Effect of pH and heat treatment conditions on physicochemical and acid gelation properties of liquid milk protein concentrate.

Milk protein concentrates (MPC) are typically dried high-protein powders with functional and nutritional properties that can be tailored through modification of processing conditions, including temperature, pH, filtration, and drying. However, the effects of processing conditions on the structure-function properties of liquid MPC (fluid ultrafiltered milk), specifically, are understudied. In this report, the pH of liquid MPC [13% protein (70% protein DM basis), pH 6.7] was adjusted to 6.5 or 6.9, and samples at pH 6.5, 6.7, and 6.9 were subjected to heat treatment at either 85°C for 5 min or 125°C for 15 s. Sodium dodecyl sulfate PAGE was used to determine the distribution of caseins and denatured whey proteins in the soluble and micellar phases, and HPLC was used to quantify native whey proteins as a measure of denaturation, based on the processing conditions. Both heat treatments resulted in substantial whey protein denaturation at each pH, with ß-lactoglobulin denatured more extensively than α-lactalbumin. Changes in liquid MPC physicochemical properties were monitored at d 1, 5, and 8 during storage at 4°C. Viscosity increased after heat treatment and also over time, regardless of pH and heating conditions, suggesting the role of whey protein denaturation and aggregation, and their interactions with casein micelles. The MPC samples processed at pH 6.9 had a significantly higher viscosity than those heated at pH 6.5 or 6.7, for both temperature and time conditions; and samples processed at 85°C for 5 min had higher viscosity than those heated at 125°C for 15 s. Particle size analysis indicated the presence of larger particles after 5 and 8 d of MPC storage after heating at pH 6.9. Acid-induced gelation of the liquid MPC led to significantly higher gel firmness after processing at 85°C for 5 min, compared with 125°C for 15 s. Also, gels made from MPC adjusted to pH 6.5 had higher storage moduli, with both time and temperature combinations, demonstrating the role of pH-dependent association of denatured whey proteins with casein micelles in gel network formation. These findings enable a better understanding of the processing factors contributing to structural and functional properties of liquid MPC and can be helpful in tailoring milk protein ingredient functionality for a variety of food products.

Short communication: Determination of the whey protein index in milk protein concentrates.

Milk protein concentrates are common ingredients in the dairy industry, with varying processing histories and composition. The objective of this research was to determine the feasibility of using the whey protein nitrogen (WPN) index, a well-established index for skim milk powder and nonfat dry milk, as a quality parameter for milk protein concentrates. The WPN index is a value based on the moisture-adjusted weight of skim milk powder. We hypothesized that WPN, even when standardized based on protein, may change depending on solubilization conditions of milk protein concentrates because of differences in solubilization conditions or processing history. The WPN was measured for model concentrates with different thermal history or reconstitution conditions. The WPN was not affected by an increased concentration of soluble casein in the dispersions nor after solubilization of the powder at 22 or 60°C. All reconstituted samples were standardized for protein. The WPN was also in full accordance with residual native protein measured by chromatography.

Influence of the emulsion droplet type on the rheological characteristics and microstructure of rennet gels from reconstituted milk.

Rheological and microstructural properties of rennet-induced milk gels containing different fat globules were studied. Recombined milks were prepared by mixing reconstituted low-heat skim milk powder and anhydrous milk fat emulsified with reconstituted skim milk powder (SMP), sodium caseinate (NaCas), whey protein isolate (WPI) or Tween 20. Final elastic modulus of the rennet gels containing WPI- or Tween 20-stabilized fat globules showed significantly lower values compared with those prepared with SMP-emulsified fat globules. SMP-stabilized fat globules interacted with the continuous casein network reinforcing the gel structure. Confocal micrographs supported the rheological data revealing that gels containing SMP-stabilized fat globules formed a tighter network relative to other treatments. Microscopy images also showed some degree of droplet flocculation in the case of gels containing WPI- or Tween 20-stabilized fat globules, and this was most likely the cause of the increase of elastic modulus of these systems. Contrary to reports for acid-induced casein gels, NaCas-stabilized fat globules hindered the formation of rennet gels. These results illustrate that rennet gel structure is affected by droplet-droplet and droplet-casein interactions, which in turn are determined by the composition of the oil-water interface as well as the ionic equilibrium in the reconstituted milk gels.

The impact of the concentration of casein micelles and whey protein-stabilized fat globules on the rennet-induced gelation of milk.

The rennet-induced aggregation of skim milk recombined with whey protein-stabilized emulsion droplets was studied using diffusing wave spectroscopy (DSW) and small deformation rheology. The effect of different volume fractions of casein micelles and fat globules was investigated by observing changes in turbidity (1/l*), apparent radius, elastic modulus and mean square displacement (MSD), in addition to confocal imaging of the gels. Skim milk containing different concentration of casein micelles showed comparable light-scattering profiles; a higher volume fraction of caseins led to the development of more elastic gels. By following the development of 1/l* in recombined milks, it was possible to describe the behaviour of the fat globules during the initial stages of rennet coagulation. Increasing the volume fraction of fat globules showed a significant increase in gel elasticity, caused by flocculation of the oil droplets. The presence of flocculated oil globules within the gel structure was confirmed by confocal microscopy observations. Moreover, a lower degree of kappa-casein hydrolysis was needed to initiate casein micelles aggregation in milk containing whey protein-stabilized oil droplets compared to skim milk. This study for the first time clearly describes the impact of a mixture of casein micelles and whey protein-stabilized fat globules on the pre-gelation stages of rennet coagulation, and further highlights the importance of the flocculation state of the emulsion droplets in affecting the structure formation of the gel.

Diffusing wave spectroscopy study of the colloidal interactions occurring between casein micelles and emulsion droplets: comparison to hard-sphere behavior.

Understanding the underlying processes that govern interparticle interactions in colloidal systems is fundamental to predicting changes in their bulk properties. In this paper we discuss the colloidal behavior of casein micelles and protein-stabilized fat globules individually and in a mixture. The colloidal interactions were observed by transmission diffusing wave spectroscopy. The turbidity parameter, l*, and the diffusion coefficients of the samples studied were measured experimentally and compared to the theoretically calculated parameters for a hard-sphere system. The light scattering properties of casein micelles (volume fraction phi = 0.1-0.2) dispersed in milk permeate showed no deviation from the theoretically predicted model. Whey protein isolate (WPI)-stabilized emulsions (phi = 0.025-0.1) prepared either in milk permeate or in 5 mM imidazole buffer at pH 6.8 showed a behavior identical to that of the hard-sphere model. Similarly to the WPI-stabilized fat globules, the sodium caseinate (NaCas)-stabilized emulsions (phi = 0.025-0.1) prepared in milk permeate also showed resemblance to the theory. In contrast, NaCas-stabilized emulsions prepared in 5 mM imidazole buffer exhibited some discrepancy from the theoretically calculated parameters. The deviation from theory is attributed to the enhanced steric stabilization properties of these droplets in a low ionic strength environment. When recombined milks made from concentrated milk and WPI- and NaCas-stabilized droplets prepared in permeate (phi = 0.125-0.2) were studied, the experimental data showed a significant deviation from the theoretical behavior of a hard-sphere model due to mixing of two different species.