Effect of surface-active stabilizers on the surface properties of coconut milk emulsions

Previously we have demonstrated improved stability of coconut milk emulsions homogenized with various surface-active stabilizers, i.e., 1 wt% sodium caseinate, whey protein isolate (WPI), sodium dodecyl sulfate (SDS), or polyoxyethylene sorbitan monolaurate (Tween 20) [Tangsuphoom, N., & Coupland, J. N. (2008). Effect of surface-active stabilizers on the microstructure and stability of coconut milk emulsions. Food Hydrocolloids, 22(7), 1233–1242]. This study examines the changes in bulk and microstructural properties of those emulsions following thermal treatments normally used to preserve coconut milk products (i.e., −20 °C, −10 °C, 5 °C, 70 °C, 90 °C, and 120 °C). Calorimetric methods were used to determine the destabilization of emulsions and the denaturation of coconut and surface-active proteins. Homogenized coconut milk prepared without additives was destabilized by freeze–thaw, (−20 °C and −10 °C) but not by chilling (5 °C). Samples homogenized with proteins were not affected by low temperature treatments while those prepared with surfactants were stable to chilling but partially or fully coalesced following freeze–thaw. Homogenized coconut milk prepared without additives coalesced and flocculated after being heated at 90 °C or 120 °C for 1 h in due to the denaturation and subsequent aggregation of coconut proteins. Samples emulsified with caseinate were not affected by heat treatments while those prepared with WPI showed extensive coalescence and phase separation after being treated at 90 °C or 120 °C. Samples prepared with SDS were stable to heating but those prepared with Tween 20 completely destabilized by heating at 120 °C.     

Monitoring air/liquid partition of mastic gum oil volatiles in model alcoholic beverage emulsions: Effect of emulsion composition and oil droplet size

The purpose of this work was to study the impact of the structure and composition of hydroalcoholic emulsions on the air–liquid partition of aroma compounds of the essential oil of Pistacia lentiscus var. chia, commonly known as mastic gum oil (mainly consists of terpenes). Oil-in-water emulsions (φ = 0.17), containing 15% (v/v) ethanol, stabilized by three different emulsifiers (sodium caseinate, whey protein isolate and Tween 40), were prepared by using two different lipid phases (sunflower oil and anhydrous butter fat). The homogenization conditions were varied to obtain emulsions with different volume–surface mean diameters. The partition of the volatile compounds between air phase and emulsions at three different temperatures (25, 37 and 50 °C) was monitored by applying the Headspace Solid Phase Microextraction technique, followed by gas chromatography–mass spectrometry (GC–MS) analysis. In general, the results obtained showed that sodium caseinate was the most effective in retaining mastic aroma compounds, while WPI was the least effective. This could partly be explained by the different structure of the two proteins which, when adsorbed at the interface, form a membrane that acts as a barrier and influences the partition of the aroma compounds between the air and the liquid. At the same time interactions of aroma compounds with the two proteins in the bulk phase may also play a role. The retention of the aroma compounds depended on the oil droplet size only in the case of sodium caseinate containing emulsions at 37 and 50 °C. This behaviour could be due to the substantial increase in the thickness of the adsorbed casein layer when moving from a fine sized emulsion to one with a much larger size as well as to differences in the ratio of free to adsorbed emulsifier. The composition of the lipid phase also appeared to have a significant impact on the concentration of volatile compounds in the headspace of mastic gum oil containing emulsions stabilized by proteins. This was lower in the case of butter fat probably due to differences in composition with regard to fatty acid degree of saturation as well as to volatile absorption by the liquid lipid at 40 °C and subsequent entrapment in the semisolid fat at 25 °C.     

Freeze–thaw stability of lecithin and modified starch-based nanoemulsions

The impact of freeze–thaw cycles on the physical stability of oil-in-water emulsions containing lecithin – coated and modified starch – coated droplets has been studied by combined dynamic light scattering (DLS) and differential scanning calorimetry (DSC) measurements. Emulsions prepared by high-pressure homogenization were within 200 nm size ranges. Lecithin-based emulsion systems were unstable to freeze–thaw cycles, which was attributed to extensive droplet aggregation induced by the ice formation during emulsion freezing process. Instead, modified starch systems were highly stable due to the formation of a thick layer of emulsifier which prevented the coalescence of nanoemulsions. The addition of ice nucleating protein lowered the freeze–thaw stability of lecithin-based emulsions, but had negligible effect on modified starch-based emulsions. In contrast, the addition of poly(ethylene glycol) improved the stability of lecithin-based emulsions but destabilized the modified starch-based emulsion systems.     

