Effect of heating temperature,pH, concentration and starch/whey protein ratio on the viscoelastic properties of corn starch/whey protein mixed gels

The viscoelastic properties of corn starch (CS) gels were more dependent on heating temperature, while the properties of whey protein isolate (WPI) gels were more dependent on pH. Thus heating temperature (75, 85, 95 °C) and pH (5, 7, 9) were varied to obtain a series of mixed gels with interesting viscoelastic properties. WPI gels showed extensive stress relaxation (SR) indicative of a highly transient network structure, while CS gels relaxed very little in 2000 s. Based on SR results, it appeared that CS/WPI mixed gels with 25 and 50% CS formed compatible network structures at 15% total solids only at pH 9. This supposition was supported by SEM microstructures obtained for dehydrated gels and a synergistic increase in the large‐strain fracture stress for these gels. Some synergy was also found for mixed gels at 30% total solids at pH 9, while at pH 7 the mixed gels seemed to contain separate additive WPI and CS networks unlike the case for pH 7 at 15% total solids. In both cases (15 and 30% total solids) the degree of elasticity of the mixed gels decreased as the WPI content increased. Mixed gels (CS:WPI = 0.5) at pH 9 showed increased fracture stress and fracture strain relative to the same gels at pH 7. This suggests that a unique chemical compatibility exists at pH 9 and results in gels that combine the elasticity of CS and the internal stress dissipation of WPI. © 2001 Society of Chemical Industry     

Effects of fluid shear and temperature on whey protein gels, pure or mixed with xanthan

The effects of shear on whey protein isolate (WPI) gels, pure or mixed with xanthan, have been investigated at pH 5.4 by dynamic oscillatory measurements and light microscopy (LM). The shear was performed on the suspensions under a constant stress of between 0.04 and 2.1 Pa. Various temperature conditions were chosen in order to describe the effects of shear at the different states of aggregation of the WPI. Shear-sensitive aggregation phenomena were already found around 40°C for the pure WPI samples. Continuous shearing during heating from 20 to 40°C, prior to heat treatment at 90°C, resulted in a gel with a storage modulus (G′) half that of the unsheared gel, independent of the shear stress. Continuous shearing during heating from 20 to 76°C resulted in a further decrease in G′. Inhomogeneities arose in networks formed from continuously sheared suspensions during heating from 20 to 50°C and above. Depending on the shear stress and on the heating range of the shear, the networks showed areas of varied compactness and different classes of pores, ranging from 10 to 200 μm. A higher G′, compared to that for the unsheared gel, was found for gels subjected to shear for short periods in the vicinity of the gel point. The presence of xanthan inhibited the aggregation and demixing of the WPI, described as a sterical phenomenon. Under static conditions, the presence of xanthan resulted in a more homogeneous WPI network. Exposing the mixed suspensions to shear generally increased the inhomogeneity of the network structure. Short periods of shearing in the vicinity of the gel point affected the kinetics of the gel formation and resulted in gels with higher G′ values than the unsheared gel. Continuous shearing under stresses below 0.09 Pa, during heating from 20 to 60°C and above, also resulted in gels with an increased G′. Continuous shear under stresses above 0.9 Pa resulted in gels with a decreased G′     

Effect of protein concentration on whey protein gels obtained by a two-stage heating process

 The influence of protein concentration on the properties of gels obtained by a two-stage heating process was determined. In the first stage, whey protein dispersion (3–10%) was heated at pH 8.0, and in the second stage it was diluted to 3% protein, adjusted to pH 7.0 and heated again. Increased protein concentration in the first stage of polymerization resulted in the gels obtained in the second stage having a lower phase angle, increased storage modulus and increased hardness. Increased protein concentration also resulted in gels with an increased optical density, which suggests thathigher protein concentration leads to more and larger aggregates. Gels obtained from dispersions preheated at a higher protein concentration had higher permeability coefficient (B _gel) values. The increase in B _gel suggests that the higher protein concentration increased the size of the aggregates, which in a second stage of heating formed a gel matrix with a larger pore size. Received: 11 February 1999     

Rheological,thermal and microstructural properties of whey protein isolate‐modified cassava starch mixed gels at different pH values

The objective of this study was to investigate the rheological, thermal and microstructural properties of whey protein isolate (WPI)‐hydroxypropylated cassava starch (HPCS) gels and WPI‐cross‐linked cassava starch (CLCS) gels at different pH values (5.75, 7.00 and 9.00). The rheological results showed that the WPI‐modified starch gels had greater storage modulus (G?) values than the WPI‐native cassava starch gels at pH 5.75 and 7.00. Differential scanning calorimetry curves suggested that the phase transition order of the WPI and modified starch changed as the pH increased. Scanning electron microscopy images showed that the addition of HPCS and CLCS contributed to the formation of a compact microstructure at pH 5.75 and 7.00. A comprehensive analysis showed that the gelling properties of the WPI‐modified starch were affected by the difference between the WPI denaturation temperature and modified starch gelatinisation temperature and by the granular properties of the modified starch during gelatinisation. These results may contribute to the application of WPI‐modified starch mixtures in food preparation.     

