Small and large deformation rheology and microstructure of κ-carrageenan gels containing commercial milk protein products

The rheological behaviour of commercial milk protein/κ-carrageenan mixtures in aqueous solutions was studied at neutral pH. Four milk protein ingredients; skim milk powder, milk protein concentrate, sodium caseinate, and whey protein isolate were considered. As seen by confocal laser microscopy, mixtures of κ-carrageenan with skim milk powder, milk protein concentrate, and sodium caseinate showed phase separation, but no phase separation was observed in mixtures containing whey protein isolate. For κ-carrageenan concentrations up to 0.5 wt%, the viscosity of the mixtures at low shear rates increased markedly in the case of skim milk powder and milk protein concentrate addition, but did not change by the addition of sodium caseinate or whey protein isolate. For κ-carrageenan concentrations from 1 to 2.5 wt%, small and large deformation rheological measurements, performed on the milk protein/κ-carrageenan gels, showed that skim milk powder, milk protein concentrate or sodium caseinate markedly improved the strength of the resulting gels, but whey protein isolate had no effect on the gel stength.     

Rheological and structural properties of differently acidified and renneted milk gels

In this study we assessed the rheological and structural properties of differently acidified and renneted milk gels by controlling pH value and renneting extent. Skim milk were exactly renneted to 4 extents (20, 35, 55, and 74%) and then direct acidified to the desired pH (4.8, 5.0, 5.2, 5.5, 5.8, and 6.2), respectively. Rheological properties were assessed by dynamic rheological measurements, structural properties were studied by spontaneous whey separation and confocal laser scanning micrograph, and protein interactions were studied by dissociation test. Results showed that minimally renneted milk samples (20 and 35%) formed weak gels with low storage modulus, and the acidification range within which gels could form was narrow (pH ≤5.2). Highly renneted milk samples formed more gels with high storage modulus. The results of this study revealed that acidification determined the structural properties of highly renneted milk gels. As pH increased from 5.0 to 6.2, highly renneted milk gels had lower loss tangent, decreased spontaneous syneresis, and smaller pores. For both the low and high rennetings, divalent calcium bonds contributed less at low pH than at high pH. In conclusion, renneting increased the pH range suitable for gel formation; acidification determined the spontaneous syneresis and microstructure of highly renneted milk gels.     

Acid-induced gelation of whey protein polymers: effects of pH and calcium concentration during polymerization

Heating whey protein dispersions (90°C for 15 min) at low ionic strength and pH values far from isoelectric point (pH>6.5) induced the formation of soluble polymers. The effect of mineral environment during heating on the hydrodynamic characteristics and acid-induced gelation properties of polymers was studied. Whey protein dispersions (80 g/l) were denatured at different pH (6.5–8.5) and calcium concentrations (0–4 mm) according to a factorial design. At pH 6.5, the hydrodynamic radius of protein polymers increased with increasing calcium concentration, while the opposite trend was observed at pH 8.5. Intrinsic viscosity results suggested that heating conditions altered the shape of protein polymers. Whey protein polymers were acidified to pH 4.6 with glucono-δ-lactone and formed opaque particulate gels. The storage modulus and firmness of gels were both affected by conditions used to prepare protein polymers. As a general trend, polymers with high intrinsic viscosity produced stronger gels, suggesting a relationship between polymer shape and gel strength.Acid gelation properties of whey protein polymers makes them suitable ingredients for yoghurt applications. Using whey protein polymers to standardize protein content increased yoghurt viscosity to 813 Pa.s while using skim milk powder at same protein concentration increased yoghurt viscosity to 393 Pa.s. Water holding capacity of protein polymers in yoghurt was 19.8 ml/g compared to 7.2 ml/g for skim milk powder protein. Acid gelation properties of whey protein polymers are modulated by calcium concentration and heating pH and offers new alternatives to control the texture of fermented dairy products.     

