Effect of high power ultrasonic treatment on whey protein foaming quality

High power ultrasonic energy at 20%, 40% and 60% amplitude was applied on whey protein suspension at concentrations of 100, 150 and 200 g kg^?1 for 5, 15 and 25 min to improve its foaming quality. Ultrasound‐treated whey protein suspension at 200 g kg^?1 showed improvement in terms of increased foaming capacity by 18%, foam stability by 35%, consistency index by 18%, storage modulus by 17%, loss modulus by 26% and viscosity by 21% compared with untreated whey protein. For maximally ultrasound‐treated samples of 60% amplitude treated for 25 min, the improved whey protein foams also had a 46% increase in the number of more evenly distributed fine bubbles which had a size smaller than 0.0025 mm³ as imaged using X‐ray microtomography.     

Effects of sucrose on egg white protein and whey protein isolate foams: Factors determining properties of wet and dry foams (cakes)

The effects of sucrose on the physical properties of foams (foam overrun and drainage ½ life), air/water interfaces (interfacial dilational elastic modulus and interfacial pressure) and angel food cakes (cake volume and cake structure) of egg white protein (EWP) and whey protein isolate (WPI) was investigated for solutions containing 10% (w/v) protein. Increasing sucrose concentration (0–63.6 g/100 mL) gradually increased solution viscosity and decreased foam overrun. Two negative linear relationships were established between foam overrun and solution viscosity on a log–log scale for EWP and WPI respectively; while the foam overrun of EWP decreased in a faster rate than WPI with increasing solution viscosity (altered by sucrose). Addition of sucrose enhanced the interfacial dilational elastic modulus (E′) of EWP but reduced E′ of WPI, possibly due to different interfacial pressures. The foam drainage ½ life was proportionally correlated to the bulk phase viscosity and the interfacial elasticity regardless of protein type, suggesting that the foam destabilization changes can be slowed by a viscous continuous phase and elastic interfaces. Incorporation of sucrose altered the volume of angel food cakes prepared from WPI foams but showed no improvement on the coarse structure. In conclusion, sucrose can modify bulk phase viscosity and interfacial rheology and therefore improve the stability of wet foams. However, the poor stability of whey proteins in the conversion from a wet to a dry foam (angel food cake) cannot be changed with addition of sucrose.     

Ultrasound‐induced changes in physical and functional properties of whey proteins

Use of high‐intensity ultrasound to modify certain functional properties of whey proteins is an alternative to traditional method in food industry. Whey protein isolate (WPI) solutions were treated with an ultrasound probe (20 kHz) at different intensities (20% or 30% amplitude) and durations (10 or 20 min). Results showed that ultrasound treatment changed physical and several functional properties of whey proteins including decreased particle size (from 190.4 nm to 138.0 nm), increased surface hydrophobicity (from 5.13 × 10⁵ to 5.77 × 10⁵), free sulphydryl groups (from 52.64 μmol SH g^?1 to 53.64–58.77 μmol SH g^?1), solubility (from 74.95% to 89.70%), emulsion activity index (from 3.18 m² g^?1 to 3.59–5.32 m² g^?1) and emulsion stability index (from 62.26 min to 71.44–104.83 min), and changed viscosity (from 5.51 mPa.s to 4.81–5.64 mPa.s). Therefore, we conclude that high‐intensity ultrasound can be potentially applied to whey proteins to improve its specific functions during food processing.     

Stability of oil–water primary emulsions stabilised with varying levels of casein and whey proteins affected by high-intensity ultrasound

This study evaluates physical and chemical stability of ultrasound-assisted grape seed oil primary emulsions stabilised by varying compositions of caseins to whey proteins (80:20, 60:40, 50:50 and 40:60) at different sono-operating conditions (81.9 and 117.0 J mL⁻¹). Physical and chemical stabilities were influenced by both sonication energy densities and milk protein compositions. Emulsions prepared at 81.9 J mL⁻¹ energy density with ≥40% whey protein fraction (60:40, 50:50, 40:60 and WPI) showed greater physical stability than the emulsions sonicated at 117.0 J mL⁻¹ which exhibited physical instability due to the depletion flocculation mechanism at the critical casein concentration (≥40%). The emulsion oxidative stability was found to be affected by sonication conditions as 117.0 J mL⁻¹ induced the oxidation reactions once the whey concentration exceeds 40%. Therefore, ultrasound prepared emulsions with casein to whey ratios of 60:40, 50:50, 40:60 and WPI at 81.9 J mL⁻¹ energy density was found to be stable for 10 days at 4 °C.     