Rheology of thermo-reversible fish protein isolate gels

Fish protein isolates (FPI) from cod muscle were studied at pH 9 and 11. Thermo-reversible gels, stable at and below room temperature could be produced at both pH values. Application of low shear stress to the gels led to an initial elastic response followed by a power-law deformation (creep) at both pH. Above a critical shear stress gels fractured and flowed regularly with a viscosity of about 0.05 Pa s.Strain–stress curves were recorded using both flow and oscillatory measurements. For all systems strain-hardening was observed followed by fracture. Fracture occurred at approximately the same deformation, but the amplitude of strain-hardening and the yield stress decreased with decreasing rate of the stress ramp. Results obtained from oscillatory shear at 1 or 0.1 Hz were close to those obtained with continuous shear during the fastest stress ramps.The structure of the gels was investigated using confocal laser scanning microscopy and turbidity measurements.     

Polyelectrolyte screening effects on the dissolution of whey protein gels at high pH conditions

The literature reports an optimum NaOH concentration for the alkaline cleaning of whey deposits or gels; at NaOH concentrations higher than this optimum, cleaning proceeds much more slowly. Although this phenomenon is of great importance in the cleaning of dairy equipment, no conclusive physical explanation has yet been presented. In this study, we present strong evidence that the dissolution rate is affected by the equilibrium-swelling ratio in β-lactoglobulin (βLg) gels. The swelling ratio is greatly reduced in the presence of salts due to the polyelectrolyte screening effect of the cations. This has been observed in free-swelling βLg gels using gravimetrical analysis and in the uniaxial swelling of WPC gel deposits using fluid dynamic gauging. At high dissolution pH (>13.3), the high Na⁺ concentration reduces swelling in spite of the high surface charge of the protein. It is proposed that the reduction of the free volume inside the gel impedes the transport of the protein aggregates out of the NaOH penetration zone. We have also observed that the final dissolution rate of gels pre-soaked in 1 M NaOH or NaCl is similar, despite the difference in pH, and much lower than for untreated gels: the high Na⁺ concentration in the soaked gels hinders swelling, inhibiting the disentanglement of the protein clusters regardless of the high pH.     

Effect of protein composition on the rheological properties of acid-induced whey protein gels

Protein dispersions with different ratios of α-lactalbumin to β-lactoglobulin were heat-denatured at pH 7.5 and then acidified with glucono-δ-lactone to form gels at room temperature. Heat treatment induced the formation of whey protein polymers with reactive thiol group concentrations ranging from 1 to 50 μmol/g, depending on protein composition. During acidification, the first sign of aggregation occurred when the zeta potential reached −18.2 mV. Increasing the proportion of α-lactalbumin in the polymer dispersions resulted in more turbid gels characterized by an open microstructure. Elastic and viscous moduli were reduced, while the relaxation coefficient and the stress decay rate constants were increased by raising the proportion of α-lactalbumin in the gel. After one week of storage at 5 °C, gel hardness increased by 12%. The effect of protein composition on acid-induced gelation of whey protein is discussed in relation to the availability and reactivity of thiol groups during gel formation and storage.     

Shear-induced structuring of particulate whey protein gels

The effects of steady shear on particulate whey protein isolate (WPI) gels, at pH 5.4, have been investigated by light microscopy (LM) and dynamic oscillatory measurements. The steady shear was performed on suspensions at constant rates between 0.5 and 126/s. The gel point under static conditions (T_g) was around 78 °C and the shearing was performed during heating from 20 to 76 or to 82 °C. The gel point was postponed by the shear up to 82 °C. Steady shear up to 76 °C, at rates less than 6/s, resulted in a weaker storage modulus (G′), less frequency dependence and a higher stress at fracture compared to the unsheared gel. Steady shear up to 82 °C, at rates below 6/s, resulted in the formation of two different types of network structure. One structure was similar in appearance to the unsheared network, showing pores in the range of 50 μm. The other structure was dense, composed of smaller particles than the unsheared network and with pores in the range of 10 μm. The gels composed of two structures showed a lower G′ and stress at fracture compared to the unsheared gel. A shear rate above 24/s up to 76 °C resulted in irregular networks, which were composed of two different types of structures. One was loose and open, similar in appearance to the unsheared network structure. The other structure was dense and compact, and was present as individual aggregates. These gels also showed a weaker G′ than the unsheared gel. A shearing up to 82 °C at rates above 24/s resulted in a coarse, inhomogeneous network structure. The gels showed a weak G′, indicating aggregate break-up during the steady shear.     

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%.     

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.     