RHEOLOGICAL PROPERTIES OF RENNET-INDUCED GELS DURING THE COAGULATION AND CUTTING PROCESS: IMPACT OF PROCESSING CONDITIONS

The effects of gelation temperature (GT), pH, milk solids nonfat (MSNF) content and aging time on the small and large deformation rheological properties of rennet‐induced skim milk gels were studied. Small amplitude oscillatory rheometry (SAOR) was used to study gel formation. A constant shear rate was applied to gels of various ages to try to simulate the cutting process used in cheese vats. Second‐order polynomial models successfully predicted (R² ≥ 0.83) the relationship between processing parameters and rheological properties of gels. The processing parameters – gelation pH, GT and MSNF – had a significant effect on the rheological properties of rennet‐induced gels. The type and the nature of bonds in these networks and the time scale of applied deformation affected the rheological properties of rennet gels. As time after rennet addition increased, storage modulus, loss modulus and yield stress values increased. This resulted from an increase in the number and strength of bonds with time. The yield strain decreased with time probably because of rearrangements in the network making the gel shorter/brittle in texture. When the impact of the time scale of the applied deformation was compared between the small (storage modulus as a function of frequency) and large (yield stress as a function of constant shear rate) deformation properties of rennet‐induced gels, similar power law exponents were obtained. This similarity presumably reflects the type and relaxation behavior of bonds in this casein network. These results identify the impact of several important processing variables on both the small and the large deformation rheological properties of rennet‐induced gels, which could be useful in identifying gelation properties that improve cheese yield.     

Effect of protein concentration, pH, lactose content and pasteurization on thermal gelation of acid caprine whey protein concentrates

The influence of pH (4.5-6.5), sodium chloride content (125-375 mM), calcium chloride content (10-30 mM), protein concentration (70-90 g/l) and lactose content on the gel hardness of goat whey protein concentrate (GWPC) in relation to the origin of the acid whey (raw or pasteurized milk) was studied using a factorial design. Gels were obtained after heat treatment (90 degrees C, 30 min). Gel hardness was measured using texture analyser. Only protein concentration and pH were found to have a statistically significant effect on the gel hardness. An increase in the protein concentration resulted in an increase in the gel hardness. GWPC containing 800g/kg protein formed gels with a hardness maximum at the pHi, whereas GWPC containing 300 g/kg protein did not form true gels. Whey from pasteurized milk formed softer gels than whey from raw milk. A high lactose content (approximately 360 g/kg) also reduced the gelation performance of GWPC.     

Comparison of micellar casein isolate and nonfat dry milk for use in the production of high-protein cultured milk products

High protein levels in yogurt, as well as the presence of denatured whey proteins in the milk, lead to the development of firm gels that can make it difficult to formulate a fluid beverage. We wanted to prepare high-protein yogurts and explore the effects of using micellar casein isolate (MCI), which was significantly depleted in whey protein by microfiltration. Little is known about the use of whey protein-depleted milk protein powders for high-protein yogurt products. Microfiltration also depletes soluble ions, in addition to whey proteins, and so alterations to the ionic strength of rehydrated MCI dispersions were also explored, to understand their effects on a high-protein yogurt gel system. Yogurts were prepared at 8% protein (wt/wt) from MCI or nonfat dry milk (NDM). The NDM was dispersed in water, and MCI powders were dispersed in water (with either low levels of added lactose to allow fermentation to achieve the target pH, or a high level to match the lactose content of the NDM sample) or in ultrafiltered (UF) milk permeate to align its ionic strength with that of the NDM dispersion. Dispersions were then heated at 85°C for 30 min while stirring, cooled to 40°C in an ice bath, and fermented with yogurt cultures to a final pH of 4.3. The stiffness of set-style yogurt gels, as determined by the storage modulus, was lowest in whey protein-depleted milk (i.e., MCI) prepared with a high ionic strength (UF permeate). Confocal laser scanning microscopy and permeability measurements revealed no large differences in the gel microstructure of MCI samples prepared in various dispersants. Stirred yogurt made from MCI that was prepared with low ionic strength showed slow rates of elastic bond reformation after stirring, as well as slower increases in cluster particle size throughout the ambient storage period. Both the presence of denatured whey proteins and the ionic strength of milk dispersions significantly affected the properties of set and stirred-style yogurt gels. Results from this study showed that the ionic strength of the heated milk dispersion before fermentation had a large influence on the gelation pH and strength of acid milk gels, but only when prepared at high (8%) protein levels. Results also showed that depleting milk of whey proteins before fermentation led to the development of weak yogurt gels, which were slow to rebody and may be better suited for preparing cultured milk beverages where low viscosities are desirable.     

