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Our objective was to determine the effects of dipotassium phosphate (DKP) addition, heat treatments (no heat, high temperature, short time [HTST]: 72°C for 15 s, and direct steam injection UHT: 142°C for 2.3 s), and storage time on the soluble protein composition and mineral (P, Ca, K) concentration of the aqueous phase around casein micelles in 7.5% milk protein-based beverages made with liquid skim milk protein concentrate (MPC) and micellar casein concentrate (MCC). Milk protein concentrate was produced using a spiral wound polymeric membrane, and MCC was produced using a 0.1-µm ceramic membrane by filtration at 50°C. Two DKP concentrations were used (0% and 0.15% wt/wt) within each of the 3 heat treatments. All beverages had no other additives and ran through heat treatment without coagulation. Ultracentrifugation (2-h run at 4°C) supernatants of the beverages were collected at 1, 5, 8, 12, and 15-d storage at 4°C. Phosphorus, Ca, and K concentrations in the beverages and supernatants were measured using inductively coupled plasma spectrometry. Protein composition of supernatants was measured using Kjeldahl and sodium dodecyl sulfate-PAGE. Micellar casein concentrate and MPC beverages with 0.15% DKP had higher concentrations of supernatant protein, Ca, and P than beverages without DKP. Protein, Ca, and P concentrations were higher in MCC supernatant than in MPC supernatant when DKP was added, and these concentrations increased over storage time, especially when lower heat treatments (HTST or no heat treatment) had been applied. Dipotassium phosphate addition caused the dissociation of α S -, β-, and κ-casein, and casein proteolysis products out of the casein micelles, and DKP addition explained over 70% of the increase in supernatant protein, P, and Ca concentrations. Dipotassium phosphate could be removed from 7.5% of protein beverages made with fresh liquid MCC and MPC (containing a residual lactose concentration of 0.6% to 0.7% and the proportional amount of soluble milk minerals), as these beverages maintain heat-processing stability without DKP addition., (The Authors. Published by Elsevier Inc. and Fass Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).)

Our objective was to determine the effect of addition of dipotassium phosphate (DKP) at 3 different thermal treatments on color, viscosity, and sensory properties of 7.5% milk protein-based beverages during 15 d of storage at 4°C. Micellar casein concentrate (MCC) and milk protein concentrate (MPC) containing about 7.5% protein were produced from pasteurized skim milk using a 3×, 3-stage ceramic microfiltration process and a 3×, 3-stage polymeric ultrafiltration membrane process, respectively. The MCC and MPC were each split into 6 batches, based on thermal process and addition of DKP. The 6 batches were no postfiltration heat treatment with added DKP (0.15%), no postfiltration heat without added DKP (0%), postfiltration high-temperature, short time (HTST) with DKP, postfiltration HTST without DKP, postfiltration direct steam injection with DKP, and postfiltration direct steam injection without DKP. The 6 MCC milk-based beverages and the 6 MPC milk-based beverages were stored at 4°C. Viscosity, color, and sensory properties were determined over 15 d of refrigerated storage. MCC- and MPC-based beverages at 7.5% protein with and without 0.15% added dipotassium phosphate were successfully run through an HTST and direct steam injection thermal process. The 7.5% protein MCC-based beverage contained a higher calcium and phosphorus content (2,425 and 1,583 mg/L, respectively) than the 7.5% protein MPC-based beverages (2,141 and 1,338 mg/L, respectively). Pasteurization (HTST) had very little effect on beverage particle size distribution, whereas direct steam injection thermal processing produced protein aggregates with medians in the range of 10 and 175 μm for MPC beverages. A population of casein micelles at about 0.15 μm was found in both MCC- and MPC-based beverages. Larger particles in the 175-μm range were not detected in the MCC beverages. In general, the apparent viscosity (AV) of MCC beverages was higher than MPC beverages. Added DKP increased the AV of both MCC- and MPC-based beverages, while increasing heat treatment decreased AV. The AV of beverages with DKP increased during 15 d of 4°C of storage for both MCC and MPC, whereas there was very little change in AV during storage without DKP and a similar effect was observed for sensory viscosity scores. The L value of beverages was higher with higher heat treatment, but DKP addition decreased L value and sensory opacity greatly. Sulfur-eggy flavors were detected in MPC beverages, but not MCC-based beverages., (The Authors. Published by Elsevier Inc. and Fass Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).)

The objective of this study was to determine the effect of adding low concentrations of calcium-binding salts on the prevention of low-temperature gelation in milk protein concentrates (MPC). The MPC were created by a combination of ultrafiltration and diafiltration, standardized from 14 to 17% (wt/vol) protein content and mixed with one of 5 calcium-binding salts (sodium citrate, sodium hexametaphosphate, sodium polyphosphate, sodium pyrophosphate, and sodium monophosphate) adjusted to a pH of 6.75. The flow properties, apparent viscosity, and gel strength were determined for MPC containing a wide range of calcium-binding salt concentrations. Low-temperature gelation occurred in MPC with 16.0% and higher protein content. Low-temperature gelation at 16.0% protein content was prevented by the addition of any of the 5 salts tested at low concentrations (0.30 mM or less; sodium citrate, sodium hexametaphosphate, sodium polyphosphate, sodium pyrophosphate or sodium monophosphate), with sodium polyphosphate and sodium monophosphate being the most consistent in preventing low-temperature gels. All MPC samples exhibited shear-thinning behavior (n = 0.52-0.72), which increased (lower n values) as the protein content increased and decreased by addition of salt. At concentrations of salt above 1.00 mM, thermally irreversible gels were observed with relative strength dependent on the salt and protein content., (© 2022, The Authors. Published by Elsevier Inc. and Fass Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).)

