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The digestion, absorption, uptake and bioavailability of a rosemary supercritical fluid extract encapsulated in oil in water emulsion were studied. Two emulsions with opposite surface charge were prepared, containing 7% canola oil, and either 2% lactoferrin or whey protein isolate. When absorption and uptake of carnosic acid and carnosol were followed on Caco-2 cell monolayers, there were no differences with protein type. However, when co-cultures of HT-29 MTX were employed, the presence of mucus caused a higher retention of carnosic acid in the apical layer for lactoferrin emulsions. The immune activity of the bioavailable fractions collected from cell absorption experiments was tested ex vivo on murine splenocytes. Although transport through the intestinal barrier models was low, the bioavailable fractions showed a significant effect on splenocytes proliferation. These results demonstrated the potential of using rosemary supercritical extract through protein stabilized oil in water emulsions, as a food with immunomodulatory functionality., (Copyright © 2017 Elsevier Ltd. All rights reserved.)

Encapsulation in lipid particles is often proposed as a solution to improve curcumin bioavailability. This bioactive molecule has low water solubility and rapidly degrades during digestion. In the present study, the uptake of curcumin from oil in water emulsions, prepared with two different emulsifiers, Tween 20 and Poloxamer 407, was investigated to determine the effect of interfacial composition on absorption. Piperine was added to the curcumin to limit the degradation of curcumin because it is known to inhibit β-glucuronidase activity. The emulsions were administered to Caco-2 cell cultures, which is used as a model for intestinal uptake, and the recovery of curcumin was measured. The curcumin uptake was significantly affected by the type of interface, and the extent of curcumin uptake improved significantly by piperine addition only in the case of oil-in-water emulsions stabilized by Poloxamer 407. This work provides further evidence of the importance of interfacial composition on the delivery of bioactives.

Scope: Solubilization of lipophilic bioactives in gastrointestinal fluids contributes to their bioavailability, but a better understanding of the transfer processes involved and the impact of molecular structure is required., Methods and Results: The transfer of β-carotene (BC), coenzyme Q10 (CoQ10), vitamin D3 (VitD3), and phytosterols (PSs) from soy protein isolate-stabilized oil-in-water emulsions to the aqueous phase during in vitro digestion was investigated. In the absence of lipolysis, transfer was mainly governed by molecular structure and partitioning within the oil droplets. Less than 3% BC and CoQ10, versus 30.4 ± 0.3% PSs and 24.7 ± 0.4% VitD3, were transferred in this case. However, with lipolysis, PSs and VitD3 rapidly partitioned into the aqueous phase, while lag phases and slower transfer rates were observed for BC and CoQ10. Positive and linear correlations between lipolysis and transfer were observed for all systems. After 2 h exposure to simulated duodenal conditions, there were no differences between percent micellization, except for BC which was proportionally lower. VitD3 and PSs mutually enhanced each other's transfer, while no interactions were observed between VitD3 and BC., Conclusion: Bioactive molecular structure and co-administration influenced the transfer behaviour, with implications for foods designed to optimize health benefits., (Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Proteins are often used as ingredients in food emulsions, as their amphiphilic structures provide electrostatic and steric stabilization. Significant attention has recently been directed at understanding how the composition and structure of oil-water interfaces change during digestion and how these can be manipulated to enhance the delivery of nutrients contained within the oil droplets. These efforts have necessitated the development of more sophisticated in vitro digestion models of greater physiological relevance and increased efforts in research to identify the role of the various digestive parameters on interfacial dynamics. The changes occurring at the oil-water interface will affect the adsorption of gastro-intestinal lipases and, ultimately, affect lipid digestion. The composition of a protein-stabilized oil droplet changes continuously during digestion, because of proteolysis and the formation of peptides with different affinities for the interface. In addition, natural bio-surfactants such as phospholipids and bile salts, other surface- active molecules present in foods, and the products of lipolysis (i.e. mono and diglycerides, lysophospholipids), all compete for access to the interface, and contribute to the dynamic changes occurring on the surface of the oil droplets. A better understanding of how to tailor the composition of oil droplet surfaces in food emulsions will aid in optimizing lipid digestion and, as a result, delivery of lipophilic nutrients. This review focuses on the physico-chemical changes occurring in protein-stabilized oil-in-water emulsions during gastric and small intestine digestion, and on how interfacial engineering could lead to differences in fatty acid release and the potential bioavailability of lipophilic molecules.