Microstructure of acid–induced skim milk–locust bean gum–xanthan gels

The microstructure of acid skim milk gels (14% w/w milk protein low heat powder) with or without addition of locust bean gum (LBG), xanthan gum (XG) and LBG/XG blends was determined by transmission electron microscopy (TEM), phase-contrast light microscopy (PCLM) and scanning electron microscopy (SEM). Three polysaccharide concentrations (0.001%, 0.02% and 0.1%, w/w) were used for binary mixtures. In the case of ternary mixtures, three LBG/XG weight ratios were used (4/16, 11/9 and 16/4) at 0.02% total polysaccharide concentration. Control acid skim milk gels were structured by a homogeneous network of casein particles (0.1–0.7 μm in diameter) and clusters immobilizing whey in small pores (1–5 μm in diameter). Filamentous structures and small aggregates were observed at the surface of casein particles. Low concentration of LBG or XG (0.001% w/w) did not affect markedly the microstructure of acid skim milk gels. Conversely, LBG or XG at 0.02 or 0.1% concentration and LBG/XG blends at the three ratios selected had a great influence on the gel microstructure. Although the size and surface structure of the casein particles were not modified by the presence of polysaccharides, the primary casein network appeared very compact with a decrease of pore size and a large increase in the porosity of the network at the supramolecular level (sponge-like morphology). The effect is stronger for gels containing LBG and XG used at higher concentration and less apparent for gels containing LBG/XG blends. Skim milk/XG gels were highly organized into fibrous structures whereas skim milk/LBG gels were more heterogeneous. These structures were discussed in the light of volume-exclusion effects (demixing) and specific interactions between casein micelles and polysaccharides. At the three weight ratios, skim milk/LBG/XG gels displayed both jagged “coral-like”, “veil-like” and filamentous structures. These structures could originate from a secondary network constituted by the known LBG/XG synergistic interactions.     

Rheological properties of milk gels formed by a combination of rennet and glucono-delta-lactone

The effects of heat treatment of milk, and a range of rennet and glucono-delta-lactone (GDL) concentrations on the rheological properties, at small and large deformation, of milk gels were investigated. Gels were made from reconstituted skim milk at 30 degrees C, with two levels each of rennet and GDL. Together with controls this gave a total of sixteen gelation conditions, eight for unheated and eight for heated milk. Acid gels made from unheated milks had low storage moduli (G') of < 20 Pa. Heating milks at 80 degrees C for 30 min resulted in a large increase in the G' value of acid gels. Rennet-induced gels made from unheated milk had G' values in the range approximately 80-190 Pa. However, heat treatment severely impaired rennet coagulation: no gel was formed at low rennet levels and only a very weak gel was formed at high levels. In gels made with a combination of rennet and GDL unusual rheological behaviour was observed. After gelation, G' initially increased rapidly but then remained steady or even decreased, and at long ageing times G' values increased moderately or remained low. The loss tangent (tan delta) of acid gels made from heated milk increased after gelation to attain a maximum at pH approximately 5.1 but no maximum was observed in gels made from unheated milk. Gels made by a combination of rennet and GDL also exhibited a maximum in tan delta, indicating increased relaxation behaviour of the protein-protein bonds. We suggest that this maximum in tan delta was caused by a loosening of the intermolecular forces in casein particles caused by solubilization of colloidal calcium phosphate. We also suggest that in combination gels made from unheated milk a low value for the fracture stress and a high tan delta during gelation indicated an increased susceptibility of the network to excessive large scale rearrangements. In contrast. combination gels made from heated milk formed firmer gels crosslinked by denatured whey proteins and underwent fewer large scale rearrangements.     

