Phytosterol oxidation in oil-in-water emulsions and bulk oil

Dietary plants sterols (phytosterols) have been shown to lower plasma cholesterol level in humans. Since phytosterols may protect against coronary heart diseases, they are being incorporated into functional foods. However, phytosterols are susceptible to oxidative degradation. The purpose of this study was to evaluate the formation of phytosterols oxidation products (POPs) in oil-in-water emulsions and bulk corn oil. The extent of lipid oxidation was monitored by measuring the lipid hydroperoxides and hexanal, whereas 7-keto derivatives of phytosterols were determined by gas chromatography to follow sterol oxidation. A higher POPs level and formation rate was found in the oil-in-water (o/w) emulsion than in the bulk oil. Interfacial tension measurements showed that phytosterols had a high degree of surface activity, which would allow them to migrate to the oil–water interface of the emulsion droplets where oxidative stress is high.     

Physicochemical properties of whey protein isolate stabilized oil-in-water emulsions when mixed with flaxseed gum at neutral pH

Concentrations ranging from 0% to 0.33% (w/v) of gum (Emerson and McDuff) were added to the emulsions at pH 7. Particle size distribution, viscosity, ζ-potential, microstructure, and phase separation kinetics of the emulsions were observed. Both polysaccharides and protein coated droplets are negatively charged at this pH, as shown by ζ-potential measurements. At all the concentrations tested, the addition of gum did not affect significantly (p < 0.05) the apparent diameter of the emulsion droplets. At low concentrations (gum  0.075% (w/v)), no visual phase separation was observed and the emulsion showed a Newtonian behaviour. However, at concentrations above the critical concentration of gum, depletion flocculation occurred: when 0.1 flaxseed gum was present, there was visual phase separation over time and the emulsion exhibited shear-thinning behaviour. These results demonstrate that flaxseed gum is a non-interacting polysaccharide at neutral pH; it could then be employed to strengthen the nutritional value of some milk-based drinks, but at limited concentrations.     

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.     

Heat-induced changes in oil-in-water emulsions stabilized with soy protein isolate

The physicochemical properties of soy proteins stabilized oil-in-water emulsions were studied after heating at two different temperatures, 75 and 95 °C. The effect of changing the order of the process (heating the solution before emulsification, or heating the emulsion) was also studied. The heating temperatures were chosen as they are known to selectively cause denaturation of the two major proteins present in the soy protein isolate: β-conglycinin and glycinin. The thermal transitions observed for soy proteins adsorbed at the interface were different from those measured in protein solutions, suggesting that some changes occur in the structure of the soy proteins upon adsorption on the oil droplet. Heating induces aggregation of the oil droplets, as shown by an increase of the particle size and the bulk viscosity of the emulsions, with a more prominent effect after heating at 95 °C. Transmission electron microscopy observations clearly demonstrate that heating induces the formation of large protein aggregates at the interface. In addition, the composition of the protein present at the interface changes depending on the order of heating and homogenization. While heating the solutions before emulsification results in all the protein subunits to be present at the interface in an aggregated form, when heating is applied after emulsification, a portion of the α and the α′ subunit of β-conglycinin as well as the acidic subunits of glycinin remain unadsorbed.     

Antioxidant and emulsifying properties of potato protein hydrolysate in soybean oil-in-water emulsions

The efficacy of a previously developed antioxidative potato protein hydrolysate (PPH) for the stabilisation of oil droplets and inhibition of lipid oxidation in soybean oil-in-water (O/W) emulsions was investigated. Emulsions (10% lipid, pH 7.0) with PPH-coated oil droplets were less stable than those produced with Tween 20 (P < 0.05). However, the presence of PPH, whether added before or after homogenisation with Tween 20, retarded emulsion oxidation, showing reduced formation of peroxides up to 53.4% and malonaldehyde-equivalent substances up to 70.8% after 7-d storage at 37 °C (P < 0.05), when compared with PPH-free emulsions. In the emulsions stabilised by PPH + Tween 20, 8–15% of PPH was distributed at the interface. Adjustment of the pH from 3 to 7 markedly increased ζ-potential of such emulsions (P < 0.05). Inhibition of lipid oxidation by PPH in soybean O/W emulsions can be attributed to both chemical and physical (shielding) actions.     