Milk protein concentrates (MPCs), which are produced from skim milk following a series of manufacturing steps including pasteurization, membrane filtration, evaporation and spray drying, represent a relatively new category of dairy ingredients. MPC powders mainly comprise caseins and whey proteins in the same ratio of occurrence as in milk. While bovine MPCs have applications as an ingredient in several protein enriched food products, technofunctional concerns, e.g., reduced solubility and emulsification properties, especially after long-term storage, limit their widespread and consistent utilization in many food products. Changes in the surface and internal structure of MPC powder particles during manufacture and storage occur via casein-casein and casein-whey protein interactions and also via the formation of casein crosslinks in the presence of calcium ions which are associated with diminishment of MPCs functional properties. The aggregation of micellar caseins as a result of these interactions has been considered as the main cause of insolubility in MPCs. In addition, the occurrence of lactose-protein interactions as a result of the promotion of the Maillard reaction mainly during storage of MPC may lead to greater insolubility. This review focuses on the solubility of MPC with an emphasis on understanding the factors involved in its insolubility along with approaches which may be employed to overcome MPC insolubility. Several strategies have been developed based on manipulation of the manufacturing process, along with composition, physical, chemical and enzymatic modifications to overcome MPC insolubility. Despite many advances, dairy ingredient manufacturers are still investigating technical solutions to resolve the insolubility issues associated with the large-scale manufacture of MPC.

Milk protein concentrate-85 (MPC85) is a dairy ingredient which has a diverse range of applications in food products. The technofunctional properties of two MPC85 samples having similar gross composition but different levels of native whey protein (WP), i.e., MPC85S1 and MPC85S2 with 16.6 and 6.0 g native WP/100 g protein, respectively, were compared. Rheometeric analysis showed that under an applied normal stress of 1.0-15.0 kPa, the compressibility, the air permeability and the cohesiveness of MPC85S2 was higher compared to MPC85S1. Differential scanning calorimetry showed that protein denaturation in MPC85S1 began at 63 °C while for MPC85S2 it began at 70 °C. The heat coagulation time (HCT at 140 °C) for 4.2% (w/v, on a protein basis) reconstituted MPC85S1 and MPC85S2 was 2.2 and 2.7 min, respectively. While a higher lightness for MPC85S1 was evidenced using colourimeter analysis, the colour stability on oven drying at 95 °C for MPC85S2 was higher than MPC85S1. The emulsion produced with MPC85S1 flocculated after 1 d and phase separation occurred after 14 d. In the case of MPC85S2, flocculation began after 4 d while phase separation was observed at 33 d. The viscosity of MPC85S2 (4.2% (w/v) protein) was higher than MPC85S1. This study showed differences between the flowability, viscosity, colour properties, thermal stability (in powder and in reconstituted format), emulsification and buffering capacity for MPC samples having two different levels of WP denaturation. The results demonstrated that the MPCs studied having two different levels of WP denaturation could be targeted for different functional applications. The minimal/maximum level of denaturation required to induce technofunctional property differences requires further study., (Copyright © 2021 The Author(s). Published by Elsevier Ltd.. All rights reserved.)

The solubility of high-protein milk protein concentrate (MPC) may decrease significantly during storage, particularly at relatively high temperatures and humidity. The objective of this study was to seek correlations between the solubility loss of MPC during storage and various surface characteristics determined on the basis of simultaneous nanoscale topographical imaging and nanomechanical mapping of MPC particle surfaces using atomic force microscopy. A control MPC and a calcium-depleted MPC were stored at 45°C and 66% relative humidity for up to 60 d. The solubility of the control MPC was 56% at the beginning of the storage and gradually decreased to 10% at the end of the 60-d storage. The calcium-depleted MPC exhibited more rapid decreases from almost 100% at the beginning of the storage to 18% after storage for 45 d, after which we observed no significant difference in solubility between the control and calcium-depleted MPC. Averaged or root mean squared roughness values calculated using topographical images were found to have no correlation with the solubility. Deformation, Derjaguin-Muller-Toropov modulus, and adhesion images revealed the presence of individual casein micelles and larger clusters of aggregated casein micelles at MPC particle surfaces, whereas we observed no correlation between the solubility and averaged values of these nanomechanical properties. Furthermore, Derjaguin-Muller-Toropov modulus and adhesion images showed that the peripheral edges of individual casein micelles and their clusters had significantly higher values of the corresponding nanomechanical properties than other regions in the images, indicating the occurrence of the fusion of casein micelles. The surface area coverage or the percent area of the fused regions in an image revealed significant negative linear correlations with the solubility for both the control and calcium-depleted MPC. The present results support the hypothesis that the fusion of casein micelles at MPC powder particle surfaces is a causative factor for the solubility loss of MPC during storage and in turn suggest that the solubility loss may be alleviated by inhibiting the formation of a crust or skin on powder particle surfaces., (Copyright © 2021 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

In this work, pressure-assisted enzymatic gelation was applied to milk proteins, with the goal of enhancing the structure and stability of pressure-created milk protein gels. High-pressure processing (HPP) at 600 MPa, 3 min, and 5°C was applied to milk protein concentrate (MPC) samples of 12.5% protein concentration, both in the absence and in the presence of calf chymosin [up to 60 IMCU (international milk-clotting units)/kg of milk] or camel chymosin (up to 45 IMCU/kg of milk). Gel hardness, water-holding capacity, and degree of proteolysis were used to assess network strength and shelf stability. The processing trials and all measurements were conducted in triplicate. Statistical analyses of the data were performed by ANOVA, at a 95% confidence level. After HPP treatment, we observed significant structural changes for all samples. Pressurization of MPC, with or without chymosin addition, led to extensive protein aggregation and network formation. The strength of HPP-created milk protein gels without chymosin addition, as measured by the elastic modulus (G'), had a value of 2,242 Pa. The value of G' increased with increasing chymosin concentration, reaching as high as 4,800 Pa for samples with 45 IMCU/kg of camel chymosin. During 4 wk of refrigerated storage, the HPP and chymosin MPC gels maintained higher gel hardness and better structural stability compared with HPP only (no chymosin) MPC gels. The water-holding capacity of the gels without chymosin remained at 100% during 28 d of refrigerated storage. The HPP and chymosin MPC gels had a lower water-holding capacity (91-94%) than the HPP-only counterparts, but their water-holding capacity did not decrease during storage. Overall, these findings demonstrate that controlled, fast structural modification of high-concentration protein systems can be obtained by HPP-assisted enzymatic treatment, and the created gels have a strong, stable network. This study provides insights into the possibility of using HPP for the development of milk-protein-based products with novel structures and textures and long refrigerated shelf life, along with the built-in safety imparted by the HPP treatment., (The Authors. Published by Elsevier Inc. and Fass Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).)