Rheological and structural characterization of gels from whey protein hydrolysates/locust bean gum mixed systems

The gelling ability of whey proteins can be changed by limited hydrolysis and by the addition of other components such as polysaccharides. In this work the effect of the concentration of locust bean gum (LBG) on the heat-set gelation of aqueous whey protein hydrolysates (10% w/w) from pepsin and trypsin was assessed at pH 7.0. Whey protein concentrate (WPC) mild hydrolysis (up to 2.5% in the case of pepsin and 1.0% in the case of trypsin) ameliorates the gelling ability. The WPC synergism with LBG is affected by the protein hydrolysis. For a WPC concentration of 10% (w/w), no maximum value was found in the G′ dependence on LBG content in the case of the hydrolysates, unlike the intact WPC. However, for higher protein concentrations, the behaviour of gels from whey proteins or whey protein hydrolysates towards the presence of LBG becomes very similar. In this case, a small amount of LBG in the presence of salt leads to a big enhancement in the gel strength. Further increases in the LBG concentration led to a decrease in the gel strength.     

Structure and rheology of the κ-carrageenan/locust bean gum gels

The structure and interaction of κ-carrageenan and locust bean gum (LBG) has been studied using rheology, cryo-SEM, conductivity and syneresis characterization. The rheological behaviour of the binary system has been characterized using both compression and shear measurements. Elimination of slip in the shear measurements yields G′ values of the order 10,000–30,000 Pa for a 1% κ-carrageenan gel in 0–0.2 M added KCl. These values are higher than previously reported. No synergistic peak was found with the addition of LBG as has been previously reported. The measured modulii for these gels yields a Poisson's ratio of 0.5. Compression rupture stress and strain were also monitored. The rupture measurements do show a synergistic peak indicating that the interaction does occur and is important at high strain amplitudes. The gel points as determined by conductivity for these systems show a decrease in temperature with increasing LBG concentration, which is consistent with rheological measurements. Syneresis results are reported for the range of κ-carrageenan/LBG ratios. The syneresis shown by the mixtures is the same as that shown by the same concentration of κ-carrageenan. Structures of the gels as determined by cryo-SEM are also reported. Characteristic length scales in these systems are of the order of tens of microns and show little change with LBG concentration. The reduction in the characteristic length scale with increasing LBG concentration is discussed in terms of the rheological behaviour.     

A novel technique for differentiation of proteins in the development of acid gel structure from control and heat treated milk using confocal scanning laser microscopy

The incorporation of caseins and whey proteins into acid gels produced from unheated and heat treated skimmed milk was studied by confocal scanning laser microscopy (CSLM) using fluorescent labelled proteins. Bovine casein micelles were labelled using Alexa Fluor 594, while whey proteins were labelled using Alexa Fluor 488. Samples of the labelled protein solutions were introduced into aliquots of pasteurised skim milk, and skim milk heated to 90 degrees C for 2 min and 95 degrees C for 8 min. The milk was acidified at 40 degrees C to a final pH of 4.4 using 20 g glucono-delta-lactone/l (GDL). The formation of gels was observed with CSLM at two wavelengths (488 nm and 594 nm), and also by visual and rheological methods. In the control milk, as pH decreased distinct casein aggregates appeared, and as further pH reduction occurred, the whey proteins could be seen to coat the casein aggregates. With the heated milks, the gel structure was formed of continuous strands consisting of both casein and whey protein. The formation of the gel network was correlated with an increase in the elastic modulus for all three treatments, in relation to the severity of heat treatment. This model system allows the separate observation of the caseins and whey proteins, and the study of the interactions between the two protein fractions during the formation of the acid gel structure, on a real-time basis. The system could therefore be a valuable tool in the study of structure formation in yoghurt and other dairy protein systems.     

