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.     

Effect of iron chelates on oil–water interface,stabilized by milk proteins: The role of phosphate groups and pH. Prediction of iron transfer from aqueous phase toward fat globule surface by changes of interfacial properties

Iron incorporated into food systems induces oxidation and precipitation. The consequences are reduced bioavailability and a functional modification of other food components such as proteins. The iron-chelates such as ferrous bisglycinate represent a possibility to avoid side effects, since the iron is protected. The aim of this study is to investigate the effects of iron-chelates compounds on the properties of an oil/water interface stabilized by caseinate or β-lacotoglobulin, under environmental conditions at 20 °C. Analyses were performed using dynamic drop tensiometry during 5000 s. The aqueous bulk phase is an imidazole/acetate buffer (0.1 M), containing 0.4 × 10⁻⁶ M protein, and 0.2 × 10^-6 9 M iron-chelates compounds. The results indicate that, under neutral conditions, the addition of some irons salts (NaFe-EDTA or Fe-bisglycinate) do not change the structure of the interface stabilized by a protein containing no phosphate groups (β-lactoglobulin). In the case of caseinate, NaFe-EDTA addition increases the lowering rate of surface tension at pH 6.5. On the contrary, the lowering rate of surface tension with caseinate is inhibited by Fe-bisglycinate at pH 6.5. Such an effect is not observed with β-lactoglobulin. The low transfer of irons ions from the bulk to the interface stabilized by β-lactoglobulin is confirmed by zetameter and FTIR measurements. These results indicate an effective strategy to follow for controlling the physical and chemical stability of an emulsion stabilized with proteins.     

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.     

Design of interfacial films to control lipid oxidation in oil-in-water emulsions

In oil-in-water (O/W) emulsions, the droplets covered by native proteins are more prone to oxidation than droplets covered by surfactants. We attempted in this work to improve the barrier properties of protein-stabilized interfacial layers by controlled modifications of their composition and structure. Native bovine β-lactoglobulin (BLG) or β-casein (BCN), partially aggregated BLG and mixtures of the proteins with dilauroyl phosphatidylcholine (DLPC) were used to prepare emulsions and reconstituted Langmuir–Blodgett films. Lipid oxidation in the emulsions, as evaluated from oxygen uptake and formation of conjugated dienes, propanal and hexanal was roughly unmodified with aggregated BLG and DLPC–BLG mixtures and even favored with DLPC–BCN mixtures. The reconstituted phospholipid/protein interfacial layers presented interfacial heterogeneity evidenced by atomic force microscopy (AFM). This indicates that the structural homogeneity of the interface could be a key factor in controlling lipid oxidation.     

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.     

Time-dependent competitive adsorption of milk proteins and surfactants in oil-in-water emulsions

Competitive adsorption of pure milk proteins and non-ionic surfactants has been studied in model oil-in-water emulsions (4 g kg^?1 β-lactoglobulin or β-casein, 200 g kg^?1 n-hexadecane) as a function of the age of the adsorbed protein layer at the oil-water interface. With β-lactoglobulin-stabilised emulsions containing oil-soluble surfactant C₁₂ E₂ (diethylene glycol n-dodecyl ether), there is found to be a steadily increasing amount of protein associated with the emulsion droplets over a few hours following emulsification. Addition of water-soluble surfactant Tween 20 (polyoxyethylene (20) sorbitan monolaurate) to a β-lactoglobulin-stabilised emulsion (with or without C₁₂E₂) leads to less protein displacement if the emulsion is aged prior to addition of Tween 20. Moderate additions of C₁₂E₂ or Tween 20 produce no time dependence in the competitive adsorption in β-casein-stabilised emulsions, although some time dependence is observed when C₁₂E₂ and a high concentration of Tween 20 are present together. Crystallisation of the oil phase in β-casein-stabilised emulsions at pH 7 leads to a lowering of the measured protein surface concentration, especially in the presence of C₁₂E₂ and a reduction in the surfactant to protein molar ratio required for complete protein displacement by water-soluble surfactant (Tween 20 or octaethylene glycol n-dodecyl ether). Under more acidic conditions of pH 5 or pH 3, the surface coverage and ease of displacement of β-lactoglobulin at the surface of liquid emulsion droplets is substantially different from that under neutral pH conditions.     

