Effect of medium molecular weight xanthan gum in rheology and stability of oil‐in‐water emulsion stabilized with legume proteins

Xanthan gum is a water‐soluble extracellular polysaccharide that has gained widespread commercial use because of its strong pseudoplasticity and tolerance to high ionic strength, which bring unique rheological properties to solutions. This study compares and evaluates the emulsifying properties of oil‐in‐water (30:70 v/v) emulsions stabilized with lupin and soya protein isolates and medium molecular weight xanthan gum. The protein was obtained by an isoelectric precipitation method and the polysaccharide was produced by Xanthomonas campestris ATCC 1395 in batch culture in a laboratory fermenter (LBG medium) without pH control. The addition of xanthan gum in the emulsion formulation enhances emulsion stability through the phenomenon of thermodynamic incompatibility with the legume protein, resulting in an increase of the adsorbed protein at the interface. The emulsion stability is also enhanced by a network structure built by the polysaccharide in the bulk phase. Copyright © 2005 Society of Chemical Industry     

The effect of glycosylation on emulsifying and structural properties of bovine β‐casein

A number of attempts have been made to improve the functional properties of milk proteins by chemical modifications. One of such modifications is glycosylation which was carried out to determine the effect of covalent binding of glucose molecules to β‐casein (βCN) on its emulsifying properties. It was found that up to six molecules of glucose were bound to one molecule of βCN. Glycosylated βCN produced smaller emulsion droplets than the intact βCN. Increases in emulsion‐forming and ‐stabilizing properties were observed. A prerequiste of proteins to form emulsions is their adsorption onto oil/water interface. Therefore the secondary structure of intact and glycosylated βCN, both in solution and adsorbed onto a hydrophobic teflon/water interface also were studied by far‐ultra violet circular dichroism (CD). It appeared, that after glycosylation the degree of helicity of intact βCN decreased and the incorporation of glucose moieties most likely resulted in a type β‐turn formation after adsorption onto the interface.     

In vitro β‐Carotene Bioaccessibility and Lipid Digestion in Emulsions: Influence of Pectin Type and Degree of Methyl‐Esterification

Citrus pectin (CP) and sugar beet pectin (SBP) were demethoxylated and fully characterized in terms of pectin properties in order to investigate the influence of the pectin degree of methyl‐esterification (DM) and the pectin type on the in vitro β‐carotene bioaccessibility and lipid digestion in emulsions. For the CP based emulsions containing β‐carotene enriched oil, water and pectin, the β‐carotene bioaccessibility, and lipid digestion were higher in the emulsions with pectin with a higher DM (57%; “CP57 emulsion”) compared to the emulsions with pectin with a lower DM (30%; “CP30 emulsion”) showing that the DM plays an important role. In contrast, in SBP‐based emulsions, nor β‐carotene bioaccessibility nor lipid digestion were dependent on pectin DM. Probably here, other pectin properties are more important factors. It was observed that β‐carotene bioaccessibility and lipid digestion were lower in the CP30 emulsion in comparison with the CP57, SBP32, and SBP58 emulsions. However, the β‐carotene bioaccessibility of CP57 emulsion was similar to that of the SBP emulsions, whereas the lipid digestion was not. It seems that pectin type and pectin DM (in case of CP) are determining which components can be incorporated into micelles. Because carotenoids and lipids have different structures and polarities, their incorporation may be different. This knowledge can be used to engineer targeted (digestive) functionalities in food products. If both high β‐carotene bioaccessibility and high lipid digestion are targeted, SBP emulsions are the best options. The CP57 emulsion can be chosen if high β‐carotene bioaccessibility but lower lipid digestion is desired.     