Rheology of whey protein isolate-xanthan mixed solutions and gels. Effect of pH and xanthan concentration

Flow properties at pH 5.5-7.5 of whey protein isolate (WPI)-xanthan solutions containing 0-0.5 w/w% xanthan were studied by viscosimetry, although rigidity and fracture properties of the corresponding heat-set gels (90°C, 30 min) were determined by uniaxial compression. All the studied solutions displayed generalized shearthinning flow behaviour. Synergistic WPI-xanthan interactions has been revealed by observing that rheological parameters [σ_msf, K, n, η (γ)] characterizing blends were larger than those calculated from the two separated solutions. Such a behaviour was attributed to segregative phase separation of whey proteins and xanthan. Effects of xanthan on WPI-xanthan gel properties both depended on pH and xanthan concentration. Simultaneous increased xanthan concentration and decreased pH inhibited gelation of WPI-xanthan blends. Regarding gel strength, synergistic WPI-xanthan interactions were observed at pH >7.0 and low xanthan concentration (0.05 or 0.1 w/w%). Antagonism between the two macromolecules occurred at low xanthan concentration and pH ≤6.5, and high xanthan concentration (0.2 or 0.5 w/w%) at all pH tested. Low xanthan concentration rendered mixed gels more brittle than protein gels, and high xanthan concentration decreased pH effects on gel stress-strain relationships. The balance between strong thermal aggregation of concentrated whey proteins - in presence of incompatible xanthan -, high viscosity of blends and repulsive surface forces of protein molecules was thought to be at the origin of WPI-xanthan gel mechanical properties.     

The relationship between rheological parameters and whey separation in milk gels

The relation between whey separation of rennet-induced gels and rheological properties of those gels is reasonably well understood. A low fracture stress and a high value for the loss tangent at low frequencies have been correlated with a tendency to exhibit syneresis in rennet gels. In contrast, little is known about the relationship between mechanical properties of gels and whey separation in acid-induced milk gels, such as yoghurt, although this continues to be a major defect. In recent work, it has been found that conditions such as high milk heat treatment, fast rates of acidification and high incubation temperatures all gave high levels of whey separation compared with gels made from unheated milk that were incubated at low temperatures and where the rate of acidification was slow (i.e. when bacterial cultures were used instead of the acidogen, glucono-δ-lactone). The tendency to exhibit whey separation in acid gels made from heated milk was related to a low fracture strain and an increase in the loss tangent (observed even at high frequencies) during the gelation process (a high value indicates conditions favouring relaxation of bonds). Excessive rearrangements of particles in the gel network before and during gelation were implicated as being responsible for whey separation and rheological conditions that appeared to indicate this defect are described. It was also concluded that techniques that measure the spontaneous formation of surface whey should be distinguished from those that measure the expression of whey from networks under pressure as the latter tests only measure gel rigidity.     

Structure modification of stirred fermented milk gel due to laccase-catalysed protein crosslinking in a post-processing step

Laccases are a promising candidate for crosslinking milk proteins in stirred fermented milks. It was applied in a post-processing step due to its acidic pH optimum reported in literature for rebodying of the gel and an improvement in structure. A laccase preparation from Trametes versicolor had a lower oxidation activity in ultrafiltration permeate than in model buffer systems, and a pH optimum of 4.5. It was applied to stirred skim milk gels but no significant change in the storage modulus or apparent viscosity of yoghurt occurred. Confocal laser scanning micrographs showed a more porous structure of the milk gel. Some fresh cheese samples had improved rheological properties. A competing crosslinking activity and peptidolytic activity was assumed and smaller peptides were detected in acidified milk by fluorescence. Mass spectrometry of the laccase preparation returned mainly laccase sequences. Although this does not exclude proteases, it indicates that the radical mechanism of laccases may lead to protein degradation.Industrial RelevanceEnzymatic modification of milk proteins can alter the structure of fermented milk gels and even create new structures.Rheological properties can be improved via crosslinking, thus reducing costs due to the addition of protein powders or stabilisers.An innovative approach to combining biotechnology and food science and engineering is investigated.The study is interesting for both enzyme manufacturers and dairy companies as it aims to at least partially fill the knowledge gap between enzymology and their real-world application in dairy products.However, enzymatic treatment is an additional step and also incurs costs which should be taken into account.     

