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.     

The effect of ionic strength on the rheology of pH-induced bovine serum albumin/κ-carrageenan coacervates

Protein/polysaccharide coacervates are frequently applied to food products to control the rheology. This study investigated the effect of ionic strength (I) on the rheology of pH-induced protein/polysaccharide coacervates. Bovine serum albumin (BSA) and κ-carrageenan were used as a model protein and a polysaccharide, respectively. As the formation of BSA/κ-carrageenan coacervates increased the turbidity of an aqueous mixture, pH_c, pH_?, and pH_max values were identified corresponding to the pH of the formation of soluble coacervates, insoluble coacervates, and large insoluble coacervates respectively. Based on pH_c, pH_?, and pH_max, a state diagram of BSA/κ-carrageenan coacervation versus pH and I was constructed. Involvement of salt in coacervation screened out the electrostatic interaction between BSA and κ-carrageenan coacervation, resulting in the shift of pH_c, pH_?, and pH_max to lower pH. The shift was linearly changed to 1/I^1/2 that corresponded to the Debye length. BSA/κ-carrageenan coacervates were more elastic than viscous. The transition from insoluble coacervates to large insoluble coacervates contributed to enhancement of the rheology, especially in elasticity. An increase in the I of a BSA/κ-carrageenan mixture reduced the degree of coacervation and the elasticity, and the viscosity of BSA/κ-carrageenan coacervates.     

The effect of freeze–thaw cycles on microstructure and physicochemical properties of four starch gels

The effect of repeated freeze–thaw (FT) cycles (up to seven) on microstructure, thermal and textural properties of four starch gels from various botanical origins (gingko, Chinese water chestnut, potato and rice) was investigated and compared by scanning electronic microscope, differential scanning calorimetry and texture analyzer. The chemical composition and molecular structure of four starches were also examined. The Chinese water chestnut, potato and rice starch gels formed a honey-comb structure after 7 FT cycles, while gingko starch gel exhibited lamellar structure. The 7 FT cycles decreased the transition temperatures and enthalpies of four starches in comparison with each native starch, and the retrogradation percentage followed the order: rice > gingko > Chinese water chestnut > potato. The 7 FT cycles increased the hardness of all the evaluated starch gels and decreased springiness and cohesiveness. Results showed that the molecular structure of starches caused notable differences to the microstructure and textural properties of starch gels. The higher amount of longer branch chain (degree of polymerization (DP) > 18) might benefit the formation of the lamellar structure of gingko starch. The percentage of branch chains (DP 18–23) was negatively related with the springiness and cohesiveness of native starch gels, while the percentage of medium chains (DP 12–17) was positively related to the springiness of starch gels after 7 FT cycles.     

Viscoelastic behavior and microstructure of aqueous mixtures of cross-linked waxy maize starch,whey protein isolate and κ-carrageenan

The viscoelasticity and microstructure of mixtures of cross-linked waxy maize starch (CH10), whey protein isolate (WPI) and κ-carrageenan (κC) at pH 7.0 with 100 mM NaCl were investigated by oscillatory rheometry and confocal laser scanning microscopy (CLSM). Mixtures were heated to 90 °C (1.5 °C/min), held for 10 min at this temperature and cooled. Within the range of concentrations studied, CH10 swollen granules reinforced WPI and κC networks. The mechanical behavior of the three-component mixtures was modified by different WPI concentrations, but κC governed the overall response due to its gelling ability. CLSM images of three-component mixtures showed particulate systems in which swollen starch granules are surrounded by κC and WPI. CH10 granules were immersed in a single phase and a separate phase of κC and WPI, for low and high concentrations of these components, respectively. Therefore, it is possible to obtain two- and three-phase mixtures.     

Rheology and microstructure of basil seed gum and β-lactoglobulin mixed gels

Gelling profiles and interaction between basil seed gum (BSG) and β-lactoglobulin (BLG) were characterized using dynamic rheology and scanning electron microscopy. Sequence of experimental sweeps of time–temperature, frequency, and strain were applied for BSG, BLG and BLG–BSG mixtures in the ratio of 10:1, 5:1, 2:1 & 1:2. Rheological behavior of BLG was found to be different from that of BSG and gelling point was raised during the heating period. By increasing BSG concentration, storage and loss moduli were increased and gel point was determined at about 80 °C, which was dependent of concentration and occurred during cooling period. Upon heating–cooling period (temperature sweep) of BLG–BSG mixture from 20 °C to 90 °C and coming back to original temperature, mixed gels presented a biphasic profile: the first phase, characterized by a sharp increase in the storage modulus in which gelation of BLG happened and the second phase exhibiting an increase in the storage modulus, corresponded to the build-up of a BSG network. Strain sweep results obtained for mixed gels at the end of the temperature sweep tests supported the biphasic hypothesis. The SEM results showed that BLG has a globular structure in comparison with BSG which has fibril and globular structure and the mean diameter of its globular structure was higher than that of BLG. Increasing the ratio of BSG to BLG resulted in a finer microstructure, which could retain higher water to form gel. In addition, microstructural study showed that BLG–BSG mixed is a bicontinuous network in which BSG dispersed in BLG continuous phase.     

