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1.
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 相似文献
2.
Rheological, Thermal and Microstructural Properties of Whey Protein-Cassava Starch Gels 总被引:2,自引:0,他引:2
Mixed gels of cassava starch (CS) and a whey protein isolate (WPI), obtained by heating solutions of 10% total solids, pH 5.75 to 85°C, were characterized as a function of the starch fraction, θs, by axial compression, small-amplitude oscillatory rheometry, differential scanning calorimetry (DSC) and scanning electron microscopy (SEM). Gelation did not occur for θs > 0.7. In the range 0<θs < 0.4 mixed gels showed higher mechanical (E, elastic modulus) and rheological (G′, storage modulus) properties than pure gels, with maximum values for θs= 0.2–0.3. Viscoelastic measurements as a function of time showed that gels containing higher levels of WPI developed a larger G. Blends of both biopolymers showed independent thermal transitions in DSC measurements, related to gelatinization and denaturation. Microstructure of a mixed gel formed at θs= 0.2 showed a continuous matrix formed by strands of WPI particle aggregates and an independent CS phase. 相似文献
3.
COLD GELATION OF WHEY PROTEIN EMULSIONS 总被引:4,自引:0,他引:4
PAULA ROSA GUIDO SALA TON VAN VLIET FRED VAN DE VELDE 《Journal of texture studies》2006,37(5):516-537
Stable and homogeneous emulsion‐filled gels were prepared by cold gelation of whey protein isolate (WPI) emulsions. A suspension of heat‐denatured WPI (soluble WPI aggregates) was mixed with a 40% (w/w) oil‐in‐water emulsion to obtain gels with varying concentrations of WPI aggregates and oil. For emulsions stabilized with native WPI, creaming was observed upon mixing of the emulsion with a suspension of WPI aggregates, likely as a result of depletion flocculation induced by the differences in size between the droplets and aggregates. For emulsions stabilized with soluble WPI aggregates, the obtained filled suspension was stable against creaming, and homogeneous emulsion‐filled gels with varying protein and oil concentrations were obtained. Large deformation properties of the emulsion‐filled cold‐set WPI gels were determined by uniaxial compression. With increasing oil concentration, the fracture stress increases slightly, whereas the fracture strain decreases slightly. Small deformation properties were determined by oscillatory rheology. The storage modulus after 16 h of acidification was taken as a measure of the gel stiffness. Experimental results were in good agreement with predictions according to van der Poel's theory for the effect of oil concentration on the stiffness of filled gels. Especially, the influence of the modulus of the matrix on the effect of the oil droplets was in good agreement with van der Poel's theory. 相似文献
4.
María Julia Spotti Martina J. Perduca Andrea Piagentini Liliana G. Santiago Amelia C. Rubiolo Carlos R. Carrara 《Food Hydrocolloids》2013
The effect of Maillard reaction on the mechanical properties of whey protein isolate (WPI) heat-induced gels was evaluated. WPI and dextran (15–25 kDa) conjugates were obtained by controlled dry heating during storage at 60 °C and 63% relative humidity for 2, 5 and 9 days. Changes in browning intensity and content of free amino groups were used to estimate the Maillard reaction. A decrease in free amino groups of WPI was observed when increasing polysaccharide concentration and reaction time. An increase in both a* and b* CIE Lab colour parameters indicated the development of a reddish-brown colour, typical of the Maillard reaction. Uniaxial compression and stress relaxation tests were performed to measure the mechanical properties of mixed and conjugate gels. Maillard reaction significantly modified the mechanical properties of WPI/DX gels, and even prevented fracture when conjugate gels were subjected to 80% deformation in uniaxial compression test. 相似文献
5.
Contour plots were developed for the compression stress (at 20% deformation) of single-component, mixed and filled protein gels. Samples were made by heating and acidification from skim milk powder, SMP (0–20% TS), whey protein isolate, WPI (0–10% TS), and recombined cream, within pH 3.6–3.9, 4.6–4.8 and 5.1–5.3. At higher pH, WPI gels were stronger than SMP gels. WPI had a reinforcing effect on SMP gels, while small additions of SMP to WPI gels resulted in weaker mixed gels. Filled gels containing cream had higher compression strengths than mixed gels. Micrographs showed linking of casein chains by WPI strands in mixed gels and compatibility of fat globules with casein micelles in the protein network of filled gels. 相似文献
6.