pH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins

Emulsifying properties of two partially purified legumin and vicilin (PL and PV) and protein isolate (PPI) from dry pea seeds at various pH values (3.0, 5.0, 7.0 and 9.0) were investigated. The tested emulsion characteristics included droplet size, flocculation and coalescence indices (FI and CI), creaming index, as well as interfacial protein adsorption. Some physicochemical properties of these proteins, e.g., free sulfhydryl and disulfide bond contents, protein solubility (PS), surface hydrophobicity (H_o) and thermal stability (and denaturation), were also characterized. The results indicated that emulsifying ability and emulsion stability of various pea proteins considerably varied with the preparation process, protein composition and pH. Overall, all the pea proteins exhibited least emulsifying ability at pH 5.0 (around isoelectric point), and concomitantly, the resultant emulsions were most unstable against coalescence and creaming. The emulsifying ability of these proteins at pH 3.0 was generally better than that at neutral or alkali pH values, and among all the three proteins, PL exhibited highest emulsifying ability at this pH. The flocculated state and size of droplets in fresh emulsions did not directly affect stability of these emulsions against flocculation and coalescence (upon 24 h of storage), and even creaming (up to 7 days). Interestingly, the PL and PV exhibited much better creaming stability than PPI, at pH deviating from the pI. The emulsifying properties of these proteins were not only related to their PS and H_o, but also associated with the protein adsorption and nature (e.g., viscoelasticity) of interfacial protein films. These results can greatly extend the knowledge for understanding the emulsifying properties of pea proteins, especially the pH dependence of emulsion characteristics.     

Comparing effects of α‐ vs. β‐chitosan coating and emulsion coatings on egg quality during room temperature storage

Effects of α‐ and β‐chitosan (CH), soybean oil (SO) and their emulsions (CH:SO = 2:3) as coating materials on selected internal quality and sensory properties of eggs were evaluated during 5 weeks storage at 25 °C. After 3 weeks of storage, α‐ and β‐CH‐coated eggs changed to B grade, while SO‐ and emulsion‐coated eggs preserved grade A quality. Weight loss of eggs coated with SO and CH:SO emulsions was <2.0% vs. 5.3–5.8% for noncoated and CH‐coated eggs after 5 weeks of storage. β‐CH (0.9%) maintained lower weight loss of eggs than α‐CH (1.2%) only at 1‐week storage. Albumen pH of eggs coated with SO and CH:SO emulsions decreased progressively throughout storage. Eggs coated with β‐CH:SO emulsion and SO were significantly glossier than noncoated eggs. Consumers indicated positive purchase intent (69.17–76.67%) for all coated eggs. Overall, α‐CH:SO and β‐CH:SO emulsions extended egg shelf life by at least 3 weeks during room temperature storage.     

Stability of protein‐stabilised β‐carotene nanodispersions against heating,salts and pH

BACKGROUND: Milk proteins are used in a wide range of formulated food emulsions. The stability of food emulsions depends on their ingredients and processing conditions. In this work, β‐carotene nanodispersions were prepared with selected milk‐protein products using solvent‐displacement method. The objective of this work was to evaluate the stability of these nanodispersions against heating, salts and pH. RESULTS: Sodium caseinate (SC)‐stabilised nanodispersions possessed the smallest mean particle size of 17 nm, while those prepared with whey‐protein products resulted in larger mean particle sizes (45–127 nm). Formation of large particles (mean particle size of 300 nm) started after 1 h of heating at 60 °C in nanodispersions prepared with SC. More drastic particle size changes were observed in nanodispersions prepared with whey protein concentrate and whey protein isolate. The SC‐stabilised nanodispersions were fairly stable against Na⁺ ions at concentrations below 100 mmol L^?1, but drastic aggregation occurred in ≥ 50 mmol L^?1 CaCl₂ solutions. Aggregation was also observed in whey protein‐stabilised nanodispersions after the addition of NaCl and CaCl₂ solutions. All sample exhibited the smallest mean particle size at neutral pH, but large aggregates were formed at both ends of extreme pH and at pH around the isoelectric point of the proteins. CONCLUSION: The nanodispersions prepared with SC were generally more stable against thermal processing, ionic strength and pH, compared to those prepared with whey proteins. The stable β‐carotene nanodispersions showed a good potential for industrial applications. Copyright © 2008 Society of Chemical Industry     

Physicochemical stability of egg protein‐stabilised oil‐in‐water emulsions supplemented with vegetable powders

The effect of vegetable powders on the physicochemical stability of egg protein‐stabilised oil‐in‐water emulsions was studied. Vegetable powders (beetroot, broccoli, carrot, celery, green pea, red pepper, spinach, swede, tomato and yellow pea) were added at 2.5% (w/v) to emulsions prepared with rapeseed oil. The physical stability of the emulsions was characterised using the emulsifying activity (EAI) and the emulsifying stability indices (ESI) in addition to bright field microscopy. The oxidative stability of the emulsions was monitored by means of an accelerated oxidation test (Rancimat method). The addition of most vegetable powders did not markedly affect the physical stability of the emulsions although an adverse effect of tomato was observed. The oxidative stability of the emulsions was significantly improved in most cases as indicated by the Rancimat method with broccoli exhibiting the highest increase in induction time (98.2%) compared with the control. Both polar and nonpolar antioxidants are likely to contribute to the overall chemical stability of this complex food system in a concentration‐dependent manner.     