Rheological and microstructural properties of rennet-induced milk gels containing different fat globules were studied. Recombined milks were prepared by mixing reconstituted low-heat skim milk powder and anhydrous milk fat emulsified with reconstituted skim milk powder (SMP), sodium caseinate (NaCas), whey protein isolate (WPI) or Tween 20. Final elastic modulus of the rennet gels containing WPI- or Tween 20-stabilized fat globules showed significantly lower values compared with those prepared with SMP-emulsified fat globules. SMP-stabilized fat globules interacted with the continuous casein network reinforcing the gel structure. Confocal micrographs supported the rheological data revealing that gels containing SMP-stabilized fat globules formed a tighter network relative to other treatments. Microscopy images also showed some degree of droplet flocculation in the case of gels containing WPI- or Tween 20-stabilized fat globules, and this was most likely the cause of the increase of elastic modulus of these systems. Contrary to reports for acid-induced casein gels, NaCas-stabilized fat globules hindered the formation of rennet gels. These results illustrate that rennet gel structure is affected by droplet-droplet and droplet-casein interactions, which in turn are determined by the composition of the oil-water interface as well as the ionic equilibrium in the reconstituted milk gels.

The interactions of high-methoxyl pectin (HMP) and soybean-soluble polysaccharide (SSPS) with sodium caseinate-stabilized emulsions were investigated using a multitechnique approach, including dynamic light scattering (DLS), electrophoretic mobility measurements, transmission diffusing wave spectroscopy (DWS), and ultrasonic spectroscopy (US). At pH 6.8, both polysaccharides are negatively charged and did not adsorb onto caseinate-coated droplets due to electrostatic repulsion; however, SSPS showed a different behavior compared to HMP in the turbidity parameter 1/l* and sound attenuation parameters measured by DWS and US, respectively. The present study brought the first evidence of the stabilization effect of SSPS in acidified sodium caseinate-emulsions. While destabilization occurred at low polysaccharide concentrations, probably via bridging flocculation, acid-induced aggregation of the oil droplet was completely prevented by 0.2% SSPS or HMP. However, the interaction behavior of SSPS during acidification was different from that of HMP. This was demonstrated by the different development of the parameter 1/l*, droplet sizes, sound attenuation, and velocity.

The effect of heating on the physicochemical properties of emulsions prepared with soybean soluble polysaccharide (SSPS) was investigated. The emulsions were stable after heating at 90 degrees C for up to 30 min. Heating at different pH values or in the presence of CaCl2 (<10 mM) did not affect the stability; however, at higher concentrations of calcium ions, the emulsion particle size increased. Two fractions, a high molecular weight (HMF) and a low molecular weight (LMF) fraction, were separated from the crude SSPS preparation by gel fitration. Emulsions prepared with SSPS/HMF (MW = 310-420 kDa) showed little change in size with heating, while the protein impurities of the SSPS/LMF fraction formed aggregates by heating at pH 7. Analysis of the heat-induced aggregation of the two fractions of SSPS suggested that the changes in SSPS functionality with heating can be attributed to the protein impurities (LMF) present in the SSPS.

