Casein glycomacropeptide pH-dependent self-assembly and cold gelation

The self-assembly of 3–5% (w/w) casein glycomacropeptide (CMP) at room temperature and pH 3–6.5 was determined by dynamic light scattering immediately after pH adjustment and over time, and the rate of gelation at a concentration of 3–10% (w/w) was determined by a tilting test. The intensity particle size distribution at pH 6.5 was multimodal with a predominant peak at 2.3 nm. The hydrodynamic diameter increased when decreasing the pH from 6.5 to 3. CMP solutions at a pH below 4.5 showed time-dependent self-assembly at room temperature, which led over time to gelation. The minimum concentration for cold gelation depended on pH. Below pH 4, CMP gelled even at low concentrations (3%, w/w). The pH-reversibility of self-assembled CMP was not total, showing that hydrophobically bound dimers, once formed, are stable to pH changes. A model to explain CMP self-assembly and the formation of a network-like structure (gel) at room temperature is proposed.     

Thermodynamic incompatibility between denatured whey protein and konjac glucomannan

The current study investigated the effect of a neutral polysaccharide, konjac glucomannan, on the heat-induced gelation of whey protein isolate (WPI) at pH 7. Oscillatory rheology (1 rad/s; 0.5% strain), differential scanning calorimetry and confocal laser scanning microscopy were used to investigate the effect of addition of konjac in the range 0-0.5% w/w, on the thermal gelation properties of WPI. The minimum gelling concentration for WPI samples was 11% w/w; the concentration was therefore held constant at this value. Gelation of WPI was induced by heating the samples from 20 to 80 °C, holding at 80 °C for 30 min, cooling to 20 °C, and holding at 20 °C for a further 30 min. On incorporation of increasing concentrations of konjac the gelation time decreased, while the storage modulus (G′) of the mixed gel systems increased to ∼1450 Pa for 11% w/w WPI containing 0.5% w/w konjac gels, compared to 15 Pa for 11% w/w WPI gels (no konjac). This increase in gel strength was attributed to segregative interactions between denatured whey proteins and konjac glucomannan.     

Effects of the concentration of insoluble calcium phosphate associated with casein micelles on the functionality of directly acidified cheese

Directly acidified cheeses with different insoluble Ca (INS Ca) contents were made to test the hypothesis that the removal of INS Ca from casein micelles (CM) would directly contribute to the softening and flow behavior of cheese at high temperature. Skim milk was directly acidified with dilute lactic acid to pH values of 6.0, 5.8, 5.6, or 5.4 to remove INS Ca (pH trial). Lowering milk pH also reduced protein charge repulsion, which could influence melt. In a second treatment, EDTA (0, 2, 4, or 6 mM) was added to skim milk that was subsequently acidified to pH 6.0 (EDTA trial). Both types of milks were then made into directly acidified cheese. Cheese properties were determined at approximately 10 h after pressing to reduce possible confounding effects of proteolysis. The INS Ca content was determined by the acid-base titration method. Dynamic low-amplitude oscillatory rheology was used to measure the viscoelastic properties of cheese during heating from 5 to 80°C. The composition of all cheeses was as similar as possible, with cheese-making procedures being modified to obtain similar moisture contents (∼55%). Insoluble Ca contents of cheeses significantly decreased with a reduction in pH or with the addition of EDTA to skim milk. The pH values of cheeses in the pH trial varied, but all cheeses in the EDTA trial had similar pH values (∼5.73). In the pH trial, the reduction in cheese pH and consequent decrease in INS Ca content resulted in a reduction in the G′ values of cheeses at 20°C. In contrast, the G′ values at 20°C in cheeses from the EDTA trial increased with EDTA addition up to 4 mM EDTA. The G′ values at 70°C of cheeses from the pH trial decreased with a decrease in cheese pH, and a similar decrease was observed in the G′ values of cheese from the EDTA trial with an increase in EDTA concentration even though these cheeses had a similar pH value. In both trials, loss tangent (LT) values increased with temperatures >30°C and reached a maximum at approximately 70°C. In the pH trial, LT values at 70°C increased from 1.50 to 4.24 with a decrease in cheese pH from 5.78 to 5.21. The LT values increased from 1.43 to 3.23 with an increase in the concentration of added EDTA from 0 to 6 mM. In the EDTA trial, the decrease in G′ and increase in LT values at 70°C were due to the reduction in INS Ca content, because the pH values of these cheeses were the same. It can be concluded that the loss of INS Ca increases the melting in cheeses that have the same pH and gross chemical composition, and removal of INS Ca can even make cheese at high pH (∼5.73) exhibit reasonable melt characteristics.     