Gelation of Mixed Gels Containing κ-Carrageenan and Skim Milk Components

ABSTRACT: The gelation characteristics of mixed gels containing κ-carrageenan and skim milk or milk fractions (skim milk permeate or retentate) obtained by ultrafiltration were examined. Increasing the skim milk solids content of mixtures containing carrageenan increased setting temperatures and gel strength. The milk proteins contributed to gel strength but did not influence the setting temperature of mixtures. The binding of denatured whey proteins to casein micelles affected gel network formation of milk-carrageenan mixtures containing 10% milk solids. Network formation in mixed gels containing carrageenan and milk or milk fractions was initiated by the carrageenan component and dictated primarily by the ionic content of the mixtures.     

EFECT OF pH BUFFERS ON MECHANICAL PROPERTIES OF GELLAN GELS

The strength and deformability of calcium cross-linked gellan gels as affected by pH 3.5 and 5.0 citrate and acetate buffers were measured by large compressive deformation test until failure. The trend of dependence of gel strength on polymer and calcium concentrations was similar to gels formed in distilled water without pH adjustment. A critical calcium concentration was observed for each gellan concentration. Gels formed at the critical calcium concentration exhibited the maximum strength. The chelating effect of pH 5.0 citrate buffer greatly increased the critical calcium concentration. The failure strain, representing the deformability, of gellan gels formed in buffers behaved differently from gels formed in distilled water. In the pH 3.5 buffer systems, gellan gels were brittle regardless of gellan and calcium concentrations. In the pH 5.0 buffer systems, gellan gels were brittle at high calcium concentrations and ductile at calcium concentrations less than 24 mM in citric buffer and less than 6 mM in acetate buffer.     

GEL CHARACTERISTICS OF β-LACTOGLOBULIN, WHEY PROTEIN CONCENTRATE AND WHEY PROTEIN ISOLATE

The gelation characteristics of β-lactoglobulin, whey protein isolate and whey protein concentrate at varying levels of protein (6–11%), sodium chloride (25–400 mM), calcium chloride (10–40 mM) and pH (4.0–8.0) were studied in a multifactorial design. Small scale deformation of the gels was measured by dynamic rheology to give the gel point (°C), complex consistency index (k*), complex power law factor (n*) and critical strain (γ_c). The gel point decreased and turbidity increased with increasing calcium level. The denaturation temperature measured by differential scanning calorimetry was measured at higher pH values. Large scale deformation at 20% and 70% compression was measured using an Instron Universal Testing machine. The true protein level had the largest effect on the stress required to produce 20% and 70% compression and on the consistency (k*) of the gels.     

Mixtures of whey protein microgels and soluble aggregates as building blocks to control rheology and structure of acid induced cold-set gels