Emulsifying properties of proteins extracted from Australian canola meal

Canola protein albumin fraction, globulin fraction, and canola protein isolate (CPI) were compared to commercial soy protein isolate (SPI) in terms of their emulsifying properties at various pH values. The globulin fraction had higher emulsifying capacity (EC), higher emulsifying activity index (EAI), and the droplet size of emulsions it stabilized was consistently smaller irrespective of pH compared to albumin fraction or CPI. In comparison to SPI, globulin fractions also had higher EC at all pH values tested, higher EAI at acidic pH, and smaller or comparable average emulsion droplet size at both pH 4 and 7. The stability of canola protein based emulsions were comparable to those of SPI based emulsions at most pH values (except the emulsion stabilized by the CPI at pH 4), with no significant (p > 0.05) changes in droplet size during storage for up to 7 days at room temperature. These emulsions, however, experienced separation into the emulsion and serum phases after 24 h storage at room temperature with the exception of CPI- and SPI-stabilized emulsions at pH 9. This study demonstrates the comparable emulsifying properties (forming or stabilizing) of some canola proteins to commercially available SPI, suggesting the potential use of canola proteins in food applications.     

Interaction between Emulsion Droplets and Escherichia coli Cells

ABSTRACT Oil‐in‐water emulsions (20% n‐hexadecane, v/v) were stabilized by dodecyltrimethylammonium bromide (DTAB), Tween 20, or sodium dodecyl sulfate (SDS). Particle size distribution and creaming stability were measured before and after adding Escherichia coli cells to emulsions. Both E. coli strains promoted droplet flocculation, coalescence, and creaming in DTAB emulsions, although JM109 cells (surface charge = ‐35 mV) caused faster creaming than E21 cells (surface charge = ‐5 mV). Addition of bacterial cells to SDS emulsions promoted some flocculation and coalescence, but creaming stability was unaffected. Droplet aggregation and accelerated creaming were not observed in emulsions prepared with Tween 20. Surface charges of bacterial cells and emulsion droplets played a key role in emulsion stability.     

Emulsifying and foaming properties of protein isolates prepared from heated milks

Surface activities at the air-water interface and the emulsifying and foaming properties of sodium caseinate, conventional casein-whey protein co-precipitate prepared from milk heated at 90°C × 15 min at pH 6.6 and milk protein isolates prepared from milks heated at 90°C × 15 min at pH 7.5 or at 60°C × 3 min at pH 10.0 were determined. The surface activities of the four proteins at the air-water interface were similar, while the emulsifying capacity and emulsion stabilizing ability of casein was less than that of the milk protein isolates or the conventional co-precipitate. Fat surface areas formed on emulsification with the four proteins were similar and increased with increasing power input. Total protein adsorbed at the interface and protein load (mg protein/m₂ fat) for the emulsions stabilized by sodium caseinate and the milk protein isolate prepared from the milk heated at 90°C × 15 min at pH 7.5 were similar and lower than those for emulsions stabilized by the other two proteins. Foam overruns followed the order: sodium caseinate > milk protein isolate prepared from milk heatedat90°C × 15min, pH 7.5 > milk protein isolate prepared from milk heated at 60°C × 3 min, pH 10.0 > conventional co-precipitate, while foam stabilities followed the reverse order.     

Immunodetection of legume proteins resistant to small intestinal digestion in weaned piglets

Experiments were conducted to investigate the biochemistry of digestion of the major storage proteins from soya bean, pea, faba bean, blue lupin, and chickpea seeds in the ileum of piglets. Hyperimmune plasmas against the crude protein extracts and the purified 11S and 7S globulin fractions of each legume seed and an anti‐pea albumin PA2 and lectin antibody were used. They served to probe immunoblots of feed protein extracts and ileal digesta samples. Globally, the recognition by plasmas of intact or partially digested proteins in ileal digesta was rather faint, in agreement with the fairly high in vivo digestibility data obtained with these legume seed proteins. Nevertheless, immunoreactive polypeptides found in digesta of piglets fed pea, faba bean and chickpea belonged mainly to proteins of the 7S family, and to other proteins including low‐molecular weight components such as PA2 albumin and lectin in the case of pea. In piglets fed lupin, nearly intact polypeptides from the 11S family were detected. To conclude, the present immunochemical study conducted on ileal digesta of piglets revealed a few dietary legume proteins of the vicilin and albumin families. Legumin proteins were demonstrated unequivocally in the case of lupin and white chickpea. Copyright © 2003 Society of Chemical Industry     