In this study, we investigated the effect of pH and calcium on the structural properties of gels created by high-pressure processing (HPP, 600 MPa, 5°C, 3 min) of milk protein concentrate (MPC, 12.5% protein). The pH level of the MPC was varied between 6.6 and 5.1 by adding glucono-δ-lactone (GDL), and the calcium content was varied from 24 to 36 mg of Ca/g of protein by adding calcium chloride. The rheological properties and microstructure of the pressure-treated MPC were assessed. The pressurization treatments and analytical testing were conducted in triplicate. Data were analyzed statistically using one-way ANOVA with Tukey's honestly significant difference post hoc tests. A pressurization time of 3 min was sufficient to induce gel formation in MPC at pH 6.6, so it was used throughout the study. Adjusting either pH or calcium affected the structure of the HPP-created milk protein gels, likely by influencing electrostatic interactions and shifting the calcium-phosphate balance. Gels were formed after pressurization of MPC at pH above 5.3, and increasing the pH from 5.3 to 6.6 resulted in stronger gels with higher values of elastic moduli (G'). At neutral pH (6.6), adding calcium to MPC further increased G'. Scanning electron microscopy showed that reducing pH or adding calcium resulted in more porous, aggregated microstructures. These findings demonstrate the potential of HPP to create a variety of structures using MPC, facilitating a new pathway from dairy protein ingredients to novel, gel-based, high-protein foods, such as puddings or on-the-go protein bars., (Copyright © 2021 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Milk protein concentrate (MPC) is a preferred ingredient to provide nutritional and functional benefits in various dairy and food products. Altering the protein configuration and protein-protein interactions in MPC can provide a novel functionality and may open doors for new applications. The fibrilization process converts the globular structure of whey proteins to fibrils and consequently increases viscosity and water holding capacity compared with the native protein structure. The objective of the current work was to selectively convert the whey proteins in MPC as fibrils. For this purpose, simulated control model MPC was prepared by combining solutions of micellar casein concentrate (MCC) and milk whey protein isolate (mWPI) to give casein and whey protein in an 80:20 ratio. The mWPI solution was converted to fibrils by heating at low pH, neutralized, and combined with MCC solution similar to control model MPC and termed "fibrillated model MPC." Thioflavin T fluorescence value, transmission electron microscopy, and gel electrophoresis confirmed the fibril formation and their survival after neutralization and mixing with MCC. Further, the fibrillated mWPI showed significantly higher viscosity and consistency coefficient than nonfibrillated mWPI. Similarly, fibrillated model MPC showed significantly higher viscosity and consistency coefficient compared with control model MPC. Hence, the fibrillated model MPC can be used as ingredient to increase viscosity. Heat coagulation time was found to be significantly higher for control model MPC compared with fibrillated model MPC., (Copyright © 2021 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Optimizing protein intake for very low birth weight (<1,500 g) infants is fundamental to prevent faltering postnatal growth with the potential association of impaired neurodevelopment. The protein content of human milk is not sufficient to support the growth of very low birth weight infants. To meet their elevated protein requirements, human milk is currently fortified using typically bovine milk-based protein isolates (>85% on a dry basis). However, these products have several limitations for use in this vulnerable population. To overcome the shortcomings of bovine milk-based protein supplement, a human milk protein concentrate (HMPC) was developed. In preliminary attempts using 10 kDa ultrafiltration (UF) membranes, it was not possible to reach the protein content of commercial protein isolates, presumably due to the retention of human milk oligosaccharides (HMO). Consequently, it was hypothesized that the use of a UF membrane with a higher molecular weight cut-off (50 kDa rather than 10 kDa) could improve the transmission of carbohydrates, including HMO, in the permeate, thus increasing the protein purity of the subsequent HMPC. The results showed that permeate fluxes during the concentration step were similar to either UF molecular weight cut-off, but the 50-kDa membrane had a higher permeate flux during the diafiltration sequence. However, it was not sufficient to increase the protein purity of the human milk retentate, as both membranes generated HMPC with similar protein contents of 48.8% (10 kDa) and 50% (50 kDa) on a dry basis. This result was related to the high retention of HMO, mainly during the concentration step, although the diafiltration step was efficient to decrease their content in the HMPC. As the major bioactive proteins (lactoferrin, lysozyme, bile salt stimulated lipase, and α1-antitrypsin) in human milk were detected in both HMPC, the 50-kDa membrane seems the most appropriate to the preparation of HMPC in terms of permeation flux values. However, improving the separation of HMO from proteins is essential to increase the protein purity of HMPC., (Copyright © 2021 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Background: It is unknown whether protein supplementation can enhance recovery of exercise-induced muscle damage in older adults who have a disturbed muscle protein synthetic response. We assessed whether protein supplementation could attenuate exercise-induced muscle damage and soreness after prolonged moderate-intensity walking exercise in older adults., Methods: In a double-blind, placebo-controlled intervention study, 104 subjects (81% male, ≥65 years) used either a protein (n = 50) or placebo supplement (n = 54) during breakfast and directly after exercise. Within a walking event, study subjects walked 30/40/50 km per day on three consecutive days. Muscle soreness and fatigue were determined with a numeric rating scale, and creatine kinase (CK) concentrations and serum inflammation markers were obtained., Results: Habitual protein intake was comparable between the protein (0.92 ± 0.27 g/kg/d) and placebo group (0.97 ± 0.23 g/kg/d, p = 0.31). At baseline, comparable CK concentrations were found between the protein and the placebo group (110 (IQR: 84-160 U/L) and 115 (IQR: 91-186 U/L), respectively, p = 0.84). Prolonged walking (protein: 32 ± 9 km/d, placebo: 33 ± 6 km/d) resulted in a cumulative increase of CK in both the protein (∆283 (IQR: 182-662 U/L)) and placebo group (∆456 (IQR: 209-885 U/L)) after three days. CK elevations were not significantly different between groups ( p = 0.43). Similarly, no differences in inflammation markers, muscle soreness and fatigue were found between groups., Conclusions: Protein supplementation does not attenuate exercise-induced muscle damage, muscle soreness or fatigue in older adults performing prolonged moderate-intensity walking exercise., Competing Interests: The authors declare no conflicts of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.