Whey proteins (WP) today offer an extremely high potential for innovative development of functional and nutritious food products. Acid cold-set gels present an interesting approach of gelation at low temperature upon acidification of preformed whey protein (WP) aggregates. In the present work, we aimed to demonstrate how structure and rheological properties of acid gels can be controlled by combining two types of WP aggregates with different structural and chemical properties. Whey protein microgels (WPM) and soluble aggregates (WPSA) were generated upon heating WP isolate in specific pH conditions and temperature, leading to Z-average hydrodynamic diameters close to 270 nm for WPM and 100 nm for WPSA. Mixtures of WPM and WPSA were prepared at different weight ratios ranging from 100% WPM to 100% WPSA. The total protein concentration was set to 4 or 8%wt. Acidification was performed at 40 °C by addition of 1%wt glucono-δ-lactone (GDL). Gelation was followed using turbidimetry and small deformation rheology as function of pH. Microstructures of the gel were investigated at different length scales using various microscopy techniques (CLSM, SEM, AFM). When the WPM/WPSA ratio decreased, the pH of gelation and the gel strength increased because of the different structure and chemical reactivity of the two types of WP aggregates. The final pH had a strong impact on the structure of the gels. When final pH decreased below pH 4.3, a structure change was suggested by turbidimetry measurements. This resulted in a non self-supporting gel or in a decrease of gel strength. For pH above 4.3, self supporting gel were obtained. The rheological properties of the gel could therefore be modulated depending on the properties of the building blocks used (WPM versus WPSA). Interestingly, the gel microstructures observed for WPM/WPSA mixtures or WPM were comparable to those of acidified skimmed milk gels ranging from coarse structures with clumps of aggregates or to homogeneous fine networks (WPSA only) that have been described for WP gels obtained upon direct heating at various pH.     

乳成分对酸奶凝胶微观结构和流变学性质的影响

酸奶凝胶的许多宏观的物理特性与其微观结构和流变学性质密切相关。从酸奶的微结构、流变学性质和质地等方面综述了乳脂肪、蛋白质及调节酪蛋白和乳清蛋白比例对酸奶凝胶的影响。     

Effect of increasing the colloidal calcium phosphate of milk on the texture and microstructure of yogurt

The effect of increasing the colloidal calcium phosphate (CCP) content on the physical, rheological, and microstructural properties of yogurt was investigated. The CCP content of heated (85°C for 30 min) milk was increased by increasing the pH by the addition of alkali (NaOH). Alkalized milk was dialyzed against pasteurized skim milk at approximately 4°C for 72 h to attempt to restore the original pH and soluble Ca content. By adjustment of the milk to pH values 7.45, 8.84, 10.06, and 10.73, the CCP content was increased to approximately 107, 116, 123, and 128%, respectively, relative to the concentration in heated milk. During fermentation of milk, the storage modulus (G′) and loss tangent values of yogurts were measured using dynamic oscillatory rheology. Large deformation rheological properties were also measured. The microstructure of yogurt was observed using fluorescence microscopy, and whey separation was determined. Acid-base titration was used to evaluate changes in the CCP content in milk. Total Ca and casein-bound Ca increased with an increase in the pH value of alkalization. During acidification, elevated buffering occurred in milk between pH values 6.7 to 5.2 with an increase in the pH of alkalization. When acidified milk was titrated with alkali, elevated buffering occurred in milk between pH values 5.6 to 6.4 with an increase in the pH of alkalization. The high residual pH of milk after dialysis could be responsible for the decreased contents of soluble Ca in these milks. The pH of gelation was higher in all dialyzed samples compared with the heated control milk, and the gelation pH was higher with an increase in CCP content. The sample with highest CCP content (128%) exhibited gelation at very high pH (6.3), which could be due to alkali-induced CN micellar disruption. The G′ values at pH 4.6 were similar in gels with CCP levels up to 116%; at higher CCP levels, the G′ values at pH 4.6 greatly decreased. Loss tangent values at pH 5.1 were similar in all samples except in gels with a CCP level of 128%. For dialyzed milk, the whey separation levels were similar in gels made from milk with up to 107% CCP but increased at higher CCP levels. Microstructure of yogurt gels made from milk with 100 to 107% CCP was similar but very large clusters were observed in gels made from milk with higher CCP levels. By dialyzing heated milk against pasteurized milk, we may have retained some heat-induced Ca phosphate on micelles that normally dissolves on cooling because, during dialysis, pasteurized milk provided soluble Ca ions to the heated milk system. Yogurt texture was significantly affected by increasing the casein-bound Ca (and total Ca) content of milk as well as by the alkalization procedure involved in that approach.