Ability of flaxseed and soybean protein concentrates to stabilize oil-in-water emulsions

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.     

Ability of conventional and nutritionally-modified whey protein concentrates to stabilize oil-in-water emulsions

The ability of a modified whey protein concentrate (MWPC), which contains relatively high proportions of phospholipid and high molecular weight protein fractions, to form and stabilize 10 wt% corn oil-in-water emulsions (pH 7.0, 5 mM phosphate buffer) was compared with that of a conventional whey protein concentrate (CWPC). The MWPC stabilized emulsions required less protein to prepare stable emulsions with monomodal particle size distributions and small mean droplet diameters (d₄₃ ≈ 0.3 μm at [WPC] ⩾ 0.5 wt%) than CWPC stabilized emulsions (d₄₃ ≈ 0.4 μm at [WPC] ⩾ 0.9 wt%) under similar homogenization conditions (5 passes at 5000 psi). In addition, the emulsions stabilized by 0.9 wt% MWPC were more stable to high salt concentration (NaCl ⩽ 200 mM), thermal processing (30–90 °C for 30 min) and pH (3, 6 and 7) than those stabilized by the same concentration of CWPC, which was attributed to polymeric steric repulsion rather than electrostatic repulsion. This study has important implications for the wide application of WPC as a natural emulsifier in food products.     

Chemical and physical stability of protein and gum arabic-stabilized oil-in-water emulsions containing limonene

ABSTRACT:  An important flavor component of citrus oils is limonene. Since limonene is lipid soluble, it is often added to foods as an oil-in-water emulsion. However, limonene-containing oil-in-water emulsions are susceptible to both physical instability and oxidative degradation, leading to loss of aroma and formation of off-flavors. Proteins have been found to produce both oxidatively and physically stable emulsions containing triacylglycerols. The objective of this research was to determine if whey protein isolate (WPI) could protect limonene in oil-in-water emulsion droplets more effectively than gum arabic (GA). Limonene degradation and formation of the limonene oxidation products, limonene oxide and carvone, were less in the WPI- than GA-stabilized emulsions at both pHs 3.0 and 7.0. These data suggest that WPI was able to inhibit the oxidative deterioration of limonene in oil-in-water emulsions. The ability of WPI to decrease oxidative reactions could be due to the formation of a cationic emulsion droplet interface at pH 3.0, which can repel prooxidative metals, and/or the ability of amino acids in WPI to scavenge free radical and chelate prooxidative metals.     

Emulsifying properties of lactose-amines in oil-in-water emulsions

Lactose-amines were synthesized with hexadecyl-amide and lactose via the Maillard reaction and their emulsion stabilization properties were investigated. Lactose-amines were synthesized using two different constant heating (4 and 8 h) and two different heating/cooling cycles (12 and 24 h). Each lactose-amine sample was used as an emulsifier in 20:80 ratio oil-in-water emulsions at four different concentrations (0.01%, 0.05%, 0.1%, and 1%). Emulsion stability was monitored by measuring the oil droplet sizes and the extent of destabilization via clarification over 5 days. At 1% concentrations, emulsions prepared with lactose-amines synthesized for 4, 12, and 24 h were as stable as the whey protein positive control emulsion. The 8 h lactose-amine sample resulted in a less stable emulsion. We assume the difference is related to the amount of heat this sample was exposed to during synthesis, with extensive heat leading to advanced Maillard products, which possessed reduced emulsification properties.     

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.     

猪血浆蛋白水解物对水包油型乳状液氧化稳定性的影响

本实验主要研究了猪血浆蛋白水解物（Porcine plasma protein hydrolysate,PPPH）对水包油型（O/W型）乳状液储藏过程氧化稳定性的影响。分别将PPPH以0、2.5、5、10和20 mg/m L的浓度添加到以Tween-20为乳化剂的菜籽油O/W型乳状液中,测定乳状液在37℃条件下储藏10 d时间内的荧光光谱分析、共轭二烯（Conjugated diene,CD）和硫代巴比妥酸值（Thiobarbituric acid reactive substances,TBARS）的变化趋势。研究结果表明,色氨酸的氧化降解发生在蛋白氧化的初级阶段,而荧光蛋白氧化产物（Fluorescent protein oxidation products,FP）的形成是蛋白氧化第二阶段的产物。另外,在乳化体系储藏期间,与对照组相比,添加2.5 mg/m L PPPH的处理组具有最高的色氨酸荧光强度和FP（p<0.05）,同时具有最低的CD和TBARS值（p<0.05）。与此同时,色氨酸荧光强度与CD含量和TBARS值之间呈现显著的负相关关系。总之,PPPH的添加能够显著提高O/W型乳状液的氧化稳定性,为其作为抗氧化剂在乳状液食品中的潜在应用奠定了理论基础。      