Inhibition of lipid oxidation by encapsulation of emulsion droplets within hydrogel microspheres

The purpose of this study was to assess whether the oxidation of polyunsaturated lipids could be inhibited by encapsulating them within protein-rich hydrogel microspheres (size range 1-100 μm). Filled hydrogel microspheres were fabricated as follows: (i) high methoxy pectin, sodium caseinate, and casein-coated lipid droplets were mixed at pH 7, (ii) the mixture was acidified (pH 5), (iii) casein was cross-linked using transglutaminase, (iv) the pH was adjusted to pH 7. Samples were stored in the dark at 55 °C and were monitored for lipid hydroperoxide formation and headspace propanal. Oxidation of fish oil (1% vol/vol) in the microspheres was compared with that in oil-in-water emulsions stabilised by either sodium caseinate or Tween 20. Emulsions stabilised by Tween 20 oxidised faster than either microspheres or emulsions stabilised by casein, while microspheres and the casein stabilised emulsion showed similar oxidation rates. Results highlight the natural antioxidant properties of food proteins.     

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.     

Characterisation of binding of iron to sodium caseinate and whey protein isolate

The fortification of dairy products with iron is an important approach to delivering iron in required quantities to the consumer. The binding of iron (ferrous sulfate) to two commercial milk protein products, sodium caseinate and whey protein isolate (WPI), dissolved in 50 mM HEPES buffer, was examined as a function of pH and iron concentration. Sodium caseinate had more sites (n = 14) than WPI (n = 8) for binding iron, and the affinity of caseinate to bind iron was also higher than that of WPI. These differences were attributed to the presence of clusters of phosphoserine residues in casein molecules, which are known to bind divalent cations strongly. The amount of iron bound to sodium caseinate was found to be independent of pH in the range 5.5–7.0, whereas acidification (pH range 7.0–3.0) caused a marked decrease in the amount of iron bound to WPI.     

Impact of whey protein – Beet pectin conjugation on the physicochemical stability of β-carotene emulsions

The aim of the present study was to investigate the impact of whey protein isolate (WPI)-beet pectin conjugation on the physical and chemical properties of oil-in-water emulsions incorporating β-carotene within the oil droplets. Covalent coupling of WPI to beet pectin was achieved by dry heating of WPI-beet pectin mixtures of different weight ratios at 80, 90, 100 °C and 79% relative humidity for incubation times ranging from 1 to 9 h. It was confirmed by SDS-polyacrylamide gel electrophoresis that WPI covalently linked to beet pectin. The physical and chemical stability of β-carotene emulsions was characterized by droplet size and distribution, transmission profiles using novel centrifugal sedimentation technique, microstructure and β-carotene degradation during the storage. Compared with those stabilized by WPI alone and unheated WPI-beet pectin mixtures, β-carotene emulsions stabilized by WPI-beet pectin conjugates had much smaller droplet sizes, more homogenous droplet size distribution, less change in centrifugal transmission profiles and obviously improved freeze–thaw stability, indicating a very substantial improvement in the physical stability. Rheological analysis exhibited that emulsions stabilized by WPI-beet pectin conjugates changed from a shear thinning to more like Newtonian liquid compared those with WPI alone and unheated WPI-beet pectin mixtures. Degradation of β-carotene in emulsion during storage was more obviously retarded by WPI-beet pectin conjugate than WPI and unheated WPI-beet pectin mixture, probably due to a thicker and denser interfacial layer in emulsion droplets. These results implied that protein–polysaccharide conjugates were able to improve the physical stability of β-carotene emulsion and inhibit the deterioration of β-carotene in oil-in-water emulsions.     

