Effect of ionic strength on the heat-induced soy protein aggregation and the phase separation of soy protein aggregate/dextran mixtures

The effects of ionic strength on heat-induced aggregation of soy protein and phase separation of different soy protein aggregates with dextran were investigated. The increase of ionic strength accelerated protein aggregation as shown by an increase in turbidity, aggregate fraction and particle size of salt-induced aggregates (SA). Adding salt (NaCl) to the aggregates formed at the ionic strength of zero (non-salt aggregates, non-SA), the increase of aggregate size was also found. Zeta potential results evidenced the charge screening effects of NaCl. The results of phase diagrams indicated that the compatibility of mixtures at higher ionic strength was lower than those at lower ionic strength, and SA was more incompatible with dextran than non-SA. The effects of the increase of aggregate size on the phase separation outweighed the ionic strength, which indicated that the depletion interaction also played an important role in the phase separation of soy protein aggregates and dextran. CLSM (Confocal Laser Scanning Microscopy) and rheological observations provided additional information of the microstructures of the mixtures.     

Interfacial dynamic properties of whey protein concentrate/polysaccharide mixtures at neutral pH

The effect of two non-surface active polysaccharides (sodium alginate, SA, and λ-carrageenan, λ-C) in the aqueous phase on the surface dynamic properties (dynamic surface pressure and surface dilatational properties) of a commercial milk whey protein concentrate (WPC) adsorbed film at the air–water interface has been studied. A whey protein isolate (WPI) was used as reference. The WPC and WPI concentration (at 1.0% wt), temperature (at 20 °C), pH (7), and ionic strength (at 0.05 M) were maintained constant, while the effect of polysaccharide (PS) was evaluated within the concentration range 0.0–1.0% wt. The surface dynamic properties of the adsorbed films were measured in an automatic pendant drop tensiometer. At short adsorption time and in the presence of PS, the rate of diffusion of WPC to the interface was affected by the interactions with PS in the aqueous phase, which could limit protein availability for the adsorption. On the other hand, at long-term adsorption, the magnitudes of the molecular penetration and configurational rearrangement rates of WPC in mixed systems (WPC/PS) reflected the viscoelastic characteristics of the adsorbed films. The attractive interactions between WPC and PS and/or the WPC aggregation in the presence of PS, which depend on the proper polysaccharide and its concentration in the aqueous phase, have an effect on the adsorption kinetic parameters, the amount of WPC adsorbed at the air–water interface, and the dilatational viscoelastic characteristics of WPC/PS mixed systems.     

The effects of sodium alginate and calcium levels on pea proteins cold-set gelation

A multi-scale investigation of pea proteins – alginate cold-set gels was proposed in this study. The gel preparation followed a two-steps procedure. Globular pea proteins were first denatured and aggregated by a pre-heating step. Sodium alginate was then added at different concentrations. Thereafter the in situ gelation process was induced at 20 °C using glucono-δ-lactone (GDL) and two calcium carbonate (CC) levels; calcium cations were released as the pH decreased. Small-amplitude rheology measurements (storage modulus G′) showed that stronger mixed gels were obtained than single-biopolymer solutions. Confocal laser scanning microscopy (CLSM) revealed phase-separating microstructures of mixed gels, foremost owing to biopolymers incompatibility. Phase separation was kinetically entrapped by gelation at different evolution stages. According to the co-occurrence method and microstructure classification, image texture analysis disclosed that a continuous protein network dispersing small gelled alginate microdomains corresponded to the strongest mixed gels. Transmission electron microscopy (TEM) evidenced that during gelation, the pre-aggregated proteins were mainly associated into large agglomerates with no peculiar pattern. Higher cohesiveness between both networks was hypothesized, since protein agglomerates could expose “anchoring points” for alginate chains. Depending on both protein – alginate initial composition and calcium availability, non-specific inter-biopolymer cross-links via calcium were assumed to be the key factor of synergism within mixed gels.     

The effect of the pH at cooking on the properties of processed cheese spreads containing whey proteins

Processed cheese spreads were made with and without whey proteins under varying cooking pH conditions. The processed cheeses were cooked at one pH value and at the end of the cooking process the pH was adjusted to the final product pH of 5.7. The rheological properties and whey protein denaturation levels of the processed cheese spreads were measured. The rheological properties and texture of the processed cheeses containing whey proteins could be markedly modified by varying the cooking pH during processing, whereas those without whey proteins were unaffected. These textural modifications could not be explained solely by the changes in whey protein denaturation during cooking. It is proposed that the interactions of the whey proteins during cooking affect the processed cheese texture, and that these interactions are affected by the pH of the processed cheese during processing.     

Effect of protein supplementation on the rheological characteristics of milk permeates fermented with exopolysaccharide-producing Lactococcus lactis subsp. cremoris

This research studied the effect of addition of whey proteins on the rheological properties of ultrafiltration permeate fermented with the exopolysaccharide (EPS)-producing strain Lactococcus lactis subsp. cremoris JFR1. Milk permeates containing 8% solids and various levels of added whey proteins (0, 2, 4, 6 and 8%) were fermented for 12 h at 30 °C. The rheological properties of the fermented samples were then evaluated and compared to controls fermented with a non-EPS producing strain. Scanning electron microscopy was also employed to confirm the existence of interactions between whey protein aggregates and EPS. The presence of EPS considerably increased the viscosity and viscoelastic properties of the media, especially in samples containing >2% whey protein added. The results obtained demonstrate the importance of EPS–protein interactions in structure formation and may help explain the viscosifying mechanism of EPS in fermented dairy products. Production of highly viscous material could potentially be employed in the future as a novel fiber-rich functional ingredient in dairy products.