The stability of emulsions prepared with soy protein isolates was investigated as a function of pH in the presence of two negatively charged polysaccharides: high methoxyl pectin (HMP) and soy soluble polysaccharide (SSPS). Both polysaccharides are composed of a backbone which contains galacturonic acid but, when added to soy protein isolate-stabilized emulsions, SSPS showed a different behavior than that of HMP. At neutral pH and above a critical concentration of stabilizer (0.05%), HMP caused flocculation of the emulsion droplets via a depletion mechanism. On the other hand, the emulsions containing a similar amount of SSPS did not show creaming or flocculation. At acidic pH (<4.0) the addition of pectin caused extensive droplet aggregation, while no aggregation was observed with the addition of SSPS. The differences in the stabilization behavior between the two polysaccharides can be attributed to their differences in charge, neutral sugars side chains, and molecular weight.

Polysaccharides are widely used in the food industry to modify the stability of protein-based drinks. However, an in depth knowledge of the interactions occurring in the system is still lacking. In this study, the interactions between sodium caseinate and high methoxyl pectin under acidification conditions were studied nondestructively and without dilution using transmission diffusing wave spectroscopy. Oil-in-water emulsions were prepared with 10% soybean oil and 0.5% sodium caseinate. Various concentrations of pectin (ranging from 0 to 0.2%) were added, and the emulsions were acidified with glucono-delta-lactone. With acidification, a "sol-gel" transition occurred and emulsions containing pectin were more stable at lower pH than those without pectin. Furthermore, the sol-gel transition of the mixtures was more sudden for control emulsions without pectin. While in control samples the final solidlike emulsion after gelation tended to be more inhomogeneous and more dissimilar to the starting emulsion, emulsions with pectin in solution gelled later under acidification. With a sufficient amount of pectin, the emulsions showed no aggregation and the destabilization pH varied depending on the amount of pectin present in the emulsions. At intermediate pH values (pH > 5.5), the emulsions displayed a decrease in particle size, more pronounced in samples containing pectin. The results collected using light scattering in concentrated systems, 10% (v/v) in our case, suggested that pectin stabilizes the emulsion oil droplets forming a network of oil droplets loosely connected by strands of pectin.

The interactions between whey protein isolate (WPI) and high methoxyl pectin (HMP) at pH 3.5 were investigated in situ using ultrasound (US) and diffusing wave spectroscopy (DWS). HMP was added to 10% oil-in-water emulsions containing 1% WPI. At neutral pH, no protein-pectin interactions were observed as both molecules are negatively charged, while at pH 3.5 bridging flocculation occurred via electrostatic interactions. Four different stages were distinguished during the addition of HMP in WPI-stabilized emulsions at pH 3.5. At a concentration below a critical value, no interactions were observed. At concentrations >0.02% HMP, a change in the l factor indicated a change in the ordering of the emulsion droplets, influenced by long-range interactions. At higher concentrations (in the range between 0.04 and 0.06% HMP), attenuation showed significant changes in the surface of the oil droplets, changes which affected the droplet-droplet interactions. At pectin concentrations >0.05%, attenuation of sound and 1/l* decreased, while velocity of sound and particle size increased, as a result of bridging flocculation. These results demonstrated for the first time that methods such as US and DWS combined permit the observation of the early stages of the interactions between two biopolymers at the interface. This is significant in light of increasing efforts in engineering complex interfacial layers.

The effects of temperature, time, metal, citric acid, and tocopherol contents on the oxidation stability of a model oil-in-water emulsion prepared with enzymatically synthesized menhaden oil-caprylic acid structured lipid were evaluated by response surface methodology. The emulsions were stabilized by whey protein isolate. Oxidation was monitored by measuring lipid hydroperoxides and thiobarbituric acid reactive substances (TBARS). Cupric sulfate and ferrous sulfate were used to study the effect of metal concentration and type. A statistical model was developed to determine the relationships between all variables considered. The relationships differed depending on the type of metal catalyst used. For both metal types, the metal concentration had the highest positive effect on peroxide value. Citric acid had the highest negative effect on peroxide value for iron-containing emulsions, while tocopherol had the highest negative effects for copper-containing emulsions. Results from the TBARS test did not vary significantly enough to yield an acceptable model.