Replacement of milk protein with protein isolates from vegetable resources can significantly influence the characteristics of feta whey less cheese and also decrease the cost of final production. In this study, various blends of milk protein concentrate (MPC) and pea protein isolate (PPI) were mixed at levels of 12% MPC and 0% PPI (MP0), 10% MPC and 2% PPI (MP2), 9% MPC and 3% PPI (MP3), 8% MPC and 4% PPI (MP4), 7% MPC and 5% PPI (MP5), 6% MPC and 6% PPI (MP6) and used in the manufacture of wheyless feta cheese. The chemical, textural, rheological, and sensorial properties, as well as the microstructure of the cheese samples, were evaluated after 1, 15, and 30 days of storage. The general linear model procedure of SAS statistical software was used for statistical analysis. Duncan's multiple range tests was used to compare the means of different treatments. The results showed that all properties of the cheeses were influenced by different levels of PPI due to different total solids content. The use of high concentrations of PPI resulted in a more open protein network, softer structure and decreasing the storage (G') and loss (G″) moduli in the cheeses. Sensory evaluation of the samples revealed that total score in terms of flavor, texture and overall acceptability was gradually decreased with increasing PPI levels, but still preferable for the panelists. Furthermore, for each sample, with increasing levels of PPI, the whiteness and the greenness were decreased, but the yellowness was increased., (© 2020 Wiley Periodicals, Inc.)

Low and high protein dairy powders are prone to caking and sticking and can also be highly insoluble; with powder storage conditions an important factor responsible for such issues. The aim of this study focused on the bulk and surface properties of anhydrous and humidified spray-dried milk protein concentrate (MPC) powders (protein content ~40, 50, 60, 70 or 80%, w/w). Water sorption isotherms, polarized light and scanning electron micrographs showed crystallized lactose in low protein powders at high water activities. High protein systems demonstrated increased bulk diffusion coefficients compared to low protein systems. Glass transition temperatures, α-relaxation temperatures and structural strength significantly decreased with water uptake. CLSM measurements showed that humidified systems have slower real time water diffusion compared to anhydrous systems. Overall, the rate of water diffusion was higher for low protein powders but high protein powders absorbed higher levels of water under high humidity conditions., (Copyright © 2019 Elsevier Ltd. All rights reserved.)

Background: Transglutaminase (TGase) catalyzes post-translational modification of proteins by γ-glutamyl-ϵ-lysine chain links, covalent conjugation of polyamines, and deamidation. Zea mays TGase (TGZ) is a plant TGase with potential application prospects in the food industry. In this study, two promoter types, P FLD1 and P TEF1 , were compared to improve the expression of TGZ, and the cross-linking effect of recombinant TGZ on the properties of acid-induced milk protein concentrate (MPC) gel was assessed., Results: A higher expression of TGZ was obtained under the induction of P FLD1 with a production of 635 U L -1 . After purification using chromatography, TGZ activity was 0.4 U mg -1 . The results indicated that TGZ treatment has effectively improved the textural properties of MPC gel at strength level and water-holding capacity. Optimal texture of MPC gel was achieved after TGZ treatment using 2 U g -1 TGZ for 2 h at 35 °C and pH 7., Conclusion: Comparative analysis of the promoters has greatly contributed to the production of TGZ in the industrial field. Furthermore, the modification of MPC gel texture by TGZ indicated that this recombinant enzyme has a practical value in dairy product, especially in yoghurt industry. © 2019 Society of Chemical Industry., (© 2019 Society of Chemical Industry.)

This study investigates the effects of pre-acidification (pH 6.7-5.4) of skim milk, followed by pH-restoration of the retentates, on spray-drying performance, physico-chemical properties and functionality of the resulting milk protein concentrate (MPC). Powder recovery decreased with decreasing pH of pre-acidification but improved with pH-restoration. Colloidal calcium was gradually solubilized with decreasing pH of pre-acidification but was slightly recovered by pH-restoration. Dissociation of micellar caseins increased with decreasing pH of pre-acidification of skim milk and was further increased by pH-restoration. Casein micelles maintained their overall structures at pre-acidification pH of 6.7-6.0, and partially disintegrated into loosely entangled aggregates at pH 5.7-5.4; while after pH-restoration, micelles generally maintained their overall structures at pre-acidification pH of 6.0, and completely disintegrated at pH 5.7-5.4. Solubility and emulsifying properties of MPC improved with decreasing pH of pre-acidification and with pH-restoration. Heat stability of MPC declined with decreasing pH of pre-acidification but improved with pH-restoration., (Copyright © 2018 Elsevier Ltd. All rights reserved.)

This study investigated the effects of dephosphorylation and sodium hexametaphosphate (SHMP) salt addition on the viscosity of milk protein concentrate (MPC) solutions. Dephosphorylation (DP) of casein was performed using bovine alkaline phosphatase. Nuclear magnetic resonance (NMR) spectra showed that dephosphorylation depleted the casein-bound phosphate region (CNP). SHMP addition (5 mM) had no impact on the 31 P NMR spectra of DP-MPC; addition of 5 mM SHMP to control MPC (C-MPC) resulted in a shift in peaks associated with the CNP region, possibly caused by SHMP sequestering calcium, leading to swelling of micelles. DP-MPC exhibited a lower viscosity compared to C-MPC, with SHMP addition at 12.5 and 25 mM causing gelation of C-MPC and DP-MPC solutions. This work confirmed the role that phosphate residues have in maintaining micelle structural stability and provides new insights into controlling viscosity of MPC solutions., (Copyright © 2018 Elsevier Ltd. All rights reserved.)