Preparation,characterisation and selected functional properties of sodium caseinate–maltodextrin conjugates

Sodium caseinate (NaCN)–maltodextrin (Md40 or Md100) conjugates were prepared by a Maillard-type reaction by dry heat treatment of mixtures of NaCN and Md at 60 °C and 79% relative humidity for 4 days. Minimal levels of coloured reaction products were formed during conjugate preparation. Conjugation resulted in a 35.6% and a 36.2% loss of available amino groups in the NaCN, and a 17.8% and a 25.7% loss of available reducing groups in Md40 and Md100, respectively. SDS–PAGE and gel permeation chromatography confirmed conjugation. When assessed in the pH range 2.0–8.0 at 20 °C and 50 °C, conjugates had improved solubility compared to NaCN, particularly around the isoelectric point of the protein. The emulsifying properties of NaCN–Md conjugates were assessed in oil-in-water (o/w) emulsions and in model cream liqueurs. The conjugate stabilised o/w emulsions and liqueurs showed improved stability when compared to NaCN stabilised o/w emulsions and liqueurs. These results indicate a potential for these NaCN–Md conjugates as speciality functional food ingredients.     

Interfacial and emulsifying properties of sucrose ester in coconut milk emulsions in comparison with Tween

In this study, sucrose esters were presented as a promising alternative to petrochemically synthesized Tweens for application in coconut milk emulsions. The interfacial and emulsifier properties of sucrose ester (SE), mainly sucrose monostearate, had been investigated in comparison with Tween 60 (TW), an ethoxylate surfactant. The interfacial tension measurement showed that SE had a slightly better ability to lower the interfacial tension at coconut oil–water interface. These surfactants (0.25 wt%) were applied in coconut milk emulsions with 5 wt% fat content. The effects of changes in pH, salt concentration, and temperature on emulsion stability were analyzed from visual appearance, optical micrograph, droplet charges, particle size distributions, and creaming index. Oil droplets in both SE and TW coconut milk emulsions extensively flocculated at pH 4, or around the pI of the coconut proteins. Salt addition induced flocculation in both emulsions. The pH and salt dependence indicated polyelectrolyte nature of proteins, suggesting that the proteins on the surface of oil droplets were not completely displaced by either added nonionic SE or TW. TW coconut milk emulsions appeared to be thermally unstable with some coalesced oil drops after heating and some oil layers separated on top after freeze thawing. The change in temperature had much lesser influence on stability of SE coconut milk emulsions and, especially, it was found that SE emulsions were remarkably stable after the freeze thawing.     

Sodium caseinate–maltodextrin conjugate hydrolysates: Preparation,characterisation and some functional properties

Hydrolysates of sodium caseinate (NaCN)–maltodextrin (Md40 or Md100) conjugates were prepared with a limited (<10%) and moderate (>10%) degree of hydrolysis. When assessed in the pH range 2.0–8.0, each conjugate hydrolysate had improved solubility compared to NaCN and their respective native unhydrolysed conjugate. Oil-in-water emulsions containing NaCN (1%, w/w, protein) and various combinations of conjugate hydrolysates (0.2%, w/w) and/or glycerol monostearate (0.07–0.3%, w/w, GMS) were prepared; emulsion storage stability (at 45 °C for up to 20 days) and heat stability (at 140 °C for up to 20 min) was determined by measuring changes in the mean size of fat globules in emulsions. NaCN plus conjugate hydrolysate-stabilised emulsions had improved storage stability compared to a NaCN stabilised emulsion. In general, NaCN plus conjugate hydrolysate-stabilised emulsions were less heat-stable than NaCN or NaCN plus GMS stabilised emulsions; however, emulsions stabilised by NaCN plus one of the conjugate hydrolysates (CH102) had improved heat stability in comparison to the NaCN stabilised emulsion. The results show that hydrolysates of NaCN–Md conjugates have potential for use as emulsification aids in emulsion-based food products.     

Comparative studies on the effect of the freeze–thawing process on the physicochemical properties and microstructures of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) muscle

The effects of different freeze–thaw cycles (0, 1, 3 and 5) on the physicochemical properties and microstructures of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) muscle were investigated. White shrimp had greater exudate loss and higher α-glucosidase (AG), as well as β-N-acetyl-glucosaminidase (NAG) activities, than did black tiger shrimp, especially when the number of freeze–thaw cycles increased (P < 0.05). The decreases in Ca²⁺-ATPase activity, sulfhydryl group content and protein solubility with concomitant increases in disulfide bond formation and surface hydrophobicity were more pronounced in white shrimp muscle, than in black tiger shrimp muscle, particularly after five cycles of freeze–thawing (P < 0.05). The shear force of both shrimps was decreased after five freeze–thaw cycles (P < 0.05). The microstructure study revealed that the muscle fibers were less attached, with the loss of Z-disks, after subjection to five freeze–thaw cycles. Therefore, the freeze–thawing process caused denaturation of proteins, cell disruption, as well as structural damage of muscle in both shrimps. White shrimp generally underwent physicochemical changes induced by the freeze–thawing process to a greater extent than did black tiger shrimp.     