Characterisation and thermo-reversible gelation of cod muscle protein isolates

Cod (Gadus Morhua) muscle proteins were solubilized using alkaline treatment of the muscle. Solutions of similar protein composition were obtained between pH 10.5 and 12.0, however, pH > 11 was required for optimal yield. Addition of salt (up to 0.25 M NaCl) did not affect protein yield or composition. Light scattering showed that a significant fraction of the proteins was present as large self similar and flexible aggregates. When the pH was decreased below 10, gelation was observed below a critical temperature of about 25 °C, which could be reversed by heating. Slow irreversible aggregation was also observed leading to coarsening and syneresis of the gels or precipitation at higher temperatures. The rate of irreversible aggregation increased with decreasing pH and was fast below pH 8. Homogeneous thermo-reversible self supporting gels that were stable for a period of days could be prepared without heating at a narrow pH range between 8.5 and 9.5.     

Modulation of thermal stability and heat-induced gelation of β-lactoglobulin by high glycerol and sorbitol levels

The influence of glycerol and sorbitol on the thermal stability and heat-induced gelation of β-lactoglobulin (β-lg) in aqueous solutions was investigated. The thermal stability of β-lg was characterized by measuring the thermal denaturation temperature (T_m) using differential scanning calorimetry, while its gelation properties were characterized by measuring the gelation temperature (T_gel) and final gel rigidity (G^∗) using dynamic shear rheology. All experiments were carried out using aqueous solutions containing 10% (w/w) β-lg, glycerol (0–70% w/w) or sorbitol (0–55% w/w), and 5 mM phosphate buffer (pH 7.0). No salt was added to these solutions so that there was a relatively strong electrostatic repulsion between the protein molecules, which usually prevents gelation. When the cosolvent concentration was increased from 0% to 50%, T_m increased from 74 to 86 °C for sorbitol, but only from 74 to 76 °C for glycerol, which indicated that sorbitol was much more effective at stabilizing the native state of the globular protein than glycerol. Protein solutions containing sorbitol (0–55%) did not form a gel after heating, but those containing glycerol formed gels when the cosolvent concentration exceeded about 10%, with G^∗ increasing with increasing glycerol concentration. We attribute these effects to differences in the preferential interactions of polyols and water with the surfaces of native and heat-denatured proteins, and their influence on the protein–protein collision frequency.     

The influence of acid type on self-assembly,rheological and textural properties of caseinomacropeptide

The influence of acid type (acetic, citric, lactic and hydrochloric acids) on caseinomacropeptide (CMP) self-assembly, rheological and textural properties was analysed. The acidulant selection had a large impact on self-assembly rate, gelation and the hardness of CMP gels. The highest self-assembly and gelation rates were for citric acid, followed by hydrochloric and lactic acids. CMP solutions did not gel when the pH was adjusted with acetic acid during the test period. Product development using CMP must be carefully designed from the point of view of gel properties. A product preparation with CMP gelled with lactic or acetic acids would not be recommended because these acids affect the rheological and textural properties of the gels.     

Effect of hydrostatic high-pressure processing on the chemical,functional, and rheological properties of starter-free Queso Fresco

Queso Fresco (QF), a popular high-moisture, high-pH Hispanic-style cheese sold in the United States, underwent high-pressure processing (HPP), which has the potential to improve the safety of cheese, to determine the effects of this process on quality traits of the cheese. Starter-free, rennet-set QF (manufactured from pasteurized, homogenized milk, milled before hooping, and not pressed) was cut into 4.5- × 4.5- × 15-cm blocks and double vacuum packaged. Phase 1 of the research examined the effects of hydrostatic HPP on the quality traits of fresh QF that had been warmed to a core temperature of 20 or 40°C; processed at 200, 400, or 600 MPa for 5, 10, or 20 min; and stored at 4°C for 6 to 8 d. Phase 2 examined the long-term effects of HPP on quality traits when QF was treated at 600 MPa for 3 or 10 min, and stored at 4 or 10°C for up to 12 wk. Warming the QF to 40°C before packaging and exposure to high pressure resulted in loss of free whey from the cheese into the package, lower moisture content, and harder cheese. In phase 2, the control QF, regardless of aging temperature, was significantly softer than HPP cheeses over the 12 wk of storage. Hardness, fracture stress, and fracture rigidity increased with length of exposure time and storage temperature, with minor changes in the other properties. Queso Fresco remained a bright white, weak-bodied cheese that crumbled and did not melt upon heating. Although high pressures or long processing times may be required for the elimination of pathogens, cheese producers must be aware that HPP altered the rheological properties of QF and caused wheying-off in cheeses not pressed before packaging.     