On the stability of oil-in-water emulsions to freezing

Oil in water emulsions (40 wt%) were prepared from a homologous series of n-alkanes (C10–C18). The samples were temperature cycled in a differential scanning calorimeter (two cycles of 40 °C to −50 °C to 40 °C at 5 °C min⁻¹) and in bulk (to −20 °C). The emulsions destabilized and phase-separated after freeze–thaw if the droplets were solid at the same time as the continuous phase and were more unstable if a small molecule (SDS or polyoxyethylene sorbitan monolaurate) rather than a protein (whey protein isolate or sodium caseinate) emulsifier was used. The unstable emulsions formed a self-supporting cryo-gel that persisted between the melting of the water and the melting of the hydrocarbon phase. Microscopy provides further evidence of a hydrocarbon continuous network formed during freezing by a mechanism related to partial coalescence which collapses during lipid melting to allow phase separation.     

Impact of iron encapsulation within the interior aqueous phase of water-in-oil-in-water emulsions on lipid oxidation

Iron (Fe³⁺) was encapsulated within the internal aqueous phase of water-in-oil-in-water (W/O/W) emulsions, and then the impact of this iron on the oxidative stability of fish oil droplets was examined. There was no significant change in lipid droplet diameter in the W/O/W emulsions during 7 days storage, suggesting that the emulsions were stable to lipid droplet flocculation and coalescence, and internal water diffusion/expulsion. The initial iron encapsulation (4 mg/100 g emulsion) within the internal aqueous phase of the water-in-oil (W/O) emulsions was high (>99.75%), although, a small amount leaked out over 7 days storage (≈10 μg/100 g emulsion). When W/O/W emulsions were mixed with fish oil droplets the thiobarbituric acid-reactive substances (TBARS) formed decreased (compared to fish oil droplets alone) by an amount that depended on iron concentration and location, i.e., no added iron < iron in external aqueous phase < iron in internal aqueous phase. These differences were attributed to the impact of W/O droplets on the concentration and location of iron and lipid oxidation reaction products within the system.     

国内外铁强化管理比较研究

铁缺乏是全球最为常见的营养缺乏病之一,也是各国的重要公共卫生问题。针对铁缺乏现状,各国制定了一系列铁强化的政策和法规,以改善缺铁性贫血以及铁缺乏相关疾病。本文就目前国内和部分国家食品铁强化法律法规体系、铁强化剂、铁强化食物载体等方面进行论述,为今后我国铁强化政策的修订提供参考。     

乳化体系中花生油氧化稳定性的研究

主要探讨花生油乳化体系中乳化剂类型、用量、pH值、EDTA、温度等对花生油氧化稳定性的影响,结果显示:乳化剂种类和pH对于乳状液体系的氧化稳定性有显著影响,阴离子乳化剂SDS稳定的乳化液,pH4.0的氧化速率最快;非离子乳化剂Tween20稳定的乳化液,pH的影响不是很显著;阳离子乳化剂CTAB稳定的乳化液,随着pH的升高,氧化速率变快。乳化液体系中微量金属离子对于体系也有相当大的影响,随着金属离子螯合剂EDTA浓度的增加,其乳化体系中花生油的氧化速率显著降低。乳化剂用量也会影响体系的氧化稳定性,随着乳化剂用量的增加,乳化乳化体系中花生油的氧化稳定性降低。     

Influence of heat processing and calcium ions on the ability of EDTA to inhibit lipid oxidation in oil-in-water emulsions containing omega-3 fatty acids

The nutritional benefits of ω-3 fatty acids make them excellent candidates as functional food ingredients if problems with oxidative rancidity can be overcome. Oil-in-water emulsions were prepared with 2% salmon oil, stabilized by 0.2% Brij 35 at pH 7. To determine the effects of heating (50–90 °C), ethylenediaminetetraacetic acid (EDTA), and calcium on the oxidative and physical stability of salmon oil-in-water emulsions, particle size, thiobarbituric acid reactive substances (TBARS), and lipid hydroperoxides were measured. The heat-processed emulsions showed no significant difference, in particle size, TBARS or hydroperoxides during storage, from unheated emulsions. Above 2.5 μM, EDTA dramatically decreased lipid oxidation in all samples. Addition of calcium to emulsions containing 7.5 μM EDTA significantly increased both TBARS and hydroperoxide formation when calcium concentrations were 2-fold greater than EDTA concentrations. These results indicate that heat-processed salmon oil-in-water emulsions with high physical and oxidative stability could be produced in the presence of EDTA.     