Whey protein isolate (WPI) was subjected to limited tryptic hydrolysis and the effect of the limited hydrolysis on the rheological properties of WPI was examined and compared with those of untreated WPI. At 10% concentration (w/v in 50 mM TES buffer, pH 7.0, containing 50 mM NaCl), both WPI and the enzyme-treated WPI (EWPI) formed heat-induced viscoelastic gels. However, EWPI formed weaker gels (lower storage modulus) than WPI gels. Moreover, a lower gelation point (77 °C) was obtained for EWPI as compared with that of WPI which gelled at 80 °C only after holding 1.4 min. Thermal analysis and aggregation studies indicated that limited proteolysis resulted in changes in the denaturation and aggregation properties. As a consequenece, EWPI formed particulated gels, while WPI formed fine-stranded gels. In keeping with the formation of a particulate gel, Texture Profile Analysis (TPA) of the heat-induced gels (at 80 °C for 30 min) revealed that EWPI gels possessed significantly higher (p < 0.05) cohesiveness, hardness, gumminess, and chewiness but did not fracture at 75% deformation. The results suggest that the domain peptides, especially β-lactoglobulin domains released by the limited proteolysis, were responsible for the altered gelation properties. 相似文献
7.
The rheological properties at small (oscillatory shear) and large (uniaxial compression) deformations of heat-induced gels (80 °C for 20 min, pH 7.3) containing 25% rennet casein (RCN), 2.5% disodium phosphate and 0%, 2.3% or 6.3% of whey protein isolate (WPI) were measured for samples cooked in a torque-rheometer at mixing speeds within a range of 20–200 rpm (shear rates: ∼15–230 s−1). In addition, microstructure analyses were performed, separately staining RCN and WPI, by Confocal Scanning Laser Microscopy (CSLM). Both small and large deformation tests indicated that increasing addition of WPI prior to the cooking process of RCN resulted in gels exhibiting higher storage and deformability moduli than WPI-free samples. Increasing shear rates during cooking also affected the rheological properties of RCN–WPI gels, and stronger gels were formed as the shear rate during cooking was increased. Despite the data dispersion among replicates, the effect of shear rate on gel strength were evident for RCN gels with 6.3% WPI and relatively clear for gels with 2.3% WPI; however, the trend was uncertain for WPI-free RCN gels. Possible explanations for this observation are that when increasing WPI levels in the presence of RCN and heat, disulfide-thiol exchange reactions between denatured WPI and κ-casein (κ-CN) are increased and possibly promoted by shear rate, resulting in stronger and more cross-linked gel structure. CSLM results were not conclusive to support this hypothesis. 相似文献
8.
Guido Sala Ton van Vliet Martien A. Cohen Stuart George A. van Aken Fred van de Velde 《Food Hydrocolloids》2009
The large deformation properties of gelatine, κ-carrageenan and whey protein isolate (WPI) gels filled with bound and unbound oil droplets were studied as a function of compression speed. The rheological properties of the gel matrices controlled the compression speed-dependency of the gels containing oil droplets. Polymer gels (gelatine and κ-carrageenan gels) showed a predominantly elastic behaviour. Their Young's modulus was not affected by the compression speed. The increase of fracture stress and strain observed with increasing compression speed was related to friction between the structural elements of the gels and, for gelatine, to the unzipping of physical bonds. Particle gels (WPI gels) showed a more viscoelastic behavior. Their Young's modulus and fracture stress increased with compression speed. This was attributed to the viscous flow of the matrix and friction phenomena between structural elements of the gel. The effect of an increase in the oil volume fraction (φ) on the Young's modulus was for all gels according to the Van der Poel theory. In addition, oil droplets embedded in the gel matrix acted as stress concentration nuclei and increased friction. The relative impact of these two effects was related to the viscoelastic properties of the gels and to droplet–matrix interaction. For polymer gels and gels with bound droplets, stress concentration phenomena played a relatively larger role. For particle gels and gels with unbound droplets, friction phenomena were relatively more important, increasing the viscoelastic character of the gels. As a result, an increase in φ resulted in a decrease of both fracture stress and fracture strain for polymer gels and in an increase of the fracture stress and a decrease of fracture strain for particle gels. 相似文献
9.