Influence of brine concentration and temperature on composition, microstructure, and yield of feta cheese

The protein matrix of cheese undergoes changes immediately following cheesemaking in response to salting and cooling. Normally, such changes are limited by the amount of water entrapped in the cheese at the time of block formation but for brined cheeses such as feta cheese brine acts as a reservoir of additional water. Our objective was to determine the extent to which the protein matrix of cheese expands or contracts as a function of salt concentration and temperature, and whether such changes are reversible. Blocks of feta cheese made with overnight fermentation at 20 and 31°C yielded cheese of pH 4.92 and pH 4.83 with 50.8 and 48.9 g/100 g of moisture, respectively. These cheeses were then cut into 100-g pieces and placed in plastic bags containing 100 g of whey brine solutions of 6.5, 8.0, and 9.5% salt, and stored at 3, 6, 10, and 22°C for 10 d. After brining, cheese and whey were reweighed, whey volume measured, and cheese salt, moisture, and pH determined. A second set of cheeses were similarly placed in brine (n = 9) and stored for 10 d at 3°C, followed by 10 d at 22°C, followed by 10 d at 3°C, or the complementary treatments starting at 22°C. Cheese weight and whey volume (n = 3) were measured at 10, 20, and 30 d of brining. Cheese structure was examined using laser scanning confocal microscopy. Brining temperature had the greatest influence on cheese composition (except for salt content), cheese weight, and cheese volume. Salt-in-moisture content of the cheeses approached expected levels based on brine concentration and ratio of brine to cheese (i.e., 4.6, 5.7 and 6.7%). Brining at 3°C increased cheese moisture, especially for cheese with an initial pH of 4.92, producing cheese with moisture up to 58 g/100 g. Cheese weight increased after brining at 3, 6, or 10°C. Cold storage also prevented further fermentation and the pH remained constant, whereas at 22°C the pH dropped as low as pH 4.1. At 3°C, the cheese matrix expanded (20 to 30%), whereas at 22°C there was a contraction and a 13 to 18 g/100 g loss in weight. Expansion of the protein matrix at 3°C was reversed by changing to 22°C. However, contraction of the protein matrix was not reversed by changing to 3°C, and the cheese volume remained less than what it was initially.     

Kinetic study of β-lactoglobulin thermal aggregation at low pH

Kinetics of β-lactoglobulin (β-lg) thermal aggregation at pH 3.35, 85 °C, and 2-8% w/w protein concentration was studied using high performance liquid chromatography (HPLC) coupled with multi-angle laser light scattering (MALS) and rheology. Rate of β-lg aggregation was found to be of first order with respect to the initial protein concentration, and the conversion of native-like β-lg monomers/dimers (<36 kDa) to aggregates increased with initial concentration and heating times. The size of the aggregates formed during heating was dependent on the initial protein concentration. A simple nucleation and growth model was described for the β-lg aggregation at pH 3.35, where nucleation was found to be a rate limiting step below the previously identified critical concentration, C_c ∼ 6.4% protein. Above the C_c, nucleation occurred quickly and was not rate limiting. Critical size of the nucleus varied with protein concentration, with larger critical size needed at lower protein concentrations.     

Effect of milk pasteurisation temperature on age-related changes in lactose metabolism,pH and the growth of non-starter lactic acid bacteria in half-fat Cheddar cheese

Half-fat Cheddar cheese (∼15%, w/w, fat) was manufactured on three occasions from milk pasteurised at 72, 77, 82 or 87 °C for 26 s, and analysed over a 270 day ripening period. Increasing milk pasteurisation temperature significantly increased the levels of moisture (from ∼45% at 72 °C to 50% at 87 °C), total lactate, and D(−)-lactate in cheese over the 270 day ripening period. Conversely, the cheese pH decreased significantly on increasing pasteurisation temperature. Increasing the pasteurisation temperature did not significantly affect the populations of starter or non-starter lactic acid bacteria during maturation. The use of higher pasteurisation temperatures would appear particularly amenable to exploitation as a means of producing high-moisture (e.g., 40–41%), short-ripened, mild-flavoured Cheddar or Cheddar-like cheeses.     