Retention of propanal in protein-stabilised tuna oil-in-water emulsions

Propanal concentrations in the static headspace (HS) above water, aqueous protein solutions and freshly made tuna oil-in-water emulsions spiked with propanal (an indicator of omega-3 fatty acid oxidation) were compared. In the presence of proteins, HS propanal concentration was reduced and its decrease above aqueous hydrolysed whey protein isolate (HWPI) solutions was significantly greater than that above whey protein isolate (WPI) solutions. Similar trends were found for emulsions stabilised by HWPI and WPI. The results suggested that there was stronger binding of propanal to HWPI compared to WPI. Emulsification decreased the HS propanal concentration even further for both the WPI and HWPI matrices, but its effect was less in comparison to the protein type. Phosphate buffer decreased the HS propanal concentration, but this effect was minor. The difference in the release of propanal from protein stabilised tuna oil-in-water emulsions was interpreted in terms of the chemical interaction between propanal and protein.     

Mannans as stabilizers of oil-in-water beverage emulsions

The stabilizing effect of spruce galactoglucomannan (GGM) on a model beverage emulsion system was studied and compared to that of guar gum and locust bean gum galactomannans, konjac glucomannan, and corn arabinoxylan. In addition, guar gum was enzymatically modified in order to examine the effect of the degree of polymerization and the degree of substitution of galactomannans on emulsion stability. Use of GGM increased the turbidity of emulsions both immediately after preparation and after storage of up to 14 days at room temperature. GGM emulsions had higher turbidity than the emulsions containing other mannans. The initial turbidity increased with increasing GGM content, but after 14 days storage at room temperature, the turbidity was the highest for GGM/oil ratio of 0.10:1 when ethanol-precipitated GGM was used. Increasing the storage temperature to +45 °C led to rapid emulsion breakdown, but a decrease in storage temperature increased emulsion stability after 14 days. Confocal microscopy showed that the average particle size in the bottom part of GGM emulsions stored for 14 days was smaller than 1 μm. A low degree of polymerization and a high degree of substitution of the modified galactomannans were associated with a decrease in emulsion turbidity.     

Infrared spectroscopic analysis of structural features and interactions in olive oil-in-water emulsions stabilized with soy protein

Lipid and protein structural characteristics of olive oil-in-water emulsions formulated with various stabilizer systems were investigated using Fourier transform infrared spectroscopy (FT-IR). Proximate composition, water binding and textural properties were also evaluated in these emulsions. Two different olive oil-in-water emulsions were studied: E/SPI prepared with soy protein isolate as a stabilizing system, and E/SPI + SC + MTG prepared with a combination of soy protein isolate, sodium caseinate and microbial transglutaminase as a stabilizing system. Results showed that textural properties (P < 0.05) were dependent on the stabilizing system. E/SPI + SC + MTG emulsion presented greater (P < 0.05) lipid chain disorder, more lipid-protein interactions, and more (P < 0.05) ??-helix and ??-sheet structures. A relationship between textural and structural properties was also observed as a function of the stabilizing system employed in the formulation of emulsions. A more thorough understanding of this connection could help improve the development of food products with appropriate physical properties.     