Physical and oxidative stability of whey protein oil-in-water emulsions produced by conventional and ultra high-pressure homogenization: Effects of pressure and protein concentration on emulsion characteristics

Oil-in-water pre-emulsions (15% sunflower + 5% olive oils) obtained by colloid mill homogenization (CM) at 5000 rpm using whey protein isolate at different levels (1, 2 and 4%) were stabilized by ultra high-pressure homogenization (UHPH, 100 and 200 MPa) and by conventional homogenization (CH, 15 MPa). Emulsions were characterized for their physical properties (droplet size distribution, microstructure, surface protein concentration, emulsifying stability against creaming and coalescence, and viscosity) and oxidative stability (hydroperoxide content and thiobarbituric acid reactive substances, TBARs) under light (2000 lux/m² for 10 days). UHPH produced emulsions with lipid droplets of small size in the sub-micron range (100–200 nm) and low surface protein with unimodal distribution when produced at 4% whey proteins and 200 MPa. All emulsions exhibited Newtonian behavior (n ≈ 1). Long term physical stability against creaming and coalescence was observed in UHPH-emulsions, compared to those obtained by CM and CH. However, CH emulsions were highly stable against creaming (days) in comparison to the CM emulsions (hours). UHPH resulted in emulsions highly stable to oxidation compared to CM and CH treatments, especially when 100 MPa treatment was applied.Industrial relevanceIn the food, cosmetic and pharmaceutical sectors, industrial operators are currently interested in developing encapsulating systems to delivery bioactive compounds, which are generally hydrophobic, unstable and sensitive to light, temperature or/and oxygen. Ultra high-pressure homogenization is capable of producing stable submicron emulsions (< 1 μm) with a narrow size distribution, inducing more significant changes in the interfacial protein layer thus preventing droplet coalescence and also inhibit lipid oxidation. The present study suggests that emulsions produced by whey protein (4%) treated by ultra high-pressure homogenization have a good physical stability to flocculation, coalescence and creaming and also high stability to lipid oxidation, opening a wide range of opportunities in the formulation of emulsions containing bioactive components with lipid nature.     

Effect of ultrasound on the structure and functional properties of transglutaminase-crosslinked whey protein isolate exposed to prior heat treatment

Effects of ultrasound treatment (20 kHz, 41–45 W cm⁻², 0, 20, 40 or 60 min) on the physicochemical, functional properties and elements of the secondary structure of transglutaminase (TGase)-crosslinked whey protein isolate (WPI) exposed to prior thermal treatment (75 °C, 15 min) were investigated. The largest molecular size of proteins in the TGase-crosslinked WPI was observed after the ultrasound and thermal pre-treatment (HU-WPI-TGase). HU-WPI-TGase had the maximum intrinsic fluorescence intensity, with highest loss of free amino groups. Ultrasound-treated WPI (U-WPI) showed more (13%) emulsifying activity and more (63%) foaming ability than untreated WPI, but HU-WPI-TGase had higher foam stability and lower emulsifying activity than U-WPI. FTIR analysis indicated that ultrasound, heat treatment and TGase cross-linking had effects on the β-sheet, β-turn and random coil of WPI. The outcomes from this study show a potential application in providing novel functional ingredients for the dairy industry.     

Rheological,thermal and sensory properties of whey protein concentrate/pectin‐fortified mashed potatoes made from dehydrated flakes

The effect of different amounts of whey protein concentrate (50–150 g kg^?1), low and high methoxyl pectin (5–15 g kg^?1) on the rheological, thermal, structural properties and sensory quality of mashed potatoes prepared from dried mashed potatoes flakes was investigated. The response surface technique was used to analyse the effects of whey protein concentrate and pectin simultaneously on the consistency index, flow behaviour index, apparent viscosity and Casson plastic viscosity. Both whey protein concentrate and pectin decreased the consistency of the mashed potatoes weakening its structure in all concentrations assayed. Results suggest that whey protein concentrate interacts with high methoxyl pectin through non‐covalent interactions. Based on the sensory evaluation results, up to 100 g kg^?1 whey protein concentrate with 15 g kg^?1 of low methoxyl pectin and 15 g kg^?1 of high methxyl pectin could be incorporated to dried mashed potatoes flakes without losing significantly the sensory quality of the product.     

