl) and thermal treatments (50–90 °C for 30 min). Considerable droplet flocculation occurred in the emulsions near the isoelectric point of the proteins: CCP2 (pH ∼ 4.3); WPI (pH ∼ 4.8). Emulsions with monomodal particle size distributions, small mean droplet diameters, and good creaming stability could be produced at pH 7 for WPI, but CCP2 produced bimodal distributions at this pH. The CCP2 and WPI emulsions remained relatively stable to droplet aggregation and creaming at NaCl concentrations ⩽50 and ⩽100 mM, respectively. In the absence of salt, both CCP2 and WPI emulsions were quite stable to thermal treatments (50–90 °C for 30 min). 相似文献
10.
Physicochemical Properties of Whey Protein-Stabilized Emulsions as affected by Heating and Ionic Strength 总被引:4,自引:0,他引:4
Corn oil-in-water emulsions (19.6 wt%; d32~ 0.6 μm) stabilized by 2 wt% whey protein isolate (WPI) were prepared with a range of pH (3–7) and salt concentrations (0–100 mM NaCl). These emulsions were heated between 30 and 90°C and their particle size distribution, rheological properties and susceptibility to creaming measured. Emulsions had a paste-like texture around the isoelectric point of WPI (~φ 5) at all temperatures, but tended to remain fluid-like at pH >6 or <4. Heating caused flocculation in pH 7 emulsions between 70 and 80°C (especially at high salt concentrations), but had little effect on pH 3 emulsions. Flocculation increased emulsion viscosity and creaming. Results were interpreted in terms of colloidal interactions between droplets. 相似文献
11.
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. 相似文献
12.
The ability of flaxseed protein concentrate (FPC) to stabilize soybean oil-in-water emulsion was compared with that of soybean protein concentrate (SPC). The stability of emulsions increased with increase in protein concentration. The FPC-stabilized emulsions had smaller droplet size and higher surface charge, but worse stability at the same protein concentration compared to SPC-stabilized emulsions. Oil-in-water emulsions stabilized by both proteins were diluted and compared at different pH values (3–7), ionic strength (0–200 mM NaCl) and thermal treatment regimes (25–95 °C for 20 min). Considerable emulsion droplet flocculation occurred around iso-electric point of both proteins: FPC (pH 4.2) and SPC (pH 4.5). FPC and SPC-stabilized emulsions remained relatively stable against droplet aggregation and creaming at NaCl concentration below 100 and 50 mM, respectively. The emulsions stabilized by both proteins were fairly stable within these thermal processing regimes. FPC appears to be less effective as an emulsifier compared to SPC due to its lower emulsion viscosity. Hence, FPC could be more effective in emulsions that are fairly viscous. 相似文献
13.
Characterisation of emulsion properties and of interface composition in O/W emulsions prepared with hen egg yolk, plasma and granules 总被引:1,自引:0,他引:1
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. 相似文献
14.
ABSTRACT: Calcium chloride (0 to 10 mM) and potassium chloride (0 to 600 mM) were added into model nutritional beverage emulsions containing 7% (w/w) soybean oil droplets and 0.35% (w/w) whey protein isolate (pH 6.7). The particle size, surface charge, viscosity, and creaming stability of the emulsions then were measured. The surface charge decreased with increasing mineral ion concentration. The particle size, viscosity, and creaming instability of the emulsions increased appreciably above critical CaCl2 (3 mM) and KCl (200 mM) concentrations because of droplet flocculation. The origin of this effect was attributed to reduction of the electrostatic repulsion between droplets due to electrostatic screening and ion binding. CaCl2 promoted emulsion instability more efficiently than KCl because Ca2+ ions are more effective at reducing electrostatic repulsion than K+ ions. 相似文献
15.
Lactoferrin is a globular protein from bovine milk with an unusually high isoelectric point (pI > 8), which may lead to novel functional properties in foods and other products because it is cationic across a wide pH range. In this study, we investigated the influence of pH (2–9), NaCl addition (0–200 mM), CaCl2 addition (0–200 mM), and thermal processing (30–90 °C, 20 min) on the stability of lactoferrin (LF) stabilized oil-in-water emulsions. At ambient temperature, the emulsions were stable to droplet aggregation at low pH (pH ≤ 6), but exhibited some aggregation at pH ≈ pI (pH 7–9). The thermal stability of the emulsions depended on pH, holding temperature, and thermal history. When LF-coated droplets were heated in distilled water, and then their pH was adjusted in the range 2–9, they were highly unstable to aggregation at pH 7 and 8. On the other hand, when the pH was altered in the range 2–9 first, and then they were heated, the LF-coated droplets were highly unstable to aggregation at pH ≥ 5 when heated above 50 °C. The stability of the emulsions to salt addition depended on pH and salt type, which was attributed to counter-ion binding and electrostatic screening effects. For NaCl, emulsions were stable from 0 to 200 mM at pH 3 and 9, but aggregated at ≥100 mM at pH 6. For CaCl2, emulsions were stable from 0 to 200 mM at pH 3, but aggregated with ≥150 mM CaCl2 at pH 6 and 9. These results have important implications for the formulation and production of emulsion-based products using lactoferrin as an emulsifier. 相似文献
16.