Impact of thermal processing on the antioxidant mechanisms of continuous phase β-lactoglobulin in oil-in-water emulsions

The influence of native and thermally (50–95 °C) denatured β-lactoglobulin (β-Lg) on the oxidative stability of surfactant-stabilized menhaden oil-in-water emulsions (pH 7.0) was evaluated. β-Lg (500 μg/g oil) heated at 95 °C for 30 min provided the best protection against lipid oxidation, inhibiting the formation of lipid hydroperoxides and thiobarbituric acid reactive substances (TBARS) by 87% and 88%, respectively, following 7 days of storage. The possible mechanisms of antioxidant activity of native and heated β-Lg were evaluated by measuring peroxyl radical scavenging and iron chelating capacities of the protein treatments, as well as reactive sulfhydryl concentrations and tryptophan fluorescence (a marker of protein conformation changes). The aforementioned in vitro assays only partially corroborated the results from the oxidizing emulsion system since β-Lg heated at 95 °C exhibited the lowest iron chelation capacity and free sulfhydryl concentration, yet displayed the highest peroxyl radical scavenging capacity and inhibition of lipid oxidation in oil-in-water emulsions of all treatments tested. The results of this study demonstrate the feasibility of proteins as a natural class of antioxidants in food emulsions, and further elucidate the possible mechanisms by which proteins inhibit lipid oxidation.     

Relationship between the physical properties of chlorogenic acid esters and their ability to inhibit lipid oxidation in oil-in-water emulsions

In oil-in-water emulsions, the physical location of antioxidants has been postulated to be one of the most important factors impacting activity. The purpose of this research was to examine how the esterification of various hydrocarbon chains (C₄, C₈, or C₁₂) onto chlorogenic acid (CGA) influenced physical properties and antioxidant activity in menhaden oil-in-water emulsions. Both surface activity and partitioning of CGA and its hydrocarbon esters into the lipid phase of oil-in-water emulsions increased with increasing size of the hydrocarbon chain. When CGA and its esters were added to a menhaden oil-in-water emulsion at concentration that resulted in equal free radical scavenging activity, CGA, butyl CGA and octyl CGA had similar antioxidant activity while dodecyl CGA was ineffective. These results suggest that phenolic antioxidants conjugated with hydrocarbon chains are more highly associated with lipid emulsions droplets, but these changes in physical properties did not increase antioxidant activity.     

Improvement of stability of oil-in-water emulsions containing caseinate-coated droplets by addition of sodium alginate

ABSTRACT:  The potential of sodium alginate for improving the stability of emulsions containing caseinate-coated droplets was investigated. One wt% corn oil-in-water emulsions containing anionic caseinate-coated droplets (0.15 wt% sodium caseinate) and anionic sodium alginate (0 to 1 wt%) were prepared at pH 7. The pH of these emulsions was then adjusted to 3.5, so that the anionic alginate molecules adsorbed to the cationic caseinate-coated droplets. Extensive droplet aggregation occurred when there was insufficient alginate to completely saturate the droplet surfaces due to bridging flocculation, and when the nonadsorbed alginate concentration was high enough to induce depletion flocculation. Emulsions with relatively small particle sizes could be formed over a range of alginate concentrations (0.1 to 0.4 wt%). The influence of pHs (3 to 7) and sodium chloride (0 to 500 mM) on the properties of primary (0 wt% alginate) and secondary (0.15 wt% alginate) emulsions was studied. Alginate adsorbed to the droplet surfaces at pHs 3, 4, and 5, but not at pHs 6 and 7, due to electrostatic attraction between anionic groups on the alginate and cationic groups on the adsorbed caseinate. Secondary emulsions had better stability than primary emulsions at pH values near caseinate's isoelectric point (pHs 4 and 5). In addition, secondary emulsions were stable up to higher ionic strengths (< 300 mM) than primary emulsions (<50 mM). The controlled electrostatic deposition method utilized in this study could be used to extend the range of application of dairy protein emulsifiers in the food industry.     