Effect of freezing on the viscoelastic behaviour of whey protein concentrate suspensions

The effect of freezing on viscoelastic behaviour of whey protein concentrate (WPC) suspensions was studied. Suspensions with total protein content of 5% and 9% w/v were prepared from a commercial WPC (unheated suspensions). A group of unheated suspensions was treated at two temperatures (72.5 and 77.5 °C) during selected times to obtain 60% of soluble protein aggregates (heat-treated suspensions). Unheated suspensions and heat-treated suspensions were frozen at −25 °C (frozen unheated and frozen heat-treated suspensions). Frequency sweeps (0.01–10 Hz) were performed in the region of linear viscoelasticity at 10, 20, 30, 40, and 50 °C. Mechanical spectra of all studied suspensions at 20 °C were similar to viscoelastic fluids and complex viscosity increased with the frequency (ω). Elastic (G′) and viscous (G″) moduli were modelled using power law equations (G′ = aω^x, G″ = bω^y), using fitted parameters a, x, b, and y for statistical analysis. Exponent y was the most influenced by freezing, indicating the existence of a higher degree of arrangement in frozen unheated suspensions and a lower degree of arrangement in frozen heat-treated suspensions. Only characteristic relaxation times (inverse of the crossover frequency) of suspensions with 5% w/v of total protein content were significantly influenced by freezing. Time–temperature superposition was satisfactory applied in unheated whey protein concentrate suspensions only in the range of high temperatures (30–50 °C). However, this principle failed over the complete temperature range in most of the frozen suspensions. It is possible that freezing produced an increase in the susceptibility to morphological changes with temperature during the rheological measurements.     

Synthesis of galactooligosaccharides using sweet and acid whey as a substrate

Two commercial available lactases from Aspergillus oryzae and Kluyveromyces lactis were used to study the synthesis of galactooligosaccharides (GOS) in sweet and acid whey. At 38 g L⁻¹ initial lactose concentration, the A. oryzae enzyme gave a GOS yield of 10.91 ± 0.01% in lactose solution, 10.93 ± 0.18% in sweet whey and 11.32 ± 0.59% in acid whey. Thus, the components in whey did not influence the enzymes transgalactolytic activity. On the other hand, the K. lactis enzyme showed a strong dependence on whey type and whey concentration. At 38 g L⁻¹ initial lactose concentration, GOS yields were 10.93 ± 0.26% in lactose solution, 4.30 ± 0.17% in sweet whey and 10.56 ± 0.41% in acid whey. However, with increasing initial lactose concentration, the inhibitory effect of sweet whey was decreasing, which resulted in even higher yields than in lactose solution.     

High hydrostatic pressure modification of whey protein concentrate for improved functional properties

Whey protein concentrate (WPC) has many applications in the food industry. Previous research demonstrated that treatment of whey proteins with high hydrostatic pressure (HHP) can enhance solubility and foaming properties of whey proteins. The objective of this study was to use HHP to improve functional properties of fresh WPC, compared with functional properties of reconstituted commercial whey protein concentrate 35 (WPC 35) powder. Fluid whey was ultrafiltered to concentrate proteins and reconstituted to equivalent total solids (8.23%) as reconstituted commercial WPC 35 powder. Solutions of WPC were treated with 300 and 400 MPa (0- and 15-min holding time) and 600 MPa (0-min holding time) pressure. After HHP, the solubility of the WPC was determined at both pH 4.6 and 7.0 using UDY and BioRad protein assay methods. Overrun and foam stability were determined after protein dispersions were whipped for 15 min. The protein solubility was greater at pH 7.0 than at pH 4.6, but there were no significant differences at different HHP treatment conditions. The maintenance of protein solubility after HHP indicates that HHP-treated WPC might be appropriate for applications to food systems. Untreated WPC exhibited the smallest overrun percentage, whereas the largest percentage for overrun and foam stability was obtained for WPC treated at 300 MPa for 15 min. Additionally, HHP-WPC treated at 300 MPa for 15 min acquired larger overrun than commercial WPC 35. The HHP treatment of 300 MPa for 0 min did not improve foam stability of WPC. However, WPC treated at 300 or 400 MPa for 15 min and 600 MPa for 0 min exhibited significantly greater foam stability than commercial WPC 35. The HHP treatment was beneficial to enhance overrun and foam stability of WPC, showing promise for ice cream and whipping cream applications.     

