Effects often overlooked in lipid oxidation in oil-in-water emulsions:Agitation conditions and headspace-to-emulsion ratio

The effects of the agitation conditions and headspace-to-emulsion volume ratio on lipid oxidation in emulsions can be considerable, but have not been systematically investigated yet. In the current paper, lipid oxidation was monitored in model oil-in-water (O/W) emulsions at pH 4.0 and 25°C in the presence of 200 μM iron sulfate. The formation of primary (conjugated dienes and hydroperoxides) and secondary (p-anisidine value and TBARS) oxidation products confirmed that using rotating or shaking devices doubled the rate of oxidation product formation compared to a non-agitated system, as a result of enhanced oxygen transfer. Furthermore, we found that a higher headspace-to-emulsion volume ratio at least doubled the rate of lipid oxidation due to a higher amount of oxygen available per mass of oil, which is in agreement with the kinetics of the reaction. This indicates that the variation in literature data on lipid oxidation in emulsions can be attributed to differences in mixing conditions and volume ratios. These factors are crucial and should be reported systematically along with the agitation conditions, and sampling method. This will enable a better comparison of literature information.</p

Chemical Stability of α-Tocopherol in Colloidal Lipid Particles with Various Morphologies

Colloidal lipid particles (CLPs) are promising encapsulation systems for lipophilic bioactives, such as oil-soluble antioxidants that are applied in food and pharmaceutical formulations. Currently, there is no clear consensus regarding the relation between particle structure and the chemical stability of such bioactives. Using α-tocopherol as a model antioxidant, it is shown that emulsifier type (Tween 20 or 40, or sodium caseinate) and lipid composition (tripalmitin, tricaprylin, or combinations thereof) modulated particle morphology and antioxidant stability. The emulsifier affects particle shape, with the polysorbates facilitating tripalmitin crystallization into highly ordered lath-like particles, and sodium caseinate resulting in less ordered spherical particles. The fastest degradation of α-tocopherol is observed in tripalmitin-based CLPs, which may be attributed to its expulsion to the particle surface induced by lipid crystallization. This effect is stronger in CLPs stabilized by Tween 40, which may act as a template for crystallization. This work not only shows how the architecture of CLPs can be controlled through the type of lipid and emulsifier used, but also gives evidence that lipid crystallization does not necessarily protect entrapped lipophilic bioactives, which is an important clue for encapsulation system design. Practical Applications: Interest in enriching food and pharmaceutical products with lipophilic bioactives such as antioxidants through encapsulation in lipid particles is growing rapidly. This research suggests that for efficient encapsulation, the particle architecture plays an important role; to tailor this, the contribution of both the lipid carrier and the emulsifier needs to be considered.</p

Physicochemical stability of lycopene-loaded emulsions stabilized by plant or dairy proteins

Lycopene is a lipophilic bioactive compound that has many health benefits but can be challenging to deliver in vivo. To mediate this, delivery strategies should be developed, and protein-stabilized oil-in-water (O/W) emulsions have been suggested to improve the physicochemical stability, bioaccessibility and bioavailability of lycopene. In this research different proteins were compared to determine their impact on the physical stability (droplet size, charge, interfacial rheology) and lycopene retention in canola O/W emulsions. Two were of dairy (whey protein isolate, sodium caseinate) and two of plant (soy and pea protein isolate) origin; plant proteins being of interest due to their wider availability, reduced cost, and lower impact on the environment compared to dairy proteins. Particle size distribution for sodium caseinate and pea protein-stabilized emulsions remained unchanged after 14 days of refrigerated storage, while whey and soy protein isolate-stabilized emulsions became unstable. The droplet charge was largely negative (~ -45 – -60 mV) for all emulsions and the lycopene concentration in plant protein-stabilized emulsions at 14 days of storage was similar to that in sodium caseinate-stabilized emulsions, but significantly higher than that in whey proteinstabilized emulsions. While sodium caseinate formed relatively viscous films at the oil-water interface, the other proteins showed more viscoelastic behaviour. In spite of this difference, both the caseinate and pea protein stabilized emulsions were promising delivery vehicles. This also indicates that plant-derived proteins can be feasible alternatives to dairy emulsifiers

Tiny, yet impactful:Detection and oxidative stability of very small oil droplets in surfactant-stabilized emulsions

Hypothesis: The shelf life of multiphase systems, e.g. oil-in-water (O/W) emulsions, is severely limited by physical and/or chemical instabilities, which degrade their texture, macroscopic appearance, sensory and (for edible systems) nutritional quality. One prominent chemical instability is lipid oxidation, which is notoriously complex. The complexity arises from the involvement of many physical structures present at several scales (1–10,000 nm), of which the smallest ones are often overlooked during characterization. Experiments: We used cryogenic transmission electron microscopy (cryo-TEM) to characterize the coexisting colloidal structures at the nanoscale (10–200 nm) in rapeseed oil-based model emulsions stabilized by different concentrations of a nonionic surfactant. We assessed whether the oxidative and physical instabilities of the smallest colloidal structures in such emulsions may be different from those of larger colloidal structures. Findings: By deploying cryo-TEM, we analyzed the size of very small oil droplets and of surfactant micelles, which are typically overlooked by dynamic light scattering when larger structures are concomitantly present. Their size and oil content were shown to be stable over incubation, but lipid oxidation products were overrepresented in these very small droplets. These insights highlight the importance of the fraction of “tiny droplets” for the oxidative stability of O/W emulsions.</p