Gelation of whey protein and xanthan mixture: Effect of heating rate on rheological properties

The effects of heating rate and xanthan addition on the gelation of a 15% w/w whey protein solution at pH 7 and in 0.1 M phosphate buffer were studied using small-amplitude oscillatory shear (SAOS) rheological measurements and uniaxial compression tests. WPI solutions were heated from 25 to 90 °C at five heating rates (0.1, 1, 5, 10 and 20 °C/min). Gelation temperature of WPI decreased with decreasing of heating rates and with xanthan addition. Under uniaxial compression, the WPI gels prepared with no more than 0.2% w/w xanthan exhibited distinct fracture point and were tougher (i.e. higher fracture stress and fracture strain) than the gels prepared with no less than 0.5% w/w xanthan. In general, the fracture strain of WPI gels increased with heating rate, though not significantly, at all xanthan contents investigated. However, the fracture stress of WPI gels, generally, decreased with heating rate when xanthan content was 0–0.2% and increased with heating rate when xanthan content was 0.5 and 1%.     

Study on the rheological properties of heat-induced whey protein isolate-dextran conjugate gel

Effect of glycosylation on the rheological properties of whey protein isolate (WPI) during the heat-induced gelation process was evaluated. Significant changes in browning intensity, free amino groups content and SDS-PAGE profile showed that the conjugate of WPI and dextran (150 kDa) was successfully prepared using the traditional dry-heating treatment. For the conjugate, during the heating and cooling cycle, the curves of G′ and G″ were considerably shifted to lower values and their shapes varied comparing to the corresponding spectra of initial WPI and WPI + dextran mixture. After holding at 25 °C, G' reached a value of about 2200 Pa, only a tenth of the value that obtained in the initial WPI gel. Moreover, frequency sweep measurements revealed that the stiffness of gel was greatly reduced in the conjugate, although a typical elastic gel was still formed. All data showed that the rheological properties of thermal gelation could be modified upon the covalent attachment of dextran.     

Dynamic oscillatory rheological measurement and thermal properties of pea protein extracted by salt method: Effect of pH and NaCl

The effects of two important factors, pH (3.0-10.0) and NaCl (0-2.0 M), on pea protein gelation properties were studied using dynamic oscillatory rheometer and differential scanning calorimeter (DSC). The strongest gel stiffness was achieved at 0.3 M NaCl; higher or lower salt concentrations lead to weakening of the gel. The gelation temperature was also influenced by ionic strength; salt had a stabilization effect which inhibited pea protein denaturation at higher salt concentrations resulting in higher gelling points (p < 0.05). At a NaCl concentration 2.0 M, pea protein gelation was completely suppressed at temperatures ?100 °C. The pH also played an important role in gel formation by pea protein isolates since acid and base cause partial or even total protein denaturation. In this paper the maximum gel stiffness occurred at pH 4.0 in 0.3 M NaCl; higher or lower pH values resulted in reduced gel stiffness (p < 0.05). pH also altered the denaturation temperature of the pea protein; higher pH values resulted in higher denaturation temperatures and higher enthalpies of denaturation (p < 0.05). At pH 3 pea proteins seem like completely denatured by acid as the DSC curve showed a straight line. The gelation temperature (gelling point) peaked at pH ∼6.0 (89.1 °C). Careful adjustment of pH and NaCl concentration would enable the food industry to effectively utilize the salt-extracted pea protein isolate as a gelling agent.     

Dielectric properties of ground almond shells in the development of radio frequency and microwave pasteurization

To develop pasteurization treatments based on radio frequency (RF) or microwave energy, dielectric properties of almond shells were determined using an open-ended coaxial-probe with an impedance analyzer over a frequency range of 10–1800 MHz. Both the dielectric constant and loss factor of almond shells decreased with increasing frequency, but increased with increasing temperature and moisture content. The absolute value of the slopes of log–log plots between loss factor and frequency increased with increasing temperature at low frequencies, especially at high temperatures and moisture contents. The effective electrical conductivity of shell samples was close to zero at the lowest moisture content (6% w.b.) and 3–9 times larger at 90 °C than 20 °C for the highest moisture content (36% w.b.). A good linear relationship was observed between permittivity and density at 1800 MHz. The power penetration depths at RF range (27 and 40 MHz) were about 6–24 times as deep as those for microwave frequencies (915 and 1800 MHz) at each corresponding temperature and moisture content. It is likely that RF energy may provide uniform heating and high throughput treatments for controlling Salmonella in in-shell almonds after washing.     