Influence of calcium-binding salts on heat stability and fouling of whey protein isolate dispersions

The effect of the calcium-binding salts (CBS), trisodium citrate (TSC), tripotassium citrate (TPC) and disodium hydrogen phosphate (DSHP) at concentrations of 1–45 mm on the heat stability and fouling of whey protein isolate (WPI) dispersions (3%, w/v, protein) was investigated. The WPI dispersions were assessed for heat stability in an oil bath at 95 °C for 30 min, viscosity changes during simulated high-temperature short-time (HTST) and fouling behaviour using a lab-scale fouling rig. Adding CBS at levels of 5–30 mm for TSC and TPC and 25–35 mm for DSHP improved thermal stability of WPI dispersions by decreasing the ionic calcium (Ca²⁺) concentration; however, lower or higher concentrations destabilised the systems on heating. Adding CBS improved heat transfer during thermal processing, and resulted in lower viscosity and fouling. This study demonstrates that adding CBS is an effective means of increasing WPI protein stability during HTST thermal processing.     

Influence of high intensity ultrasound on microbial reduction,physico-chemical characteristics and fermentation of sweet whey

The aim of this study was to investigate the influence of high intensity ultrasound on quality of reconstituted sweet whey in order to substitute thermal treatments i.e. pasteurization. Also, it was intended to study the influence of ultrasound on fermentation process of pasteurized or thermo-sonicated whey with respect to culture activation and sensory properties of the fermented whey. In the first stage, whey was subjected to treatments with different power inputs (480 W, 600 W) over 6.5, 8 and 10 min at constant temperature (45 °C, 55 °C). Treated whey samples were analyzed for microbiological quality, particle size distribution, protein content, acidity, electrical conductivity, viscosity and sensory properties. All of the analyzed parameters were compared with the control sample (pasteurized) and fresh whey. Subsequently, influence of high intensity ultrasound on pasteurized or thermo-sonicated whey fermentation with yoghurt culture and with monoculture Lactobacillus acidophilus La-5 was investigated. Ultrasound treatments were applied for culture activation prior to or after the inoculation. Whey thermo-sonication by nominal power of 480 W for 10 min at 55 °C resulted in better microbiological quality and sensory properties in comparison to whey pasteurization. Ultrasound treatments with nominal input power of 84 W over 150 s resulted in the highest increase of the viable count during the activation process. Whey fermentation by ultrasonicated culture La-5 lasted 30 min shorter and resulted in higher viable cells count.Industrial relevanceAttached paper (“Influence of high intensity ultrasound on microbial reduction, physico-chemical characteristics and fermentation of sweet whey”) reports the influence of high intensity ultrasound on quality and fermentation process of sweet whey. Also, the influence of high intensity ultrasound on pasteurized or thermo-sonicated whey fermentation with yoghurt culture and with monoculture Lactobacillus acidophilus La-5 was investigated.Whey proteins are thermo-labile proteins and degradable at higher temperatures (above 60 °C), and at conventional processing (pasteurization), denaturation and precipitation of proteins occur. Ultrasound gives a great replacement for pasteurization where precipitation does not occur. Also, ultrasonic treatment of the whey results in homogenization and thus, stability is increased. When microbiological cultures for fermentation, prior to the inoculation in the samples, are treated by ultrasound their activity is higher (explained in the paper) and thus fermentation is faster.From an economical point of view, processing by ultrasound can reduce costs a lot, since fermentation time is shorter, and the same effect as pasteurization is achieved. Ultrasonic treatment is a future in the dairy industry.     

Isolation and characterisation of κ-casein/whey protein particles from heated milk protein concentrate and role of κ-casein in whey protein aggregation

Milk protein concentrate (79% protein) reconstituted at 13.5% (w/v) protein was heated (90 °C, 25 min, pH 7.2) with or without added calcium chloride. After fractionation of the casein and whey protein aggregates by fast protein liquid chromatography, the heat stability (90 °C, up to 1 h) of the fractions (0.25%, w/v, protein) was assessed. The heat-induced aggregates were composed of whey protein and casein, in whey protein:casein ratios ranging from 1:0.5 to 1:9. The heat stability was positively correlated with the casein concentration in the samples. The samples containing the highest proportion of caseins were the most heat-stable, and close to 100% (w/w) of the aggregates were recovered post-heat treatment in the supernatant of such samples (centrifugation for 30 min at 10,000 × g). κ-Casein appeared to act as a chaperone controlling the aggregation of whey proteins, and this effect was stronger in the presence of α_S- and β-casein.     