Heat Stability of Oil-in-Water Emulsions Containing Milk Proteins: Effect of Ionic Strength and pH

Emulsions (20 wt% soybean oil; 2 wt% protein) made with caseinate at pH 7 and with whey protein isolate (WPI) at pH 7 and 3 were stable to heating at 90 and 121°C. WPI emulsions destabilized at pH values between 3.5 and 4.0. In the presence of KCI (12.5–200 mM), large particles were formed in WPI emulsions at pH 3 and the emulsions were viscous. At pH 7, moderate concentrations of KCI decreased the heat stability and gels were formed. KCI had less effect on WPI emulsions made at pH 3. Combining the emulsions with caseinate allowed some control of the heat-induced gelation.     

Rheology and microstructure of myofibrillar protein-plant lipid composite gels: Effect of emulsion droplet size and membrane type

Composite gels were prepared from 2% myofibrillar protein (MP) with 10% imbedded pre-emulsified plant oils (olive and peanut) of various particle sizes at 0.6 M NaCl, pH 6.2. Dynamic rheological testing upon temperature sweeping (20-70 °C at 2 °C/min) showed substantial increases in G′ (elastic modulus) of MP sols/gels with the addition of emulsions, and the G′ increases were inversely related to the emulsion droplet size. Furthermore, gels containing emulsified olive oil had a greater (P < 0.05) hardness than those containing emulsified peanut oil. Regardless of oil types, MP-coated oil droplets exhibited stronger reinforcement of MP gels than Tween 80-stablized oil droplets; the latter composite gels had considerable syneresis. Light microscopy with paraffin sectioning revealed a stable gel structure when filled with protein-coated oil droplets, compared to gels with Tween 80-treated emulsions that showed coalesced oil droplets. These results suggest that rheological characteristics, hardness, texture, and water-holding capacity of MP gels were influenced by type of oils, the nature of the interfacial membrane, and the size of emulsion droplets.     

Freeze-thaw stability of oil-in-water emulsions prepared with native and thermally-denatured soybean isolates

Freeze-thaw stability of oil-in-water emulsions prepared with native or thermally-denatured soy isolates (NSI and DSI, respectively) as the sole emulsifier and sunflower oil (? = 0.25) has been examined at various protein concentrations (0.5, 1.0 and 2.0% w/v), comparatively with sodium caseinate (SC). The freeze-thaw stability was assessed by measurements of particle size, oiling off and gravitational separation after isothermal storage at −20 °C for 24 h and further thawing. The oil phase remained in liquid state and the amount of ice formed was similar (>97%) whatever the sample type and protein concentration. At 0.5%, NSI and DSI emulsions where highly unstable, exhibiting a coagulated cream layer with appreciable oiling off (>25%), whereas those prepared with SC were more stable, due to their initial lower flocculation degree (FD %) and particle size. For all emulsions, the increase of protein concentration (0.5–2.0% w/v) improves the freeze-thaw stability as a consequence of a decrease of initial FD %. At 2.0%, where is enough protein to cover the interface, a lower coalescence stability of NSI emulsion respect to those prepared with NSI was observed after freeze-thawing. This result can be attributed to the high tendency to aggregation of native soy globulins at subzero temperatures. Notwithstanding this, unlike the SC emulsions, the formation of new flocs in soy isolates-stabilized emulsions during freeze-thawing cannot be totally controlled.     

Kinetic and thermodynamic study of thermal inactivation of the antimicrobial peptide P34 in milk

The knowledge on thermal inactivation of biopreservatives in a food matrix is essential to allow their proper utilisation in food industry, enabling the reduction of heating times and optimisation of heating temperatures. In this work, thermal inactivation of the antimicrobial peptide P34 in skimmed and fat milk was kinetically investigated within the temperature range of 90–120 °C. The inactivation kinetic follows a first-order reaction with k-values between 0.071 and 0.007 min⁻¹ in skimmed milk, and 0.1346 and 0.0119 min⁻¹ in fat milk. At high temperatures, peptide P34 was less resistant in fat milk, with a significant decrease in residual activity as compared with skimmed milk. At temperatures below 110 °C, the fat globules seem to have protective effect to the peptide P34. Results suggest that peptide P34 is heat stable in milk with activation energy of 90 kJ mol⁻¹ in skimmed milk and 136 kJ mol⁻¹ in fat milk.     