The effects of the emulsifiers lecithin, Tween 20, whey protein isolate, mono-/diacylglycerols, and sucrose fatty acid ester on oxidation stability of a model oil-in-water emulsion prepared with enzymatically synthesized menhaden oil-caprylic acid structured lipid were evaluated. Oxidation was monitored by measuring lipid hydroperoxides, thiobarbituric acid reactive substances, and the ratio of combined docosahexaenoic acid (DHA) and eicosapentaenoic acid (EPA) contents to palmitic acid in the emulsion. After high-pressure homogenization, all emulsions, except those prepared with lecithin, had similar droplet size distributions. All structured lipid emulsions, except for the lecithin-stabilized emulsions, were stable to creaming over the 48-day period studied. Emulsifier type and concentration affected oxidation rate, with 0.25% emulsifier concentration generally having a higher oxidation rate than 1% emulsifier concentration. Overall, oxidation did not progress significantly enough in 48 days of storage to affect DHA and EPA levels in the emulsion.

BSTRACT: 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. [ABSTRACT FROM AUTHOR]

BSTRACT: Oil-in-water emulsions containing a commercial fraction of soy protein concentrate (SPC) were characterized for stability and microstructural differences. Emulsions were prepared with SPC (concentrations between 1% and 10% (w/v)) and soybean oil (10% w/w) and homogenized at 80 MPa. When SPC was added at a concentration high enough to be present in the dispersed phase, the average particle size, as determined by integrated light scattering, reached a plateau value. In addition, emulsions prepared with > 4% SPC showed increased viscosity with increasing SPC concentration. The protein formed a continuous network and emulsions were stable to creaming. Microstructural observations showed that phase separation occurred in emulsions prepared with high SPC concentrations. [ABSTRACT FROM AUTHOR]

Abstract: Structural changes ensuing from denaturation of soy proteins in solution or occurring at the oil–water interface were studied by fluorescence spectroscopy. Studies were carried out on solutions and emulsions stabilized with β-conglycinin or glycinin. Tryptophan fluorescence spectroscopy was used to evaluate tertiary structural changes. The binding of fluorescent dyes and the accessibility of reactive cysteine thiols were also used to better identify structural changes of these proteins in solution. Protein conformational changes after interaction with the hydrophobic oil surface were compared with those ensuing from physical (temperature) or chemical denaturation (chaotropes). Results from solution denaturation experiments indicate that structural changes of β-conglycinin by both temperature and chaotropes are reversible under appropriate conditions, and result in a rearrangement of the supramacromolecular assembly of the protein structure. On the other hand, glycinin treated under the same conditions undergoes irreversible denaturation in solution at temperatures well below 90°C. Both proteins undergo partial denaturation after adsorption on the lipid surface, and no further denaturation occurs upon heating of the emulsions prepared with either protein. [Copyright &y& Elsevier]

• In situ gelation of pectin created nanocapsules in the inner phase. • Multiple emulsions with gelled nanocapsules required less emulsifier. • Magnesium and brilliant blue release was not affected by the gelled inner phase. Pectin nanocapsules were obtained by gelling the inner droplets, in situ, in a multiple emulsion of the water in oil in water (W/O/W) type, using the enzyme Pectin methyl esterase. The inner phase was tested for its encapsulation efficiency by addition of brilliant blue or magnesium chloride. Rheological measurements and light scattering showed similarities for gelled and non gelled droplets containing high methoxy pectin. After one month of storage, the gelled nanocapsules showed a population of larger droplets, not appearing in the other W/O/W emulsions: the non gelled pectin droplets or control with no pectin. Confocal microscopy observations demonstrated the presence of the inner water droplets in all emulsions after one month of storage at 4 °C. Brilliant blue was retained in the inner droplets containing pectin, and the retention was not affected by the gelled inner phase. Magnesium ions were retained in all treatments, even in the case of control W/O/W emulsions, not containing pectin. With both systems studied, the presence of gelled nanocapsules did not cause significant differences in the encapsulation efficiency or stability of the W/O/W emulsions. [ABSTRACT FROM AUTHOR]