Because of their high protein and low lactose content, milk protein concentrates (MPC) are typically used in the formulation of ready-to-drink beverages. Calcium-mediated aggregation of proteins during storage is one of the main reasons for loss of storage stability of these beverages. Control and calcium-reduced MPC [20% calcium-reduced (MPC-20) and 30% calcium-reduced (MPC-30)] were used to evaluate the physicochemical properties in this study. This study was conducted in 2 phases. In phase I, 8% protein solutions were prepared by reconstituting the 3 MPC and adjusting the pH to 7. These solutions were divided into 3 equal parts, 0, 0.15, or 0.25% sodium hexametaphosphate (SHMP) was added, and the solutions were homogenized. In phase II, enteral dairy beverage formulations containing MPC and a mixture of gums, maltodextrin, and sugar were evaluated following the same procedure used in phase I. In both phases, heat stability, apparent viscosity, and particle size were compared before and after heat treatment at 140°C for 15 s. In the absence of SHMP, MPC-20 and MPC-30 exhibited the highest heat coagulation time at 30.9 and 32.8 min, respectively, compared with the control (20.9 min). In phase II, without any addition of SHMP, MPC-20 exhibited the highest heat coagulation time of 9.3 min compared with 7.1 min for control and 6.2 min for MPC-30. An increase in apparent viscosity and a decrease in particle size of reconstituted MPC solutions in phases I and II with an increase in SHMP concentration was attributed to casein micelle dissociation caused by calcium chelation. This study highlights the potential for application of calcium-reduced MPC in dairy-based ready-to-drink and enteral nutrition beverage formulations to improve their heat stability., (The Authors. Published by FASS Inc. and Elsevier Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).)

In recent years, a large increase in the production of milk protein concentrates (MPC) has occurred. However, compared with other types of milk powders, few studies exist on the effect of key processing parameters on powder properties. In particular, it is important to understand if key processing parameters contribute to the poor solubility observed during storage of high-protein MPC powders. Ultrafiltration (UF) and diafiltration (DF) are processing steps needed to reduce the lactose content of concentrates in the preparation of MPC with a protein content of 80% (MPC80). Evaporation is sometimes used to increase the TS content of concentrates before spray drying, and some indications exist that inclusion of this processing step may affect protein properties. In this study, MPC80 powders were manufactured by 2 types of concentration methods: membrane filtration with and without the inclusion of an evaporation step. Different concentration methods could affect the mineral content of MPC powders, as soluble salts can permeate the UF membrane, whereas no mineral loss occurs during evaporation, although a shift in calcium equilibrium toward insoluble forms may occur at high protein concentration levels. It is more desirable from an energy efficiency perspective to use higher total solids in concentrates before drying, but concerns exist about whether a higher protein content would negatively affect powder functionality. Thus, MPC80 powders were also manufactured from concentrates that had 3 different final protein concentrations (19, 21, and 23%; made from 1 UF retentate using batch recirculation evaporation, a similar concentration method). After manufacture, powders were stored for 6 mo at 30°C to help understand changes in MPC80 properties that might occur during shelf-life. Solubility and foaming properties were determined at various time points during high-temperature powder storage. Inclusion of an evaporation step, as a concentration method, resulted in MPC80 that had higher ash, total calcium, and bound calcium (of rehydrated powder) contents compared to concentration with only membrane filtration. Concentration method did not significantly affect the bulk (tapped) density, solubility, or foaming properties of the MPC powders. Powder produced from concentrate with 23% protein content exhibited a higher bulk density and powder particle size than powder produced from concentrate that had 19% protein. The solubility of MPC80 powder was not influenced by the protein content of the concentrate. The solubility of all powders significantly decreased during storage at 30°C. Higher protein concentrations in concentrates resulted in rehydrated powders that had higher viscosities (even when tested at a constant protein concentration). The protein content of the concentrate did not significantly affect foaming properties. Significant changes in the mineral content are used commercially to improve MPC80 solubility. However, although the concentration method did produce a small change in the total calcium content of experimental MPC80 samples, this modification was not sufficiently large enough (<7%) to influence powder solubility., (Copyright © 2018 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Milk protein concentrate (MPC) powders (∼81% protein) were made from skim milk that was heat treated at 72°C for 15 s (LHMPC) or 85°C for 30 s (MHMPC). The MPC powder was manufactured by ultrafiltration and diafiltration of skim milk at 50°C followed by spray drying. The MPC dispersions (4.02% true protein) were prepared by reconstituting the LHMPC and MHMPC powders in distilled water (LHMPC w and MHMPC w , respectively) or milk permeate (LHMPC p and MHMPC p , respectively). Increasing milk heat treatment increased the level of whey protein denaturation (from ∼5 to 47% of total whey protein) and reduced the concentrations of serum protein, serum calcium, and ionic calcium. These changes were paralleled by impaired rennet-induced coagulability of the MHMPC w and MHMPC p dispersions and a reduction in the pH of maximum heat stability of MHMPC p from pH 6.9 to 6.8. For both the LHMPC and MHMPC dispersions, the use of permeate instead of water enhanced ethanol stability at pH 6.6 to 7.0, impaired rennet gelation, and changed the heat coagulation time and pH profile from type A to type B. Increasing the severity of milk heat treatment during MPC manufacture and the use of permeate instead of water led to significant reductions in the viscosity of stirred yogurt prepared by starter-induced acidification of the MPC dispersions. The current study clearly highlights how the functionality of protein dispersions prepared by reconstitution of high-protein MPC powders may be modulated by the heat treatment of the skim milk during manufacture of the MPC and the composition of the solvent used for reconstitution., (Copyright © 2018 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