Physical properties of acid milk gels prepared at 37°C up to gelation but at different incubation temperatures for the remainder of fermentation

We investigated the effect of altering temperature immediately after gels were formed at 37°C. We defined instrumentally measurable gelation (IMG) as the point at which gels had a storage modulus (G′) ≥5 Pa. Gels were made at constant incubation temperature (IT) of 37°C up to IMG, and then cooled to 30 or 33.5, or heated to 40.5 or 44°C, at a rate of 1°C/min and maintained at those temperatures until pH 4.6. Control gel was made at 37°C (i.e., no temperature change during gelation/gel development). Gel formation was monitored using small strain dynamic oscillatory rheology, and the resulting structure and physical properties at pH 4.6 were studied by fluorescence microscopy, large deformation rheology, whey separation (WS), and permeability (B). A single strain of Streptococcus thermophilus was used to avoid variations in the ratios of strains that could have resulted from changes in temperature during fermentation. Total time required to reach pH 4.6 was similar for samples made at constant IT of 37°C or by cooling after IMG from 37 to either 30 or 33.5°C, but gels heated to 40 or 44°C needed less time to reach pH 4.6. Cooling gels after IMG resulted in an increase in G′ values at pH 4.6, a decrease in LT_max, WS, and B, and an increase in the area of protein aggregates of micrographs compared with the control gel made at constant IT of 37°C. Heating gels after IMG resulted in a decrease in G′ values at pH 4.6 and an increase in LT_max values and WS. The physical properties of acid milk gels were dominated by the temperature profile during the gel-strengthening phase that occurs after IMG. This study indicates that the final properties of yogurt greatly depend on the environmental conditions (e.g., temperature, time/rate of pH change) experienced by the casein particles/clusters during the critical early gel development phase when bonding between and within particles is still labile. Cooling of gels may encourage inter-cluster strand formation, whereas heating of gels may promote intra-cluster fusion and the breakage of strands between clusters.     

Influence of green tea polyphenols on the colloidal stability and gelation of WPC

Green tea extracts are being widely used in food products due to their health-promoting properties. Polyphenols can interact with food proteins leading to the formation of soluble or insoluble complexes; therefore they could alter functional properties of proteins. The objective of the present work was to study the colloidal stability and gelation characteristics of a whey protein concentrate (WPC) in the presence of green tea polyphenols. Mixtures of WPC35 (8 and 30% w/v) and green tea polyphenols (0.25–1% w/v) were prepared at pH 4.5 and 6.0. The size of particles formed was analyzed by light scattering, while gelation was characterized by means of dynamic rheometry and texture analysis of gels. At pH 6.0, the particles were smaller and had a higher net charge than at pH 4.5, which accounted for by a less precipitation of the system at pH 6.0. The G′ parameters of gels upon cooling at 35 °C increased with increasing polyphenols concentration at both pH values. However, the relative viscoelasticity decreased. The texture analysis indicated that the addition of polyphenols improved the firmness and adhesiveness of the gels at pH 6.0, while no significant differences were seen at pH 4.5. The results obtained in this work indicate that pH-dependent interaction between green tea polyphenols and WPC induces the formation of aggregates that modifies the viscoelastic and texture properties of the gels.     

Influence of salt-to-moisture ratio on starter culture and calcium lactate crystal formation