Comparison between structural changes of heat-treated and transglutaminase cross-linked beta-lactoglobulin and their effects on foaming properties

The main whey protein, β-lactoglobulin, was enzymatically modified by transglutaminase and analyzed for structural and conformational changes and their impact in protein foaming properties: foamability and foam stability. Solutions containing 25 mg mL⁻¹ of β-lactoglobulin, 0.07 M cysteine in 20 mM sodium phosphate buffer pH 8.0 were incubated with transglutaminase, at a level of 1 U g⁻¹ substrate, for different periods of time: 30, 60, 120 and 180 min. Protein structural characterization was discussed based on electrophoresis, fluorescence and viscosity studies. Comparison between the effects on foaming properties of this enzymatic treatment with those produced by heating, assayed in a previous work, was made. While 3 min was pointed as the critical time in heating treatment, 60 min was identified as the corresponding crucial time for transglutaminase treatment. The most significant conformational change, the greatest amount of dimers and trimers, and approximately the same proportion among protein species were verified at these times. Foamabilities were similar regardless of the treatment, but foam stability for heated β-lactoglobulin, measured through the change in foam volume with time is ∼250% higher than the same property for the protein enzymatically treated. Heating produces a higher degree of unfolding and index of surface hydrophobicity; less compact and more asymmetrical structures, with higher flexibility, which implies a greater capacity of rearrangement in the interface, producing a stiffer viscoelastic film, which slows down disproportionation through mechanisms that involve resisting compression and reducing gas transport. This improved film can be responsible for the higher foam volume stability.     

Improved mapping of in-mouth creaminess of semi-solid dairy products by combining rheology,particle size,and tribology data

The effects of fat, protein, and casein to whey protein ratio on lubricating properties of stirred yogurt were determined and the relation of those to the sensory properties graininess, viscosity, and creaminess was assessed. Results demonstrated decreased friction effects with increasing fat and protein level, and decreasing proportion of whey protein. The predictive ability of in-mouth viscosity (r² = 0.91) and in-mouth creaminess (r² = 0.97) could be improved by combined assessments of rheological, particle size, and tribological characteristics. Graininess was not affected by friction data. To this end, the applicability of generated models has been tested. This study depicts a better understanding of the key drivers for creaminess and enables food manufacturers to develop fat-reduced dairy products without compromise on sensory properties.     

Gelation of single heated vs. double heated whey protein isolate

Gelation of single and double heated whey protein dispersions was investigated using Ca²⁺ as inducing agents. Whey protein isolate (WPI) dispersions (10% w/w) were single heated (30 min, 80 °C at pH 7.0) or double heated (30 min, 80 °C at pH 8.0 and 30 min, 80 °C at pH 7.0) and diluted to obtain the desired protein and/or calcium ions concentration (4–9% and 5–30 mm, respectively). Calcium ions were added directly or by using a dialysis method. Double-heated dispersions gelled faster at lower protein and calcium ion concentrations than single-heated dispersions. Gels obtained from double-heated dispersions had lower values of shear strain and shear stress at fracture than gels obtained from single-heated dispersions. Double heating caused a significant complex modulus (G*) increase at 4% WPI and 15 mm calcium ions in comparison with gels obtained from single-heated dispersion. Less significant differences between gels made from double and single-heated dispersions were observed at 6% WPI, however a higher value of complex modulus was obtained for 8% protein gels from the single-heated solution. Native and non-reduced SDS–PAGE did not show clearly the effect of different procedures of heating on the quantities of polymerised proteins. Proteins in double-heated dispersions had higher hydrophobicity. Increased calcium concentration caused decreased protein hydrophobicity for both single and double-heated solutions.     