Formation of oil‐in‐water (O/W) pickering emulsions via complexation between β‐cyclodextrin and selected organic solvents

Cyclodextrins (CDs) are cyclic oligosaccharides derived from the enzymatic degradation of starch. Emulsifying functionality of β‐cyclodextrin (β‐CD) upon its complexation with selected solvents (octanol, decane, and toluene) was studied. In several tests, the three‐phase systems containing the emulsion fraction in the middle position were obtained. The examination of variations in the phase behavior of the test systems showed that the decane/β‐CD/water system had the highest emulsion phase volume when β‐CD at concentration of 10% w/v was used. A reduction in interfacial tension (IFT) of the oil–water interface in each test system was observed with the following order: toluene, decane, and octanol. The precipitated fraction obtained upon centrifugation of the emulsion phase, was structurally characterized as the inclusion complex (IC) formed between β‐CD and each of the three test solvents. The wettability of the IC particles was determined through contact angle measurement and formation of the oil‐in‐water (O/W) Pickering emulsions was confirmed (θ_ow<90°). With use of size distribution data, the ICs particles as the microparticles (1–10 µm) were found to be the main species involved in the formation and stabilization of the emulsions.     

Emulsifying properties of canola and flaxseed protein isolates produced by isoelectric precipitation and salt extraction

The emulsifying (emulsion capacity, EC; emulsion activity/stability indices, EAI–ESI and creaming stability, CS) and physicochemical properties (surface charge/hydrophobicity, protein solubility, interfacial tension, and droplet size) of chickpea (ChPI), faba bean (FbPI), lentil (LPI), and pea (PPI) protein isolates produced by isoelectric precipitation and salt extraction were investigated relative to each other and a soy protein isolate (SPI). Both the legume source and method of isolate production showed significant effects on the emulsifying and physicochemical properties of the proteins tested. All legume proteins carried a net negative charge at neutral pH, and had surface hydrophobicity values ranging between 53.0 and 84.8 (H₀-ANS), with PPI showing the highest value. Isoelectric precipitation resulted in isolates with higher surface charge and solubility compared to those produced via salt extraction. The EC values ranged between 476 and 542 g oil/g protein with LPI showing the highest capacity. Isoelectric-precipitated ChPI and LPI had relatively high surface charges (~−22.3 mV) and formed emulsions with smaller droplet sizes (~ 1.6 μm), they also displayed high EAI (~ 46.2 m²/g), ESI (~ 84.9 min) and CS (98.6%) results, which were comparable to the SPI.     

Pea (<Emphasis Type="Italic">Pisum sativum,L.</Emphasis>) Protein Isolate Stabilized Emulsions: A Novel System for Microencapsulation of Lipophilic Ingredients by Spray Drying

Oil-in-water emulsions can be considered as an important delivery system for lipophilic food molecules. In this study, pea protein isolate (PPI) was studied for its emulsifying capacity at various pH values and pH 7 was selected to prepare emulsions for the production of dry microcapsules. Emulsions stabilized by PPI just enough to cover oil droplets were mixed with solutions of starch hydrolysates of various dextrose equivalent (DE) and subsequently spray dried to yield powders with 30 wt% oil. Effects of DE (6, 12, 19, and 28) on feed emulsion properties and on the characteristics of the spray-dried powders were examined. Reconstituted emulsion oil droplet size and stability were affected by DE in all cases. Microencapsulation efficiency of dried emulsions increased significantly with increasing DE. The scanning electron microscope results showed that lower maltodextrins DE microcapsules are shallow and presented rough surfaces or invaginations. However, higher carbohydrates DE microcapsules were circular and uniform showing minimum cracks and dents on the surface confirming these DE to be efficient encapsulating materials. The formation of the drying matrix seems control the destabilization of pea protein-coated oil droplets during spray drying. In systems where the matrix is formed in a uniform manner, the interfacial protein film is less affected by the drying process. Thus the functionalities of pea protein can be protected during drying by using high DE carbohydrates.     