The occurrence of l(+)-lactate crystals in hard cheeses continues to be an expense to the cheese industry. Salt tolerance of the starter culture and the salt-to-moisture ratio (S:M) in cheese dictate the final pH of cheese, which influences calcium lactate crystal (CLC) formation. This research investigates these interactions on the occurrence of CLC. A commercial starter was selected based on its sensitivity to salt, less than and greater than 4.0% S:M. Cheddar cheese was made by using either whole milk (3.25% protein, 3.85% fat) or whole milk supplemented with cream and ultrafiltered milk (4.50% protein, 5.30% fat). Calculated amounts of salt were added at milling (pH 5.40 ± 0.02) to obtain cheeses with less than 3.6% and greater than 4.5% S:M. Total and soluble calcium, total lactic acid, and pH were measured and the development of CLC was monitored in cheeses. All cheeses were vacuum packaged and gas flushed with nitrogen gas and aged at 7.2°C for 15 wk. Concentration of total lactic acid in high S:M cheeses ranged from 0.73 to 0.80 g/100 g of cheese, whereas that in low S:M cheeses ranged from 1.86 to 1.97 g/100 g of cheese at the end of 15 wk of aging because of the salt sensitivity of the starter culture. Concentrated milk cheeses with low and high S:M exhibited a 30 to 28% increase in total calcium (1,242 and 1,239 mg/100 g of cheese, respectively) compared with whole milk cheeses with low and high S:M (954 and 967 mg/100 g of cheese, respectively) throughout aging. Soluble calcium was 41 to 35% greater in low S:M cheeses (low-salt whole milk cheese and low-salt concentrated milk cheese; 496 and 524 mg/100 g of cheese, respectively) compared with high S:M cheeses (high-salt whole milk cheese and high-salt concentrated milk cheese; 351 and 387 mg/100 g of cheese, respectively). Because of the lower pH of the low S:M cheeses, CLC were observed in low S:M cheeses. However, the greatest intensity of CLC was observed in gas-flushed cheeses made with milk containing increased protein concentration because of the increased content of calcium available for CLC formation. These results show that the occurrence of CLC is dependent on cheese milk concentration and pH of the cheese, which can be influenced by S:M and cheese microflora.     

Comparative study of high intensity ultrasound effects on food proteins functionality

The objective of this work was to comparatively explore the impact of high intensity ultrasound (HIUS) on the functionality of some of the most used food proteins at the industrial level: whey protein concentrate (WPC), soy protein isolate (500E) and egg white protein (EW).10% w/w solutions at pH 6.5-7.1 were treated with HIUS for 20 min, in an ultrasonic processor. The operating conditions were: 20 kHz, 4.27 ± 0.71 W and 20% of amplitude.Before and after the HIUS treatment, the size of protein particles was measured by static light scattering. The amount of sulfhydryl groups was determined with Ellman’s reagent and the surface hydrophobicity by a fluorescence technique.The effects of HIUS on samples viscosity were determined. The evolution of the elastic (G′) and viscous (G″) moduli as well as tan δ were registered upon time and temperature in a controlled stress rheometer.In general, HIUS promoted a decrease in the consistency index of all protein solutions, mainly of soybean isolate. The gelation performance of EW was not modified by HIUS. However, WPC presented a higher elastic character, but 500E did not show changes upon heating, as it was already denatured before HIUS treatment. The size of aggregates suffered an overall reduction for WPC and 500E, but a slight increase for EW. Sulfhydryl content was unchanged for all proteins after HIUS application but surface hydrophobicity was greatly increased after treatment for all proteins. HIUS affected the studied functional properties differently depending on the size and nature of the protein. This technology could be used to obtain improved functional properties in some protein samples.     

Effect of pH on the gel properties and secondary structure of fish myosin

The relationships between gel properties and the secondary structures of silver carp myosin were investigated at pH 5.5–9.0 using dynamic rheological measurement, circular dichroism and scanning electron microscopy. The gel properties of fish myosin were strongly pH and temperature dependent. During heating at 1 °C/min, myosin formed gels in the pH range 5.5–7.5, but not at pH 8.0–9.0. α-Helix was the predominant structure at pH 7.0. The α-helix fraction declined with increasing temperature and the pH away from 7.0, whilst the other secondary structure fractions increased. The α-helix structure of myosin was more susceptive to acid-treatment than alkali-treatment. As pH increased, the gelation rate and gel strength decreased, and the water-holding capacity (WHC) showed an increasing trend followed by a plateau. High β-sheet and β-turn fractions prior to heating could improve G′ at 90 °C, but they depressed the WHC. A compact and uniform gel of fish myosin was obtained at pH 7.0.     

Concentrated whey protein particle dispersions: Heat stability and rheological properties

In this work heat stability and rheological properties of concentrated whey protein particle dispersions in different dispersing media are studied. Whey protein particles (protein content ∼20% w/v) having an average size of a few microns were formed using a combination of two-step emulsification and heat-induced gelation. Particles were dispersed (volume fraction of particles ∼0.35) in solutions of Na-caseinate, whey protein isolate or gum arabic at different concentrations. The microstructure, particle size distribution and flow behaviour of the dispersions were analyzed before and after heating at 90 °C for 30 min.