This study aimed to evaluate the effects of different concentration methods (nanofiltration and evaporation) and heat treatments on the gel properties of milk protein concentrate (MPC). The MPC gels were produced using glucono-δ-lactone (GDL) as an acidifier with different preheat treatments (30 min at 80°C and 5 min at 92°C). We then evaluated the effect of preheat treatments on MPC gel properties, including storage modulus (G'), loss tangent (tan δ), firmness, whey separation, and microstructure. The results indicated that without preheating, evaporation (EP)-MPC had higher G' and firmness, and lower tan δ and whey separation than nanofiltration (NF)-MPC. These results suggest that EP-MPC produced a better acid-induced gel than NF-MPC when no preheat treatments were performed. After preheating, however, except for a very small difference in the final G' (EP-MPC was higher), the 2 MPC did not differ significantly in firmness, final tan δ, or whey separation. Additionally, compared with the gel of unheated MPC, both preheat-treated gels (NF-MPC and EP-MPC) achieved increased G' and firmness and decreased tan δ and whey separation. The preheat-treated MPC also displayed a more flexible-stranded network. These findings demonstrate that, given a suitable heating treatment, NF-MPC compares favorably with EP-MPC in achieving desired gel properties., (Copyright © 2018 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Innovative clean label processes employed in the manufacture of acid gels are targeted to modify the structure of proteins that contribute to rheological properties. In the present study, CO 2 -treated milk protein concentrate powder with 80% protein in dry matter (TMPC80) was mixed with nonfat dry milk (NDM) in different ratios for the manufacture of acid gels. Dispersions of NDM and TMPC80 that provided 100, 90, 70, and 40% of protein from NDM were reconstituted to 4.0% (wt/wt) protein and 12.0% (wt/wt) total solids. Dispersions were adjusted to pH 6.5, followed by heat treatment at 90°C for 10 min. Glucono-δ-lactone was added and samples were incubated at 30°C, reaching pH 4.5 ± 0.05 after 4 h of incubation. Glucono-δ-lactone levels were adjusted to compensate for the lower buffering capacity of samples with higher proportions of TMPC80, which is attributable to the depletion of buffering minerals from both the serum and micellar phase during preparation of TMPC80. Sodium dodecyl sulfate-PAGE analysis indicated a higher amount of caseins in the supernatant of unheated suspensions with increasing proportions of CO 2 -treated TMPC80, attributable to the partial disruption of casein micelles in TMPC80. Heat treatment reduced the level of whey proteins in the supernatant due to the heat-induced association of whey proteins with casein micelles, the extent of which was larger in samples containing more micellar casein (i.e., samples with a lower proportion of TMPC80). Particle size analysis showed only small differences between nonheated and heated dispersions. Gelation pH increased from ˜5.1 to ˜5.3, and the storage modulus of the gels at pH 4.5 increased from ˜300 to ˜420 Pa when the proportion of protein contributed by TMPC80 increased from 0 to 60%. Water-holding capacity also increased and gel porosity decreased with increasing proportion of protein contributed by TMPC80. The observed gel properties were in line with microstructural observations by confocal microscopy, wherein sample gels containing increasing levels of TMPC80 exhibited smaller, well-connected aggregates with uniform, homogeneous pore sizes. We concluded that TMPC80 can be used to partially replace NDM as a protein source to improve rheological and water-holding properties in acid gels. The resultant gels also exhibited decreased buffering, which can improve the productive capacity of yogurt manufacturing plants. Overall, the process can be leveraged to reduce the amount of hydrocolloids added to improve yogurt consistency and water-holding capacity, thus providing a path to meet consumer expectations of clean label products., (Copyright © 2018 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Milk protein concentrate (MPC) powders are increasingly utilized in manufacturing of protein fortified beverages. Thermal stability of the protein dispersions is of significant importance in such applications. It is known that a decrease in pH can induce partial dissociation of casein micelles and modify the natural equilibrium of calcium and phosphate between the micelles and the serum phase. The presence of soluble casein may improve the rehydration properties of MPC powders, and may impact their thermal stability. The objective of this work was to investigate the effects of partial acidification of milk prior to ultrafiltration on the heat stability of reconstituted MPC dispersions. Milk protein concentrate powders were prepared from skim milk acidified to pH6.0 by addition of glucono-δ-lactone, and then concentrated using ultrafiltration (UF) and diafiltration (DF). The heat stability of the reconstituted MPC dispersions was studied, by determining heat coagulation time, particle size, turbidity, viscosity, soluble and colloidal calcium and phosphate, and non-sedimentable casein both before and after heating at 120°C. Reconstituted MPC powders made with partially acidified skim milk contained lower soluble calcium and phosphate and exhibited very poor thermal stability compared to MPC powders made with skim milk at its natural pH. The thermal stability of the acidified MPC dispersions was not only recovered by restoration of pH and the serum composition through dialysis against skim milk, but it was improved compared to control MPC dispersions. All dialyzed samples had comparable pH, protein content and calcium and phosphate concentration, but the structure of the casein micelles was altered, causing differences in the type of soluble aggregates. It was concluded that the integrity of the casein micelles and the amount of dissociated, non-sedimentable caseins play a major role in determining the thermal stability of the MPC dispersions., (Copyright © 2017. Published by Elsevier Ltd.)

Reconstituted micellar casein concentrates and milk protein concentrates of 2.5 and 10% (wt/vol) protein concentration were subjected to high-pressure processing at pressures from 150 to 450 MPa, for 15 min, at ambient temperature. The structural changes induced in milk proteins by high-pressure processing were investigated using a range of physical, physicochemical, and chemical methods, including dynamic light scattering, rheology, mid-infrared spectroscopy, scanning electron microscopy, proteomics, and soluble mineral analyses. The experimental data clearly indicate pressure-induced changes of casein micelles, as well as denaturation of serum proteins. Calcium-binding α S1 - and α S2 -casein levels increased in the soluble phase after all pressure treatments. Pressurization up to 350 MPa also increased levels of soluble calcium and phosphorus, in all samples and concentrations, whereas treatment at 450 MPa reduced the levels of soluble Ca and P. Experimental data suggest dissociation of calcium phosphate and subsequent casein micelle destabilization as a result of pressure treatment. Treatment of 10% micellar casein concentrate and 10% milk protein concentrate samples at 450 MPa resulted in weak, physical gels, which featured aggregates of uniformly distributed, casein substructures of 15 to 20 nm in diameter. Serum proteins were significantly denatured by pressures above 250 MPa. These results provide information on pressure-induced changes in high-concentration protein systems, and may inform the development on new milk protein-based foods with novel textures and potentially high nutritional quality, of particular interest being the soft gel structures formed at high pressure levels., (The Authors. Published by the Federation of Animal Science Societies and Elsevier Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).)