Rheological properties and stability of oil-in-water emulsions containing tapioca maltodextrin in the aqueous phase

The present research focuses on the effect of the concentration and dextrose equivalent (DE) values of tapioca maltodextrin in the aqueous phase on rheological behavior and stability of oil-in-water emulsions prepared with Tween80. The critical flocculation concentrations (CFCs) of oil-in-water emulsions containing tapioca maltodextrin with DE of 16 (DE16), 12 (DE12) and 9 (DE9) were 11%, 9% and 7% (w/w) respectively, as revealed by transmittance measurement. Coalescence was observed as maltodextrin concentration increased above the CFC. The rheological parameters of flow behavior index (n) and consistency index (k) have been well-described by the Herschel–Bulkley model. The relative consistency index (k_relative) increased markedly when the concentration of maltodextrin exceeded the CFC because of depleting flocculation. The consistency index (k_emulsion) and yield stress (τ₀) of emulsions containing tapioca maltodextrin increased with increasing maltodextrin concentration or decreasing DE. The emulsions containing maltodextrin showed Newtonian flow behavior when the maltodextrin concentration was below the CFC. At maltodextrin concentrations above the CFC, emulsions containing maltodextrin exhibited shear thinning behavior. An increase in the maltodextrin concentration resulted in a decrease in the n_emulsion until maltodextrin concentration reached 20% (w/w) for DE9, DE12 and 25% (w/w) for DE16. Further increase in the maltodextrin concentration resulted in an increased the n_emulsion because of predominant influence of the continuous phase.     

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

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

State of dispersed lipid carrier and interface composition as determinants of beta-carotene stability in oil-in-water emulsions

Abstract: Liposoluble bioactive compounds are often included in foods in emulsified lipid carriers. In the present study, the impact of the physical state of the lipid carrier and the interfacial composition of oil‐in‐water emulsions on the stability of β‐carotene was studied. Emulsions with hydrogenated palm kernel oil (HPKO) concentration of 10% (w/w) dispersing 0.05% (w/w) β‐carotene, and a water phase at pH 7 containing 30% (w/w) sucrose, were stabilized by 1%, 1.5%, 2%, and 3% (w/w) whey protein isolate (WPI). Crystallization and melting behavior of emulsified and bulk HPKO were studied by differential scanning calorimetry. The hysteresis of emulsified HPKO crystallization (onset approximately 10 °C; endset approximately 6 °C) and melting (onset approximately 17 °C; endset approximately 45 °C) allowed us to operate at 15 °C on systems with identical compositions but different physical states of the same lipid phase. Surface protein coverage of emulsions was calculated and size of the dispersed particles was characterized by dynamic light scattering. β‐Carotene contents of the emulsions during storage at 15 °C was analyzed spectrophotometerically. Results highlighted an impact of the phase of the lipid carrier and of the concentration of WPI on β‐carotene degradation. β‐Carotene loss showed zero‐order kinetics. A liquid dispersed phase resulted in a low degradation rate but a high concentration of protein on a solid lipid carrier was likewise effective for β‐carotene protection. Practical Application: The inclusion of lipophilic bioactive compounds, such as carotenoids, is a current trend in the production of functional foods aiming to enhance health and well‐being. However, the use of functional ingredients in food products is complicated because of the sensitivity of the active molecules to physical and chemical factors to which they are exposed during processing, storage, and consumption. The present work gives indications of the influence of the lipid carrier physical state and surface structure on ß‐carotene stability in formulated oil‐in‐water liquid food models, suggesting possible strategies for an enhanced stabilization of lipophilic labile compounds.     

Effects of composition and processing variables on the oxidative stability of protein-based and oil-in-water food emulsions

Because many common foods are emulsions (mayonnaise, coffee creamers, salad dressing, etc.), a better understanding of lipid oxidation mechanisms in these systems is crucial for the formulation, production, and storage of the relevant consumer products. A research body has focused on the microstructural and oxidative stability of protein-stabilized oil-in-water emulsions that are structurally similar to innovative products that have been recently developed by the food industry (e.g., non-dairy creams, vegetable fat spreads, etc.) This review presents recent findings about the factors that determine the development of lipid oxidation in emulsions where proteins constitute the stabilizing interface. Emphasis is given to “endogenous” factors, such as those of compositional (e.g., protein/lipid phases, pH, presence of transition metals) or processing (e.g., temperature, droplet size) nature. Improved knowledge of the conditions that favor the oxidative protection of protein in emulsions can lead to their optimized use as food ingredients and thereby improve the organoleptic and nutritional value of the related products.