Kátia Regina Kuhn Ângelo Luiz Fazani Cavallieri Rosiane Lopes Da Cunha 《International Journal of Food Science & Technology》2010,45(2):348-357
Cold‐set whey protein isolate (WPI) gels formed by sodium or calcium chloride diffusion through dialysis membranes were evaluated by mechanical properties, water‐holding capacity and microscopy. The increase of WPI concentration led to a decrease of porosity of the gels and to an increase of hardness, elasticity and water‐holding capacity for both systems (CaCl2 and NaCl). WPI gels formed by calcium chloride addition were harder, more elastic and opaque, but less deformable and with decreased ability to hold water in relation to sodium gels. The non linear part of stress–strain data was evaluated by the Blatz, Sharda, and Tschoegl equation and cold‐set gels induced by calcium and sodium chloride addition showed strain‐weakening and strain‐hardening behaviour, respectively. The fractal structure of the gels indicated a weak‐link behaviour. For WPI gels results suggest intrafloc links, formed at heating step, which were more rigid than the interfloc links, promoted by salt addition. 相似文献
10.
Guido Sala Ton van Vliet Martien Cohen Stuart Fred van de Velde George A. van Aken 《Food Hydrocolloids》2009,23(7):1853-1863
The effect of the ratio between the modulus of the oil droplets and that of the gel matrix (varied by changing gelling agent concentration and oil droplet size) on the large deformation properties of gelatine, κ-carrageenan and whey protein isolate (WPI) gels was studied at different compression speeds. The effect of gelling agent concentration and oil droplet size on strain-dependency of modulus and viscoelastic properties was also studied. An increase in the concentration of gelling agent resulted in denser gels with more bonds between structural elements. This induced an increase of both Young's modulus and fracture stress for all gels. With increasing gelling agent concentration, polymer gels (gelatine and κ-carrageenan) became less strain-hardening, and the particle gels (WPI) even became strain-softening. The effect of a decrease in the oil droplet size on the Young's modulus was generally according to the Van der Poel theory, unless when the oil droplets were aggregated. Moreover, a decrease in oil droplet size induced a decrease of the fracture strain in gels with non-aggregated bound droplets. The extent of these changes was shown to depend on the gelling agent concentration. The effect of a decrease of the oil droplet size on other fracture parameters and in other gel systems was minor. With decreasing oil droplet size gelatine gels with unbound droplets and WPI gels became more viscous and less elastic. 相似文献
11.
The effect of heating rate and pH on fracture properties and held water (HW) of globular protein gels was investigated. The study was divided into 2 experiments. In the 1st experiment, whey protein isolate (WPI) and egg white protein (EWP) gels were formed at pH 4.5 and 7.0 using heating rates ranging from 0.1 to 35 °C/min and holding times at 80 °C up to 240 min. The 2nd experiment used one heating condition (80 °C for 60 min) and probed in detail the pH range of 4.5 to 7.0 for EWP gels. Fracture properties of gels were measured by torsional deformation and HW was measured as the amount of fluid retained after a mild centrifugation. Single or micro-phase separated conditions were determined by confocal laser scanning microscopy. The effect of heating rate on fracture properties and HW of globular protein gels can be explained by phase stability of the protein dispersion and total thermal input. Minimal difference in fracture properties and HW of EWP gels at pH 4.5 compared with pH 7.0 were observed while WPI gels were stronger and had higher HW at pH 7.0 as compared to 4.5. This was due to a mild degree of micro-phase separation of EWP gels across the pH range whereas WPI gels only showed an extreme micro-phase separation in a narrow pH range. In summary, gel formation and physical properties of globular protein gels can be explained by micro-phase separation. PRACTICAL APPLICATION: The effect of heating conditions on hardness and water-holding properties of protein gels is explained by the relative percentage of micro-phase separated proteins. Heating rates that are too rapid require additional holding time at the end-point temperature to allow for full network development. Increase in degree of micro-phase separation decreases the ability for protein gels to hold water. 相似文献
12.
《Food Hydrocolloids》2006,20(5):678-686
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%. 相似文献
13.
《Food research international (Ottawa, Ont.)》2013,53(2):452-459
The following study explored how the addition of various proteins (gelatin, soy protein isolate (SPI) and heated/unheated whey protein isolate (WPI)), at two different concentration levels (1% and 2%), affected the mechanical, microstructural and optical properties of calcium cross-linked ‘wet’ alginate films. Additionally, the water holding capacity and textural profile analysis (TPA) properties were determined for the alginate–protein gels. Adding all types of protein significantly (P < 0.05) decreased the force to puncture the ‘wet’ alginate–protein composite films compared to the control alginate film. The tensile test showed significant differences in tensile strength between the various films but interestingly there was no significant difference in the percent elongation at breaks between any of the films. Micrograph images showed that the SPI and heated WPI formed relatively larger protein clumps/regions in the alginate films whereas the gelatin and unheated WPI appeared to be more integrated into the alginate film. The heated WPI films were the least transparent of all the films, followed by the SPI films. Few TPA differences existed between the alginate–protein gels. However, the alginate–gelatin gels did have significantly less water loss than the other alginate–protein gels suggesting that alginate and gelatin may be the most compatible of all the alginate–protein combinations tested. 相似文献
14.