Effects of the addition of sucrose and cellulose on the compression behaviour of ϰ-carrageenan gels

Influence of the concentration of sucrose and cellulose pulp on the compression behaviour of ϰ-carrageenan-based gels is studied. Composition of samples was established by using a second-order central composite design. Carrageenan concentrations used were between 0.5 and 1.25%, sucrose concentrations between 0 and 30% and cellulose fibre contents between 0 and 0.5%. Uniaxial compression behaviour was analysed by evaluating two parameters: maximum rupture strength (F_max) and apparent Young's modulus (E_ap). Results obtained showed that addition of sucrose increased both F_max and E_ap values while the effect of cellulose depended on the concentration of the other components.     

Influence of sugars on the characteristics of glucono-δ-lactone-induced soy protein isolate gels

The effects of the reducing sugars (glucose and lactose) and the non-reducing sugar (sucrose), heated in combination with soy protein isolate (SPI) at neutral pH, on the physicochemical and rheological properties of SPI were determined. After formation of gels induced by glucono-δ-lactone (GDL), the textural profile and physicochemical bonds of the non-heated and heated SPI gels were investigated. The gelation of SPI was induced in three stages of processing that is similar to some tofu-making procedures. First, SPI was heated in the presence of sugars at neutral pH above the denaturation temperature of SPI; then gelation was induced by GDL at iso-electric pH and finally the acidic gels were heat treated again. Heat treatment with glucose at neutral pH resulted in SPI with higher glycation degree than with lactose, whereas SPI heat treated in the presence of sucrose was not glycated. GDL-induced gels of SPI glycated with glucose was more soluble in water than gels of SPI reacted with lactose, which in turn was more soluble than the control and gels of SPI heated in the presence of sucrose. This indicates a change in the net charge of proteins caused by the glycation reaction. Glucose and lactose had a protective effect on protein denaturation at neutral pH, albeit less than sucrose, resulting in GDL-induced gels with increased water holding capacity and reduced gel hardness than sucrose. Chemical analysis indicated that disulphide bonds were involved in maintaining the structure of the gels, and solubility profiles of gels in different buffers indicate that other types of covalent bonds besides disulphide bonds were formed in gels of glycated SPI, resulting in reduced gel elasticity.     

Effect of sodium caseinate and κ-carrageenan on binding and textural properties of pork muscle gels enhanced by microbial transglutaminase addition

Response surface methodology was used to investigate the main effects and interactions of sodium caseinate (SC, 0–2%), microbial transglutaminase (MTG, 0–0.6%) and carrageenan (CGN, 0–0.8%) on water binding, textural and colour characteristics of pork gels. Higher κ-carrageenan and sodium caseinate content favored hydration properties and thermal stability, yielding lower cooking loss and higher water holding capacity. Their addition also increased hardness of pork gels, but was unable to improve springiness or cohesiveness. Sodium caseinate either alone or in combination with MTG generally has been found to be inferior to κ-carrageenan for functionality in comminuted meat systems. Although MTG had no effect on binding properties it was found to increase strength of the gels at higher SC levels. Addition of SC and ic-carrageenan significantly altered colour, while no significant influence of MTG on gel colour parameters was observed.     

Effect of PLA lamination on performance characteristics of agar/κ-carrageenan/clay bio-nanocomposite film

Multilayer films composed of PLA and agar/κ-carrageenan/clay (Cloisite® Na⁺) nanocomposite films were prepared, and the effect of lamination of PLA layers on the performance properties such as optical, mechanical, gas barrier, water resistance, and thermal stability properties was determined. The tensile strength (TS) of the agar/κ-carrageenan/clay nanocomposite films (67.8 ± 2.1 MPa) was greater than that of PLA films (43.3 ± 3.6 MPa), and the water vapor permeability (WVP), water uptake ratio (WUR), and water solubility (WS) of the nanocomposite films were higher than those of PLA films. The film properties of the multilayer films exhibited better properties of the component film layers. Especially, the WVP and water resistance of the bionanocomposite film were improved significantly, while the OTR of the PLA film decreased profoundly after lamination with PLA layers. Thermal stability of the bionanocomposite also increased after lamination with PLA layers.     