Real-time measurement of oxygen transport across an oil-water emulsion interface

A method for real-time, in situ measurement of oxygen transport across oil-in-water emulsion interface was developed. This method is based on reversible fluorescence quenching of tris ruthenium (II) bis (hexafluorophosphate) complex dye encapsulated in the oil phase of an emulsion upon interaction with oxygen. Oxygen transport across the oil-water interface for four different emulsions (whey protein isolate (WPI), sodium-dodecyl sulphate (SDS), cross-linked WPI and SDS-chitosan emulsions) was measured and effective diffusion coefficients were calculated. Results show that cross-linking of WPI did not alter the oxygen transport rate (p > 0.01), while addition of a chitosan layer to the SDS emulsion significantly reduced the oxygen transport rate (p < 0.01). An increase in temperature from 25 to 40 °C reduced the oxygen transport rate in WPI and cross-linked WPI emulsions (p < 0.01). Effective diffusion coefficient values for transport of oxygen based on fluorescence data were 0.14-1.15 × 10⁻¹² cm²/s for the tested emulsions. Regardless of relatively low effective diffusion coefficients, the selected emulsions exhibited poor barrier properties in limiting oxygen transport across an emulsion interface. In summary, this rapid method is sensitive to detect changes in rate of oxygen transport due to changes in temperature and chemical composition of emulsion interface. This method can be used to screen and evaluate the barrier properties of encapsulation matrices leading to rational design of encapsulated structures.     

Effect of different treatments for the destabilization of coconut milk emulsion

Coconut milk is an emulsion which is stabilized by naturally occurring proteins. The main objective of the present work is to explore different methods employing thermal, pH, chilling, enzyme treatments and combination of enzyme treatments followed by chilling and thawing for effective destabilization of the coconut milk emulsion. Stability of emulsion is evaluated by measuring the creaming index and observed for the changes in structure of oil droplets, using phase contrast microscope. Combination of treatments (enzyme treatment at 37 °C followed by chilling and thawing) of coconut milk emulsion has resulted in highest yield of 94.5%. Physico-chemical properties and fatty acid compositions are evaluated for coconut oil obtained by combination of treatments and compared with that of commercial coconut oil. It is found that the oil obtained by combination of treatments is low with respect to free fatty acids and peroxide value and high in lauric acid content.     

Protein-stabilized emulsions containing beta-carotene produced by premix membrane emulsification

Protein-stabilized O/W emulsions containing beta-carotene were produced by premix membrane emulsification (ME) using polymeric microfiltration membranes. Bovine serum albumin (BSA) and a whey protein concentrate (WPC) were used as protein emulsifiers while a nonionic small-molecule surfactant, Tween 20, was used both as a control and co-emulsifier. Membrane fouling caused by WPC reduced more significantly transmembrane flux than that by BSA. Mixtures of WPC or BSA with Tween 20 reduced protein membrane fouling and, simultaneously, decreased the mean droplet size. WPC/Tween 20 mixtures enable to produce emulsions with low polydispersion (span < 1) but with a significant membrane fouling while BSA/Tween 20 mixtures led to higher transmembrane fluxes although polydisperse emulsions (span = 7). During storage at 22 and 35 °C, the chemical degradation rate of emulsions with WPC/Tween 20 was slower than those with BSA/Tween 20 whereas Tween 20-stabilized emulsions led to the highest rate of beta-carotene reduction during storage at 35 °C.     

Heat-induced aggregation of whey proteins in the presence of κ-casein or sodium caseinate

Aggregates were formed by heating mixtures of whey protein isolate (WPI) and pure κ-casein or sodium caseinate at pH 7 and 0.1 M NaCl. The aggregates were characterized by static and dynamic light scattering and size exclusion chromatography. After extensive heat-treatment at 80 °C for 24 h, almost all whey proteins and κ-casein formed mixed aggregates, but a large proportion of the sodium caseinate did not aggregate. At a given WPI concentration the size of the aggregates decreased with increasing κ-casein or sodium caseinate concentration, but the overall self-similar structure of the aggregates was the same. The presence of κ-casein or caseinate therefore inhibited growth of the heat-induced whey protein aggregates. The results were discussed relative to the reported chaperone-like activity of casein molecules towards heat aggregation of globular proteins.