Improvement of emulsifying properties of milk proteins with κ or λ carrageenan: effect of pH and ionic strength

The objective of this work was to determine the effect of λ‐carrageenan or κ‐carrageenan on the emulsion capacity, emulsion work and emulsion stability of milk proteins concentrate (MP) or sodium caseinate (SC) emulsions at different levels of pH and ionic strength. Incorporation of carrageenans to proteins emulsions resulted in an improvement of emulsifying properties at pH 6.0 and low ionic strength (0.2 m NaCl). Although emulsion capacity was high in MP than for SC, irrespectively of carrageenan employed, addition of λ‐carrageenan increased twofold emulsion work values (15 327 Ω s^?1 for MP and 11 455 Ω s^?1 for SC; around 6000 Ω s^?1 in the other treatments). Emulsion stability was high with λ‐carrageenan (9.8 s) than MP‐κ‐carrageenan or MP (7.45 and 7.40 s, respectively). Carrageenan improving of emulsion properties was because of the complex formation with MP, characteristic of this type of food system when pH was above of isoelectric point.     

Interactions between Whey Protein Isolate and Soy Protein Fractions at Oil–Water Interfaces: Effects of Heat and Concentration of Protein in the Aqueous Phase

ABSTRACT:  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.     

Comparison of emulsifying properties of milk fat globule membrane materials isolated from different dairy by-products

Emulsifying properties of milk fat globule membrane (MFGM) materials isolated from reconstituted buttermilk (BM; i.e., BM-MFGM) and BM whey (i.e., whey-MFGM), individually or in mixtures with BM powder (BMP) were compared with those of a commercial dairy ingredient (Lacprodan PL-20; Arla Foods Ingredients Group P/S, Viby, Denmark), a material rich in milk polar lipids and proteins. The particle size distribution, viscosity, interfacial protein, and polar lipids load of oil-in-water emulsions prepared using soybean oil were examined. Pronounced droplet aggregation was observed with emulsions stabilized with whey-MFGM or with a mixture of whey-MFGM and BMP. No aggregation was observed for emulsions stabilized with BM-MFGM, Lacprodan PL-20, or a mixture of BM-MFGM and BMP. The surface protein load and polar lipids load were lowest in emulsions with BM-MFGM. The highest protein load and polar lipids load were observed for emulsions made with a mixture of whey-MFGM and BMP. The differences in composition of MFGM materials, such as in whey proteins, caseins, MFGM-specific proteins, polar lipids, minerals, and especially their possible interactions determine their emulsifying properties.     

The Emulsifying Properties of Commercial Milk Protein Products in Simple Oil-in-Water Emulsions and in a Model Food System

ABSTRACT: The emulsifying properties of six commercial milk protein products were studied. The products were separated into one of two groups depending on whether they contained aggregated (micellar) casein or disordered protein (casein or whey protein). Disordered proteins had a greater emulsifying ability than aggregated proteins. Dispersion of aggregated protein in dissociating buffer improved the emulsifying ability. Comparison of emulsion properties in simple oil-in-water emulsions with those in a model coffee whitener formulation showed that the lower emulsifying ability of aggregated protein could be partially compensated by other ingredients.     

Emulsifying and Foaming Properties of Different Protein Fractions Obtained from a Novel Lupin Variety AluProt‐CGNA® (Lupinus luteus)

The use of vegetable proteins as food ingredient is becoming increasingly important due to their high versatility and environmental acceptability. This work describes a chemical characterization and techno‐functional properties (emulsifying and foaming properties) of 3 protein fractions obtained from a protein‐rich novel lupin variety, AluProt‐CGNA^®. This nongenetically modified variety have a great protein content in dehulled seeds (60.6 g protein/100 g, dry matter), which is higher than soybean and other lupin varieties. A simple procedure was utilized to obtain 3 different fractions by using alkali solubilization and isoelectric precipitation. Fractions 1 and 3 were mainly composed of protein and polysaccharides (NNE), whereas fraction 2 was mainly composed by protein (97%, w/w). Fraction 3 presented interesting and potential foaming properties in comparison to the other fractions evaluated in the study. Besides, its solubility, foaming and emulsifying capacity were practically not affected by pH variations. The 3 fractions also presented good emulsion stability, reaching values above a 95%. SDS‐PAGE showed that fractions 1 and 2 contained mainly conglutin α, β, and δ, but in different ratios, whereas fraction 3 contained mainly conglutin γ and albumins. The results of this work will provide better understanding for the utilization of each protein fractions as potential ingredients in food industry.     

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.