Binding and textural properties of beef gels processed with κ-carrageenan, egg albumin and microbial transglutaminase

The combined influence of κ-carrageenan (κ-CGN, 0.5%) and egg albumin (EA, 2%) on quality characteristics of beef gels processed without or with 0.5% microbial transglutaminase (MTG) was investigated. Beef gel properties were determined by measuring textural, hydration and colour characteristics. κ-Carrageenan favourably affected hydration properties and thermal stability, yielding lower cooking loss, purge and expressible moisture. It also increased hardness and fracturability of beef gels, but was unable to improve springiness or cohesiveness. Egg albumin either alone or in combination with MTG generally has been found to be inferior to κ-carrageenan for functionality in comminuted meat systems. Addition of EA produced an increase in lightness and yellowness, and a decrease in redness of beef gels, while the presence of κ-carrageenan resulted in lower L(?) and b(?), and higher a(?) values. No significant influence of MTG on gel colour parameters was observed.     

Influence of shearing on the physical characteristics and rheological behaviour of an aqueous whey protein isolate–κappa-carrageenan mixture

The incompatibility of whey protein isolate (WPI) and κappa-carrageenan (κ-car) in aqueous mixtures has been extensively studied under quiescent conditions; however, the effect of shear on segregative phase separation is still not fully understood. The present work reports for the first time quantitatively the effect of shearing on the segregative phase separation behaviour of these two polymers. Demixing was observed at pH 7.0 and 22 °C, determining the phase diagram and rheological properties of the mixtures. Phase diagrams were derived after heating and cooling mixes at a constant shear rate (28 s⁻¹). The phase behaviour was compared to that of the same mixtures under quiescent conditions. The shearing process affects segregative phase separation, causing a shift in the position of the binodal towards lower concentrations of WPI. The bottom layer contained a higher ratio of WPI while the upper layer was enriched in κ-car. The addition of κ-car to WPI solutions led to a much stiffer heat-induced gel than that prepared with WPI heated in isolation. The height of the plateau of the final elastic modulus G′_∞(t) depends on the position of the system on the phase diagram. Using a selected tie line, the viscosity of different systems measured at 80 °C was more influenced by the amount of WPI, than by the κ-car concentration. Shear treatment of segregative phase separating systems offer a way to modulate the functional properties of the ingredients and the texture of the final product.     

Investigation of the consequences of ultrasound on the physicochemical,emulsification, and gelatinization characteristics of citric acid–treated whey protein isolate

The effect of ultrasound (US) pretreatment (0, 200, 400, 600, and 800 W) on the physicochemical, emulsification, and gelatinization characteristics of citric acid (CA)-treated whey protein isolate (WPI) was investigated. Size exclusion chromatography demonstrated that when compared with untreated WPI, US pretreatment promoted production of more molecular polymers in the CA-treated WPI. There was a reduction in particle size of CA-treated WPI with the increase of US power (0–800 W), whereas its free sulfhydryl content, surface hydrophobicity, and intrinsic fluorescence strength increased. Furthermore, compared with untreated WPI, emulsifying ability index and emulsifying stability index of CA-treated WPI were increased by 14.04% and 10.10%, respectively, at 800 W. Accordingly, US pretreatment promoted the gel formation of CA-treated WPI, and its gel hardness was increased by 28.0% with US power ranging from 0 to 800 W. Therefore, US and CA treatment can be considered as an effective way to improve the emulsifying and gelatinization characteristics of WPI.     

Pilot-scale formation of whey protein aggregates determine the stability of heat-treated whey protein solutions—Effect of pH and protein concentration

Denaturation and consequent aggregation in whey protein solutions is critical to product functionality during processing. Solutions of whey protein isolate (WPI) prepared at 1, 4, 8, and 12% (wt/wt) and pH 6.2, 6.7, or 7.2 were subjected to heat treatment (85°C × 30 s) using a pilot-scale heat exchanger. The effects of heat treatment on whey protein denaturation and aggregation were determined by chromatography, particle size, turbidity, and rheological analyses. The influence of pH and WPI concentration during heat treatment on the thermal stability of the resulting dispersions was also investigated. Whey protein isolate solutions heated at pH 6.2 were more extensively denatured, had a greater proportion of insoluble aggregates, higher particle size and turbidity, and were significantly less heat-stable than equivalent samples prepared at pH 6.7 and 7.2. The effects of WPI concentration on denaturation/aggregation behavior were more apparent at higher pH where the stabilizing effects of charge repulsion became increasingly influential. Solutions containing 12% (wt/wt) WPI had significantly higher apparent viscosities, at each pH, compared with lower protein concentrations, with solutions prepared at pH 6.2 forming a gel. Smaller average particle size and a higher proportion of soluble aggregates in WPI solutions, pre-heated at pH 6.7 and 7.2, resulted in improved thermal stability on subsequent heating. Higher pH during secondary heating also increased thermal stability. This study offers insight into the interactive effects of pH and whey protein concentration during pilot-scale processing and demonstrates how protein functionality can be controlled through manipulation of these factors.     

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

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