The role of endogenous lipids in the emulsifying properties of cocoa

This paper describes a study in which the emulsifying properties of cocoa material with and without its lipid fraction were explored. This study was motivated by the commercial interest in naturally-occurring particulate emulsifiers as opposed to the chemically modified emulsifying particles presently available for commercial use. The hypothesis was that endogenous lipids from cocoa were responsible for driving the formation of stable oil-in-water (o/w) emulsions. The data presented includes relative quantification of phospholipids from different commercially available cocoa material using 31P NMR spectroscopy and analyses of the emulsifying power of delipidified cocoa material. The commercially available cocoa material comprised several phospholipids, with phosphatidylcholine being the most abundant in all samples. Dispersions of delipidified cocoa material were found to drive the formation of o/w emulsions despite the absence of lipids. We therefore concluded that the emulsifying behaviour of cocoa material is not entirely reliant upon the endogenous lipids. This suggests that cocoa material may have a new and potentially widespread use in industrial food preparation and may inform manufacturing strategies for novel food grade emulsifiers

In vitro digestion of Pickering emulsions stabilized by soft whey protein microgel particles: influence of thermal treatment

Emulsions stabilized by soft whey protein microgel particles have gained research interest due to their combined advantages of biocompatibility and a high degree of resistance to coalescence. We designed Pickering oil-in-water emulsions using whey protein microgels by a facile route of heat-set gel formation followed by mechanical shear and studied the influence of heat treatment on emulsions stabilized by these particles. The aim of this study was to compare the barrier properties of the microgel particles and heat-treated fused microgel particles at the oil–water interface in delaying the digestion of the emulsified lipids using an in vitro digestion model. A combination of transmission electron microscopy and surface coverage measurements revealed an increased coverage of heat-treated microgel particles at the interface. The heat-induced microgel particle aggregation and, therefore, a fused network at the oil–water interface were more beneficial to delay the rate of digestion in the presence of pure lipase and bile salts compared to intact whey protein microgel particles, as shown by the measurements of zeta potential and free fatty acid release, plus theoretical calculations. However, simulated gastric digestion with pepsin impacted significantly on such barrier effects, due to the proteolysis of the particle network at the interface irrespective of the heat treatment, as visualized using sodium dodecyl sulfate polyacryl amide gel electrophoresis measurements

Whey protein microgel particles as stabilizers of waxy corn starch + locust bean gum water-in-water emulsions

Food-grade whey protein isolate (WPI) microgel particles were investigated as a particle stabilizer of water-in-water (W/W) emulsions. The microgel particles were produced via the novel method of forcing coarse particles of a pre-formed thermally processed WPI protein gel through a jet homogenizer. The Z-average particle size was 149 ± 89 nm but the particles showed a strong tendency for aggregation when the pH was lowered from pH 7 to 4, when the zeta potential also switched from -17 to +12 mV. The viscoelasticity of suspensions of the particles, measured between 1 and 15 vol.% (0.02 and 3 wt.%) increased with concentration and was also higher at pH 4 than pH 7. However, all the suspensions were only weakly shear thinning, suggesting that they did not form very strong networks. The particles were added (at 1-15 vol.%) to a model W/W system consisting of waxy corn starch (S) + locust bean gum (LBG) that normally shows phase separation when the components are mixed at 90 °C then cooled to room temperature (22-25 °C). At 10 to 15 vol.% particles and pH 4, visual observation showed striking inhibition of phase separation, for a period of up to 1 year. Confocal laser scanning microscopy suggested that under these conditions extensive aggregation of the microparticles occurred within the starch phase but also possibly at the W/W interface between the starch-rich and gum-rich regions, supporting a Pickering-type mechanism as responsible for the enhanced stabilization of the W/W emulsion by the microgel particles

Identification of emulsifier potato peptides by bioinformatics: application to omega-3 delivery emulsions and release from potato industry side streams

We are grateful for the financial support from Innovation Fund Denmark (Grant nr: 7045-00021B, PROVIDE project). We also acknowledge K.M.C. amba (Brande, Denmark) and A.K.V. amba (Langholt, Denmark) for providing the potato samples used in this study.In this work, we developed a novel approach combining bioinformatics, testing of functionality and bottom-up proteomics to obtain peptide emulsifiers from potato side-streams. This is a significant advancement in the process to obtain emulsifier peptides and it is applicable to any type of protein. Our results indicated that structure at the interface is the major determining factor of the emulsifying activity of peptide emulsifiers. Fish oil-in-water emulsions with high physical stability were stabilized with peptides to be predicted to have facial amphiphilicity: (i) peptides with predominantly α-helix conformation at the interface and having 18–29 amino acids, and (ii) peptides with predominantly β-strand conformation at the interface and having 13–15 amino acids. In addition, high physically stable emulsions were obtained with peptides that were predicted to have axial hydrophobic/hydrophilic regions. Peptides containing the sequence FCLKVGV showed high in vitro antioxidant activity and led to emulsions with high oxidative stability. Peptide-level proteomics data and sequence analysis revealed the feasibility to obtain the potent emulsifier peptides found in this study (e.g. γ-1) by trypsin-based hydrolysis of different side streams in the potato industry.Innovation Fund Denmark 7045-00021