Rheological,thermal and microstructural properties of whey protein isolate‐modified cassava starch mixed gels at different pH values
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Fei Ren Bin Yu Die Dong Zhao‐hua Hou Bo Cui 《International Journal of Food Science & Technology》2017,52(11):2445-2454
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. 相似文献
15.
Four % (wt/wt) aqueous solutions were prepared at corn starch:methylcellulose:whey protein isolate (CS:MC:WPI) ratios of 2:2:2, 1:2:3, 2:1:3, 2:2:0, 1:2:0 and 2:1:0. Glycerol (gly) was used as a plasticiser at CS–MC–WPI:gly ratios of 2:1, 2.5:1 and 3:1. CS–MC–WPI blend films were stronger than CS–WPI films and had lower oxygen permeability (OP) than MC–WPI films. The highest tensile strength (TS) of blend films was 8.01 ± 3.41 MPa, at CS:MC:WPI ratio of 2:2:0 and CS–MC–WPI:gly ratio of 3:1. Lowest OP value was 45.05 ± 7.24 cm3 μm m?2 per day kPa?1, at CS:MC:WPI ratio of 2:2:2 and CS–MC–WPI:gly ratio of 3:1. OP values were predictable based on relative amounts of components. However, TS and elastic modulus properties of the CS–MC–WPI blend films did not reflect the relative amounts of the components. All of CS–MC–WPI films were translucent indicating some degree of immiscibility among the CS, MC and WPI. These results indicate the influence of complex molecular interactions among the components. 相似文献
16.
考察了p H(3、7)、氯化钠浓度(50、200mmol/L)以及热处理(90℃、30min)对不同乳化剂(乳清分离蛋白、Tween20、Tween20+马铃薯蛋白水解物)制备O/W乳状液分层稳定性的影响。并以凝胶持水性和凝胶强度为指标,考察了p H和氯化钠浓度对上述不同界面组成的乳化颗粒填充乳清蛋白热诱导凝胶性质的影响。结果表明,以乳状液为溶剂制备的凝胶持水性与凝胶强度高于以水为溶剂制备的凝胶。加入一定量的氯化钠有助于乳状液凝胶持水性与凝胶强度的增加。研究表明,p H和盐浓度对乳状液填充凝胶强度均有影响,乳状液性质对乳状液填充凝胶强度和持水性有一定影响。 相似文献
17.
Influence of dialyzable compounds on the Theological properties (shear stress and shear strain at failure) of heat-induced whey protein concentrate (WPC) and whey protein isolate (WPI) gels was examined. Dialyzing WPC and WPI suspensions prior to gelation increased the stress of two of three WPC gels and a WPI gel. Dialysis also significantly increased the strain of the same two WPC gels, normalizing all strain values. Replacement of calcium lost through dialysis did not significantly change gel rheology. However, chelating calcium caused a significant decrease in the stress of all gels: a minimum amount of calcium and/or a calcium complex appears to have a major role in whey protein gelation. 相似文献
18.
Nanik Purwanti Emma van der Veen Atze Jan van der Goot Remko Boom 《International Dairy Journal》2013,28(2):62-69
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. 相似文献
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20.
Nanik Purwanti Anouk MoerkensAtze Jan van der Goot Remko Boom 《Food Hydrocolloids》2012,26(1):240-248
Concentrated protein gels were prepared using native whey protein isolate (WPI) and WPI based microparticles. WPI microparticles were produced by making gel pieces from a concentrated WPI suspension (40% w/w), which were dried and milled. The protein within the microparticles was denatured and the protein concentration after drying was similar to the native WPI powder. WPI microparticles had irregular shape with an average size of about 70 μm. They absorbed water when dispersed in water, but the dispersion did not gel upon heating. Replacing part of the native WPI powder with WPI microparticles in the protein gel resulted in lower gel stiffness compared with a gel with the same overall protein concentration but without microparticles. However, microparticles also strengthened the continuous phase because they take up water from this phase. This might increase gel stiffness more than would be expected from an inert particle/filler. There was also good bonding between the microparticles and the WPI continuous phase in the gel, which contributed to gel stiffness. 相似文献