Effect of monoglycerides and diglycerol-esters on viscoelasticity of heat-set whey protein emulsion gels

Summary Effects of small-molecule surfactants (emulsifiers) on the small-deformation viscoelastic properties of heat-set whey protein emulsion gels have been investigated using a controlled stress rheometer. The surfactants used in this investigation were the water-soluble diglycerol monolaurate (DGML) and diglycerol monooleate (DGMO), and the oil-soluble glycerol monooleate (GMO). The elastic modulus of the emulsion gel was found to decrease in the presence of a small amount of surfactant, but then to recover at higher surfactant concentrations. The initial reduction in modulus correlates with protein displacement from the oil droplet surface. The recovery of the storage and loss moduli at higher surfactant concentrations of DGML or DGMO may be due to the depletion flocculation of the emulsion prior to heat-treatment. However, for systems containing high content of GMO in the oil phase, the recovery of the moduli is probably owing mainly to the smaller average particle size. Effects of surface monolayer composition, droplet aggregation and average particle size were discussed. The behaviour obtained here was compared with results for previously investigated whey protein emulsion gel systems containing different emulsifiers.     

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.     

乳清分离蛋白与大豆分离蛋白混合溶液制备外源式钙交联冷凝胶型微球体

将分别经过热变性处理的乳清分离蛋白和大豆分离蛋白溶液按照2∶1,1∶1和1∶2比例(质量比)混合后,通过外源式添加钙离子的方法,获得钙交联冷凝胶型微球体。检测微球体的蛋白质包埋率、溶解度和溶胀率。结果显示,微球体的蛋白质包埋率较高,均大于99.36%,不同蛋白质比率对蛋白质包埋率没有显著影响。微球体具有一定的水溶性,在缓冲液中的溶解度顺序为pH7.0pH2.5pH4.5,且乳清蛋白质量分数越高,微球体的溶解度越小。微球体在缓冲液中发生不同程度的膨胀,溶胀率顺序为pH2.5pH7.0,而在pH值为4.5缓冲液中发生皱缩,溶胀率为负值,微球体中的乳清蛋白质量分数越高,溶胀率越小。缓冲液中的钙离子会影响微球体的溶解度和溶胀率。基本性质说明外源式钙交联冷凝胶型微球体可以作为热敏性或活性物质的传递载体,应用于相关的食品及医药行业。     

Stiffening in gels containing whey protein isolate

Gels made only from whey protein isolate (WPI) stiffened over the first few days of storage, after which the textural properties remained nearly constant. However, protein gels containing WPI microparticles, at the same total protein content, stiffened over a longer period than those without microparticles. This stiffening was suggested to be the result of rearrangement of crosslinks in the gel. Addition of particles induces additional effects leading to water distribution between the protein particles and continuous phase. The stiffness change over time was different for gels made from a mixture of locust bean gum and xanthan gum containing microparticles. The stiffness of matrix gel and of gels containing 20% (w/w) microparticles was rather stable over time; microscopy analysis of these gels showed that particle size was constant after 72 h storage. Nevertheless, changes were observed in small deformation; this might be the consequence of slow rearrangements within the protein particles.     

Effect of denatured whey protein concentrate and its fractions on rennet-induced milk gels

Denatured whey protein concentrate was fractionated by centrifugation to study the effect of its different components (sedimentable aggregates, non-sedimentable component, and diffusible component) on rennet-induced coagulation of milk and gel contraction capacity. Milk coagulation properties were characterized by optical density measurement and dynamic rheometry. The contraction kinetics of the gel during cooking was also characterized. The diffusible component of denatured whey protein concentrate showed no significant effect on coagulation or contraction parameters. Sedimentable aggregates negatively influenced the kinetics of rennet gel formation, as measured by rheology; these aggregates also reduced the contraction capacity of the gel. The non-sedimentable component negatively influenced milk coagulation properties, as measured with both optical and rheological methods, and decreased the contraction capacity of the gel. The results suggest that, beyond the effect of sedimentable whey protein aggregates, soluble proteinaceous complexes (non-sedimentable and non-diffusible) could interact with renneted casein micelles and limit gel formation and contraction.     

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).     

Effect of whey protein enzymatic hydrolysis on the rheological properties of acid-induced gels

A protein dispersion blend of β-lactoglobulin and α-lactalbumin was heat-denatured at pH 7.5, hydrolyzed by α-chymotrypsin and then acidified with glucono-δ-lactone to form gels at room temperature. Heat treatment induced the formation of whey protein polymers with high concentration of reactive thiol groups (37 μmol/g). The reactive thiol group concentration was reduced by half after 40 min enzymatic hydrolysis. It was further reduced after enzyme thermal deactivation. During acidification, the first sign of aggregation for hydrolyzed polymers occurred earlier than for non hydrolyzed polymers. Increasing the hydrolysis duration up to 30 min resulted in more turbid gels characterized by an open microstructure. Elastic and viscous moduli were both reduced, while the relaxation coefficient and the stress decay rate constants were increased by increasing the hydrolysis duration. After one week storage at 5 °C, the hardness of gels made from hydrolyzed polymers increased by more than 50%. The effect of polymer hydrolysis on acid-induced gelation is discussed in relation to the availability and reactivity of thiol groups during gel formation and storage.     

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.