Oxidative stability of oil-in-water emulsions stabilised with protein or surfactant emulsifiers in various oxidation conditions

Many studies have investigated the effect of emulsifiers on the oxidative stability of oil-in-water (O/W) emulsions. A better oxidative stability of surfactant-stabilised O/W emulsions as compared to protein-stabilised emulsions has been recently shown in conditions when the major part of the emulsifier is adsorbed at the oil-water interface and oxidation is induced by iron−ethylenediaminetetraacetic acid (EDTA) complex. In this work, the contribution of the interfacial layer to the oxidation of emulsified lipids is investigated under various incubation conditions, involving different oxidation mechanisms. O/W emulsions were formulated at pH 6.7 with limited amounts of emulsifiers in the aqueous phase. Emulsions were incubated either at 33 °C without initiator at 25 °C in the presence of iron/ascorbate, metmyoglobin or 2,2′-azobis(2-amidinopropane)-dihydrochloride (AAPH). Oxygen uptake and volatile compound formation confirmed that protein-stabilised emulsions are less oxidatively stable than Tween 20-stabilised ones. This work also shows complex oxidative interrelationships between oxidation initiator and certain proteins, such as β-casein and bovine serum albumin.     

Stability of citral in protein- and gum arabic-stabilized oil-in-water emulsions

Citral is a major flavor component of citrus oils that can undergo chemical degradation leading to loss of aroma and formation of off-flavors. Engineering the interface of emulsion droplets with emulsifiers that inhibit chemical reactions could provide a novel technique to stabilize citral. The objective of this study was to determine if citral was more stable in emulsions stabilized with whey protein isolate (WPI) than gum arabic (GA). Degradation of citral was equal to or less in GA- than WPI-stabilized emulsion at pH 3.0 and 7.0. However, formation of the citral oxidation product, p-cymene was greater in the GA- than WPI-stabilized emulsion at pH 3.0 and 7.0. Emulsions stabilized by WPI had a better creaming stability than those stabilized by GA because the protein emulsifier was able to produce smaller lipid droplets during homogenization. These data suggest that WPI was able to inhibit the oxidative deterioration of citral in oil-in-water emulsions. The ability of WPI to decrease oxidative reactions could be due to the formation of a cationic emulsion droplet interface at pH 3.0 which can repel prooxidative metals and/or the ability of amino acids in WPI to scavenge free radical and chelate prooxidative metals.     

Effect of concentrated flaxseed protein on the stability and rheological properties of soybean oil-in-water emulsions

Flaxseed protein concentrate containing-mucilage (FPCCM) was used to stabilize soybean oil-in-water emulsions. The effects of FPCCM concentration (0.5, 1.0, 1.5% w/v) and oil-phase volume fraction (5, 10, 20% v/v) on emulsion stability and rheological properties of the soybean oil-in-water emulsions were investigated. Z-average diameter, zeta-potential, creaming index and rheological properties of emulsions were determined. The result showed that FPCCM concentration significantly affected zeta-potential, creaming rate and emulsion viscosity. The increasing of FPCCM concentration led to a more negative charged droplet and a lower creaming rate. Oil-phase volume fraction significantly affected Z-average diameter, rheological properties, creaming index and creaming rate. With the increase of oil-phase volume fraction, both Z-average diameter and emulsion viscosity increased, while creaming index and creaming rate decreased. The rheological curve suggested that the emulsions were shear-thinning non-Newtonian fluids.     

Characterization of hydrophobic flavor release profile in oil-in-water emulsions

ABSTRACT:  An instrumental approach to better understand the release and persistence of flavor in oil-in-water emulsions has been developed. Emulsions were prepared with various whey protein (0.1% to 3.16%), sunflower oil (1% to 8%), and ethyl hexanoate (0% to 0.04%) concentrations. Flavor release profile in real time was measured at 37 °C using a specially designed glass cell connected directly to a gas chromatograph equipped with a flame ionization detector. The intensity of flavor released from the emulsion stirred at a shear rate of 100  s⁻¹ was monitored as a function of time and data were fitted to a 1st-order kinetic equation. Maximum intensity and decay rate constant were both determined from the model and the persistence index (inversely associated to decay rate constant) was calculated. For constant aroma concentration in the emulsion, maximum intensity significantly decreased as whey protein and oil concentrations increased. For increasing aroma concentration, maximum intensity was directly proportional to the ethyl hexanoate concentration when the oil content was kept constant but leveled off when oil content was increased. Persistence of flavor significantly increased with increasing protein and oil concentrations while aroma concentrations had no effect when oil content was constant. The results showed that oil concentration had a greater influence on flavor release characteristics than protein concentration. Aroma concentration in the oil phase, rather than in the emulsion, determines the kinetics of hydrophobic flavor release. The method provides a useful tool for the rapid and reproducible measurement of flavor release profile.