Unit operations during production influence the sensory properties of nonfat dry milk (NFDM) and milk protein concentrate (MPC). Off-flavors in dried dairy ingredients decrease consumer acceptance of ingredient applications. Previous work has shown that spray-drying parameters affect physical and sensory properties of whole milk powder and whey protein concentrate. The objective of this study was to determine the effect of inlet temperature and feed solids concentration on the flavor of NFDM and MPC 70% (MPC70). Condensed skim milk (50% solids) and condensed liquid MPC70 (32% solids) were produced using pilot-scale dairy processing equipment. The condensed products were then spray dried at either 160, 210, or 260°C inlet temperature and 30, 40, or 50% total solids for NFDM and 12, 22, or 32% for MPC70 in a randomized order. The entire experiment was replicated 3 times. Flavor of the NFDM and MPC70 was evaluated by sensory and instrumental volatile compound analyses. Surface free fat, particle size, and furosine were also analyzed. Both main effects (30, 40, and 50% solids and 160, 210, and 260°C inlet temperature) and interactions between solids concentration and inlet temperature were investigated. Interactions were not significant. In general, results were consistent for NFDM and MPC70. Increasing inlet temperature and feed solids concentration increased sweet aromatic flavor and decreased cardboard flavor and associated lipid oxidation products. Increases in furosine with increased inlet temperature and solids concentration indicated increased Maillard reactions during drying. Particle size increased and surface free fat decreased with increasing inlet temperature and solids concentration. These results demonstrate that increasing inlet temperatures and solids concentration during spray drying decrease off-flavor intensities in NFDM and MPC70 even though the heat treatment is greater compared with low temperature and low solids., (Copyright © 2016 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Transglutaminase (Tgase) crosslinking and calcium reduction were investigated as ways to improve the texture and storage stability of high-protein nutrition (HPN) bars formulated with milk protein concentrate (MPC) and micellar casein concentrate (MCC). The MPC and MCC crosslinked at none, low, and high levels, and a reduced-calcium MPC (RCMPC) were each formulated into model HPN bars. Hardness, crumbliness, moisture content, pH, color, and water activity of the HPN bars were measured during accelerated storage. The HPN bars prepared with MPC were harder and more cohesive than those prepared with MCC. Higher levels of Tgase crosslinking improved HPN bar cohesiveness and decreased hardening during storage. The RCMPC produced softer, yet crumblier HPN bars. Small textural differences were observed for the HPN bars formulated with the transglutaminase crosslinked proteins or RCMPC when compared with their respective controls. However, modification only slightly improved protein ingredient ability to slow hardening while balancing cohesion and likely requires further improvement for increased applicability in soft-texture HPN bars., (Copyright © 2016 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

A major deterrent to the usage of milk protein concentrate (MPC), a high-protein milk product with increasing demand as a food and sports drink ingredient, has been its poor functional characteristics when compared with other milk protein products such as whey protein concentrate and sodium caseinates. This review discusses the recent research on functional properties of MPC, focusing on factors that may contribute to the poor functional characteristics before, during, and after production. Current research, methods employed, and new understanding on the causes of poor solubility of MPC at mild temperatures (about 20°C) has been presented, including loss of solubility during storage as these areas have received unprecedented attention over the past decade, and also affects other useful functional properties of MPC, such as emulsifying properties, gelation, and foaming. Processing methods, which include heat treatment, high-pressure application, microwave heating, ultrasound application, and enzyme and salts modification, have been used or have potential to modify or improve the functional properties of MPCs. Future research on the effects of these processing methods on the functional properties, including effects of enzyme hydrolysis on bitterness and bioactivity, has also been discussed.

Processing, storage, dissolution conditions, and the composition of milk protein concentrates (MPC) affect the solubility of high-protein dairy powders. Increasing the storage temperature and time decrease the solubility of MPC and milk protein isolates (MPI). The MPC and MPI are popular ingredients in high-protein food products and have a variety of protein contents. In addition, the dissolution temperature has been shown to affect the solubility of the powders. This study focused on determining how protein content and dissolution temperature affect the solubility of MPC and MPI. For this study, 11 powders were obtained from a commercial manufacturer. The powders were classified as A, B, C, and D, and they had a mean protein content of 85, 87, 88, and 90%, respectively. A 5% (wt/wt) concentration of powder was dissolved in water at 40 and 48°C. The solubility of the MPC and MPI samples were characterized using an ultrasonic flaw detector (UFD) and focused beam reflectance measurement (FBRM). The UFD and FBRM data were collected every 15 and 10 s, respectively, for 1,800 s. At both dissolution temperatures, the UFD and FBRM data showed that the solubility decreased as the protein content increased. Powders A and B were found to be more soluble because they had a lower relative velocity standard deviation, high area under the attenuation curve, high peak height, and low peak time. With the FBRM, the fine and medium particle count decreased and large particle count increased as the protein content increased. Powders dissolved at 48°C typically had a lower relative velocity standard deviation, higher area under the attenuation curve, higher peak height, and lower peak time than the powders dissolved at 40°C. The FBRM showed that powders dissolved at 48°C reached a stable counts before the powders dissolved at 40°C. Overall, the study showed that increasing the protein content led to a reduction in solubility and increasing the dissolution temperature improved the solubility of the powders., (Copyright © 2016 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

This study investigated the effects of dephosphorylation extent on infant in vitro gastric clotting property and gastrointestinal digestibility of milk protein concentrate. Dephosphorylation was affected by phosphatase type and incubation pH. A series of milk protein concentrate with 0-69% dephosphorylation were obtained by incubation with calf intestinal alkaline phosphatase at pH 6.5 for 0-420 min. Both β- and αs1-caseins in the modified milk protein concentrate showed multiply dephosphorylated isoforms with different numbers of phosphate groups depending on the extent of dephosphorylation. With increased dephosphorylation of milk protein concentrate, the gastric clotting extent decreased and the gastrointestinal digestibility increased under infant in vitro conditions. These results suggested the potential of developing a dephosphorylated milk protein concentrate, with improved gastric clotting property and gastrointestinal digestibility, to simulate the multiply phosphorylated patterns of human casein and hence to further the humanization of infant formula on a molecular level., (Copyright © 2015 Elsevier Ltd. All rights reserved.)

