The objective of the study reported in this research paper was to produce micellar casein concentrate (MCC) and milk protein concentrate (MPC) with 80% crude protein relative to total solids (TS) using MF and UF processes respectively. Additionally, capillary gel electrophoresis (CGE) was used to study the protein fractions in retentate and permeate. For MCC production, 227 L of pasteurized SM was subjected to MF using 0.5-micron spiral wound polyvinylidene fluoride membrane. During the process, diafiltration (DF) water was added at six intervals, totaling 100% of the feed volume. For MPC production, 227 L of pasteurized SM from the same lot was subjected to UF using 10 kDa Polyethersulfone membranes. During the process, DF water was added at four different intervals, with a final total addition of 40% of the feed volume. Both processes used a volume reduction of five. There were significant (p < 0.05) differences in all of the compositional parameters, except fat and casein for the MF retentate (MFR) and UF retentate (UFR). UFR had a higher crude protein (CP), TS, lactose, ash and calcium content as compared to MFR and this affected the CP/TS ratio found in both the retentates. The differences in membrane pore sizes, operating pressures and level of DF used all contributed to the differences in final CP/TS ratio obtained. The CGE analysis of individual protein fractions present in the UFR and MFR showed that UFR has a β-lactaglobulin to α-lactalbumin (α-LA) ratio similar to SM, whereas the MFR has a higher ratio, indicating preferential transmission for α-LA by the MF membrane. The results from this study show that MF and UF processes could be used for production of MCC and MPC with similar CP/TS ratio with careful selection of operating parameters, and that CGE can be used for detailed analysis of various protein fractions.

Hyaluronic acid (HA) is now widely known for its ability to bind water and impart texture. The combined effects of HA and kappa-carrageenan (KC) have not yet been investigated, though. In this study, we looked at the synergistic effects of HA and KC (concentrations of 0.1 and 0.25%, and ratios of 85:15, 70:30, and 50:50 for each concentration) on the rheological properties, heat stability, protein phase separation, water-holding capacity, emulsification properties, and foaming properties of skim milk. When HA and KC were combined in various ratios with a skim milk sample, this resulted in lesser protein phase separation and a higher water-holding capacity than when HA and KC were utilized separately. Similarly, for the sample with a 0.1% concentration, the combination of HA + KC blends demonstrated a synergistic impact with greater emulsifying activity and stability. The samples with a concentration of 0.25% did not exhibit this synergistic effect, and the emulsifying activity and stability were mostly due to the HA’s higher emulsifying activity and stability at 0.25% concentration. Similarly, for rheological (apparent viscosity, consistency coefficient K, and flow behavior index n) and foaming properties, the synergistic effect of the HA + KC blend was not readily apparent; rather, these values were mostly due to an increase in the amount of KC in the HA + KC blend ratios. When HC-control and KC-control samples were compared to various HA + KC mix ratios, there was no discernible difference in the heat stability. With the added benefits of protein stability (reduced phase separation), increased water-holding capacity, improved emulsification capabilities, and foaming abilities, the combination of HA + KC would be highly helpful in many texture-modifying applications.

The amount of intact casein provided by dairy ingredients is a critical parameter in dairy-based imitation mozzarella cheese (IMC) formulation because it has a significant effect on unmelted textural parameters such as hardness. From a functionality perspective, rennet casein (RCN) is the preferred ingredient. Milk protein concentrate (MPC) and micellar casein concentrate (MCC) cannot provide the required functionality due to the higher steric stability of casein micelle. However, the use of transglutaminase (TGase) has the potential to modify the surface properties of MPC and MCC and may improve their functionality in IMC. The objective of this study was to determine the effect of TGase-treated MPC and MCC powders on the unmelted textural properties of IMC and compare them with IMC made using commercially available RCN. Additionally, we studied the degree of crosslinking by TGase in MPC and MCC retentates using capillary gel electrophoresis. Three lots of MCC and MPC retentate were produced from pasteurized skim milk via microfiltration and ultrafiltration, respectively, and randomly assigned to 1 of 3 treatments: no TGase (control); low TGase: 0.3 units/g of protein; and high TGase: 3.0 units/g of protein, followed by inactivation of enzyme (72°C for 10 min), and spray drying. Each MCC, MPC, and RCN was then used to formulate IMC that was standardized to 21% fat, 1% salt, 48% moisture, and 20% protein. The IMC were manufactured by blending, mixing, and heating ingredients (4.0 kg) in a twin-screw cooker. The capillary gel electrophoresis analysis showed extensive inter- and intramolecular crosslinking. The IMC formulation using the highest TGase level in MCC or MPC did not form an emulsion because of extensive crosslinking. In MPC with a high level of TGase, whey protein and casein crosslinking were observed. In contrast, crosslinking and hydrolysis of proteins were observed in MCC. The IMC made from MCC powder had significantly higher texture profile analysis hardness compared with the corresponding MPC powder. Further, many-to-one (multiple) comparisons using the Dunnett test showed no significant differences between IMC made using RCN and treatment powders in hardness. Our results demonstrated that TGase treatment causes crosslinking hydrolysis of MCC and MPC at higher TGase levels, and MPC and MCC have the potential to be used as ingredients in IMC applications.

Melt and stretch properties in dairy-based imitation mozzarella cheese (IMC) are affected by the amount of intact casein provided by dairy ingredients in the formulation. Rennet casein (RCN) is the preferred ingredient to provide intact casein in a formulation. Ingredients produced using membrane technology, such as milk protein concentrate (MPC) and micellar casein concentrate (MCC), are unable to provide the required functionality. However, the use of transglutaminase (TGase) has potential to modify the physical properties of MPC or MCC and may improve their functionality in IMC. The objective of this study was to determine the effect of TGase-treated MPC and MCC retentates on melt and stretch properties when they are used in IMC and to compare them with IMC made using RCN. The MCC and MPC retentates were produced using 3 different lots of pasteurized skim milk and treated with 3 levels of TGase enzyme: no TGase (control), low TGase: 0.3 units/g of protein, and high TGase: 3.0 units/g of protein. Each of the MCC and MPC treatments was heated to 72°C for 10 min to inactivate TGase and then spray dried. Each MCC, MPC, and RCN powder was then used in an IMC formulation that was standardized to 48% moisture, 21% fat, 20% protein, and 1% salt. The IMC were manufactured in a twin-screw cooker by blending, mixing, and heating various ingredients (4.0 kg). Due to extensive crosslinking, the IMC formulation with the highest TGase level (MCC or MPC) did not form an emulsion. The IMC made from MCC treatments had significantly higher stretchability on pizza compared with their respective MPC treatments. The IMC made from TGase-treated MCC and MPC had significantly lower melt area and significantly higher transition temperature (TT) and stretchability compared with their respective controls. Comparison of IMC made using TGase-treated MCC and MPC to the RCN IMC indicated no difference in TT or texture profile analysis-stretchability; however, the Schreiber melt test area was significantly lower. Our results demonstrated that TGase treatment modifies the melt and stretch characteristics of MCC and MPC in IMC applications, and TGase-treated MPC and MCC can be used to replace RCN in IMC formulations.