To study possible applications of microalgae proteins in foods, a colourless, protein-rich fraction was isolated from Tetraselmis sp. In the present study the emulsion properties of this algae soluble protein isolate (ASPI) were investigated. Droplet size and droplet aggregation of ASPI stabilized oil-in-water emulsions were studied as function of isolate concentration (1.25–10.00 mg/mL), pH (3–7), and ionic strength (NaCl 10–500 mM; CaCl2 0–50 mM). Whey protein isolate (WPI) and gum arabic (GA) were used as reference emulsifiers. The lowest isolate concentrations needed to reach d32 ≤ 1 μm in 30% oil-in-water emulsions were comparable for ASPI (6 mg/mL) and WPI (4 mg/mL). In contrast to WPI stabilized emulsions ASPI stabilized emulsions were stable around pH 5 at low ionic strength (I = 10 mM). Flocculation only occurred around pH 3, the pH with the smallest net droplet ζ-potential. Due to the charge contribution of the anionic polysaccharide fraction present in ASPI its droplet ζ-potential remained negative over the whole pH range investigated. An increase in ionic strength (≥100 mM) led to a broadening of the pH range over which the ASPI stabilized emulsions were unstable. GA emulsions are not prone to droplet aggregation upon changes in pH or ionic strength, but much higher concentrations are needed to produce stable emulsions. Since ASPI allows the formation of stable emulsions in the pH range 5–7 at low protein concentrations, it can offer an efficient natural alternative to existing protein–polysaccharide complexes. 相似文献
17.
Pea protein exhibits a novel Pickering stabilization for oil-in-water emulsions at pH 3.0 总被引:1,自引:0,他引:1
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. 相似文献
18.
《Food Hydrocolloids》2003,17(1):87-93
The influence of an anionic surfactant (sodium dodecyl sulfate, SDS) on the thermal stability of emulsions stabilized by a globular protein (bovine serum albumin, BSA) was examined. 1 wt% n-hexadecane oil-in-water emulsions (0.5 wt% BSA, 100 mM NaCl, 20 mM imidizole, pH 7.0) were held isothermally at temperatures from 30 to 90 °C for 30 min. Extensive droplet flocculation was only observed in emulsions held at 90 °C, which lead to rapid creaming instability. The thermal stability of emulsions heated at 90 °C could be greatly improved by adding SDS at surfactant-to-protein molar ratios (R) greater than 5 (∼0.01 wt% SDS). On the other hand, adding surfactant (0<R<600) to the emulsions after heating could not prevent extensive droplet aggregation. Adding SDS to emulsions prior to heating may have improved their thermal stability by increasing the electrostatic repulsion between the lipid droplets or by increasing the denaturation temperature of the adsorbed proteins. These results may have important applications in the development of heat-stable emulsions. 相似文献
19.
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. 相似文献
20.
This study examines the influence of interfacial composition on the freeze–thaw stability of oil-in-water emulsions. Three 5% w/w oil-in-water emulsions (5 mM phosphate buffer, pH 6.0) were prepared using the layer-by-layer electrostatic deposition method that had different interfacial compositions: (i) primary emulsion (β-Lg); secondary emulsion (β-Lg–ι-carrageenan); (iii) tertiary emulsion (β-Lg–ι-carrageenan–gelatin). The primary, secondary and tertiary emulsions were subjected to from one to three freeze–thaw cycles (−20 °C for 22 h, +40 °C for 2 h) in the absence or presence of sucrose (10% w/w), and then their stability was assessed by ζ-potential, particle size, microstructure and creaming stability measurements. In the absence of sucrose, the primary and secondary emulsions were highly unstable to droplet aggregation and creaming after three freeze–thaw cycles, whereas the tertiary emulsion was stable, which was attributed to the relatively thick biopolymer layer surrounding the oil droplets. In the presence of 10% w/w sucrose, all of the emulsions were much more stable, which can be attributed to the ability of sucrose to increase the amount of non-frozen aqueous phase in the emulsions. The interfacial engineering technology used in the study could therefore lead to the creation of food emulsions with improved stability to freezing and thawing. 相似文献