Properties of set-style skim milk yoghurt as affected by an enzymatic or Maillard reaction induced milk protein oligomerisation

Protein oligomers (2.9 × 10⁴-3.0 × 10⁵ g/mol) were introduced into yoghurt in amounts of 15-37% of the total protein by an enzymatic modification of proteins in yoghurt milk by lactoperoxidase, laccase or glucose oxidase as well as by a dry matter increase of yoghurt milk with sodium caseinate/lactose, sodium caseinate/pectin and total milk protein/lactose Maillard products. Yoghurt from enzymatically treated milk was characterised by an up to 10% lower acidity, up to 47% diminished gel strength and up to 18% decreased whey drainage than yoghurt from untreated milk. Yoghurt from protein/saccharide Maillard product enriched milk exhibited up to 4% reduced acidity, up to 27% increased acetic aldehyde content as well as up to 58% decreased whey drainage in relation to yoghurt from untreated protein/saccharide mixture enriched milk. Sensorically, yoghurt from enzymatically treated milk as well as from protein/saccharide Maillard product enriched milk was described by an even and whey-draining appearance, by a soft, homogeneous and creamy consistency as well as by a mild, less yoghurt characteristic taste and smell.This study for the first time presents an overview over the impact of novel protein oligomerisation techniques on physicochemical and sensory properties of yoghurt in regard to possible practical applications of an enzymatic as well as Maillard reaction induced oligomerisation in complex food systems.     

The effect of protein concentration and heat treatment temperature on micellar casein–soy protein mixtures

The objective of this study was to investigate the effect of concentration and temperature on the rheological properties of soy proteins (SP) and micellar casein (MCN) systems. Individual and mixed (1:1) protein systems of 2–15% concentration were prepared and heat treated for 5 min at 40–90 °C. After cooling to 20 °C, their rheological properties were determined using steady-shear rheology. Zeta potential and particle size measurements were also conducted. Both proteins were negatively charged under all experimental conditions, but the absolute values of zeta potential and thus the stability of the protein solutions decreased with temperature and concentration. For SP solutions, viscosity and apparent yield stress increased with concentration. Shear thinning behavior was prevalent, becoming more pronounced with increasing concentration. Heat treatments at T ≥ 80 °C induced glycinin denaturation, followed by aggregation and network formation when C ≥ 7.5%. Heat treatment did not significantly affect viscosity of MCN systems, while increasing concentration resulted in a significant increase in apparent viscosity and apparent yield stress. Most MCN systems exhibited Newtonian flow behavior, with the exception of systems with C ≥ 12.5% treated at T ≥ 80 °C, which became slightly shear thickening. Mixed SP–MCN systems mimicked the behavior of SP, with most values of rheological parameters intermediate between SP and MCN-only systems. Mixtures of 7.5–12.5% concentration treated at 90 °C displayed local phase separation, low viscosity and apparent yield stress, while 15% mixtures treated at 90 °C showed protein aggregation and incipient network formation. The data generated in this study can be used to develop a range of protein based products with unique flow characteristics and storage stability.     

Characterisation of soluble aggregates from commercial whey protein concentrate suspensions: Effect of protein concentration,pH, and heat treatment conditions

Soluble aggregates obtained from heat‐treated suspensions of commercial whey protein concentrate with 74.4% w/w protein were characterised. The effect of protein concentration (7 and 8% w/w), pH (7.0, 7.5 and 8.0), and heating time (0, 5, 10, 15, 20 and 30 min) at 80 °C were evaluated. Whey protein concentrate suspensions with the highest protein concentration (8% w/w) and the lowest pH (pH 7.0) had the highest steady shear viscosity and absorbance values, indicating the effect of the soluble aggregate content (high concentration) and the aggregate size (at lower pH values). According to principal component analysis, samples with 8% w/w and pH 7.0 were grouped in a plot region that confirmed the behaviour observed by confocal microscopy. Those whey protein concentrate suspensions could have soluble aggregates with a strong probability of interacting with cations (in cold gelation applications such as microencapsulation) and with each other (in film‐formation during coating).     

Freezing Qualities of Raw Ovine Milk for Further Processing

Raw whole ovine (sheep) milk was frozen at −15°C and −27°C and microbiological and physico-chemical properties were evaluated periodically. Total bacteria decreased at a faster rate in milk stored at −15 than at −27°C. Acid degree values for milk stored at −15°C were significantly higher than that stored at _27°C. Samples stored at −15°C exhibited protein destabilization after 6 mo of storage, while those stored at −27°C were stable throughout the 12-mo storage period.Frozen ovine milk was evaluated in several products including cheese, yogurt, and whey protein concentrates. Products produced from milk frozen at −27°C exhibited good sensory and functional characteristics. Ovine whey showed a higher proportion of β-lactoglobulin, about the same proportion of α-lactalbumin and lower proportions of serum albumin and immunoglobulin than bovine whey. Ovine whey protein concentrate showed significantly better foam overrun, foam stability, and gel strength than bovine or caprine whey protein concentrates.