Major problems associated with the fortification of soluble iron salts include chemical reactivity and incompatibility with other components. Milk protein concentrate (MPC) are able to bind significant amount of iron due to the presence of both casein and whey protein. MPC in its native state possess very poor solubility, therefore, succinylated derivatives of MPC (succ. MPC) were also used for the preparation of protein-iron complex. Preparation of the complex involved centrifugation (to remove insoluble iron), ultrafiltration (to remove unbound iron) and lyophilisation (to attain in dry form). Iron binding ability of MPC enhanced significantly (P<0.05) upon succinylation. Stability of bound iron from both varieties of complexes was monitored under different conditions encountered during processing. Higher stability (P<0.05) of bound iron was observed in succ. MPC-iron complex than native protein complex. This method could be adopted for the production of stable iron enriched protein, an organic iron source., (Copyright © 2015 Elsevier Ltd. All rights reserved.)

A previous study in our laboratory showed that addition of 150 mM NaCl or KCl into diafiltration water improved the solubility of freshly made milk protein concentrate 80 (MPC80). In the present study, the objectives were (1) to evaluate the solubility of NaCl- or KCl-treated MPC80 samples kept at varying temperatures and then stored for extensive periods at room temperature (21 °C ± 1 °C); and (2) to determine if MPC80 samples stored at different temperatures and protein conformation can be grouped or categorized together. Freshly manufactured MPC80 samples were untreated (control), processed with NaCl, or processed with KCl. One set of sample bags was stored at 4 °C; second and third sets of bags were kept at 25 °C and 55 °C for 1 mo (31 d) and then transferred to room temperature (21 °C ± 1 °C) storage conditions for 1 yr (365 d). Samples were tested for nitrogen solubility index (NSI) and for protein changes by Fourier-transform infrared (FTIR) spectroscopy. Analysis of variance results for NSI showed 2 significantly different groupings of MPC80 samples. The more soluble group contained samples treated with NaCl or KCl and stored at either 4 °C or 25 °C. These samples had mean NSI >97.5%. The less soluble groups contained all control samples, regardless of storage temperature, and NaCl- or KCl-treated samples stored at 55 °C. These samples had mean NSI from 39.5 to 58%. Within each of these groups (more soluble and less soluble), no significant differences in solubility were detected. Pattern recognition analysis by soft independent modeling of class analogy (SIMCA) was used to assess protein changes during storage by monitoring the amide I and amide II (1,700(-1) to 1,300 cm(-1)) regions. Dominant bands were observed at 1,385 cm(-1) for control, 1,551 cm(-1) for KCl-treated samples, and 1,694 cm(-1) for NaCl-treated samples. Moreover, SIMCA clustered the MPC80 samples stored at 4 °C separately from samples stored at 25 °C and 55 °C. This study demonstrates that (1) the addition of NaCl or KCl during MPC80 manufacture reduces the deleterious changes in solubility upon prolonged storage at 4 °C or 25 °C, and (2) the solubility of samples stored at 55 °C is poor irrespective of salt treatment., (Copyright © 2016 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Milk protein concentrates with more than 80% protein (that is, MPC80) are underutilized as the primary protein source in high-protein nutrition bars as they impart crumbliness and cause hardening during storage. High-protein nutrition bar texture changes are often associated with internal protein aggregations and macronutrient phase separation. These changes were investigated in model high-protein nutrition bars formulated with MPC80 and physically modified MPC80s. High-protein nutrition bars formulated with extruded MPC80s hardened slower than those formulated with toasted or unmodified MPC80. Extruded MPC80 had reduced free sulfhydryl group exposure, whereas measurable increases were seen in the toasted MPC80. High-protein nutrition bar textural performance may be related to the number of exposed free sulfhydryl groups in MPC80. Protein aggregations resulting from ingredient modification and high-protein nutrition bar storage were studied with sodium dodecyl sulfate polyacrylamide gel electrophoresis. Disulfide-based protein aggregations and changes in free sulfhydryl concentration were not consistently relatable to high-protein nutrition bar texture change. However, the high-protein nutrition bars formulated with extruded MPC80 were less prone to phase separations, as depicted by confocal laser scanning microscopy, and underwent less texture change during storage than those formulated with toasted or unmodified MPC80., (© 2016 Institute of Food Technologists®)

Processing conditions during ultrafiltration of skim milk influence properties of the casein micelle and thereby the physical properties of milk protein concentrate (MPC). The aim of the study was to establish the effects of pH adjustment of skim milk feed to obtain MPC with desired emulsification properties. The ultrafiltration was conducted using commercially pasteurized skim milk with the pH adjusted to 6.7 (control), 6.3, 5.9, or 5.5 at 15°C until a volume concentration factor of 5 was reached. Effects of pH adjustment on selected physico-chemical properties (Ca content, particle size, ζ-potential) and functionalities (solubility, heat stability, emulsification capacity, and stability) of MPC were determined. Lowering the feed pH solubilized colloidal calcium phosphate that substantially contributed to modifying the properties of casein. This caused a reduction in the particle size while increasing the net negative charge. The structural modifications in proteins were manifested in the Fourier transform infrared spectra. Subsequent concentration did not induce any further protein structural changes. Such modifications to the casein micelles and colloidal calcium phosphate negatively affected the solubility and heat stability of the corresponding MPC powders. However, the emulsion activity index improved only until the pH of the feed was lowered to 5.9 and declined when pH was dropped to 5.5, followed with the loss of stability. Readjusting the pH of MPC powder dispersions to 6.7 restored their surface properties and thereby their functionality. Lowering the feed pH also negatively affected the membrane performance by clogging the membrane pores and lowering the flux, particularly at pH 5.5. Adjusting pH to 5.9 produced MPC with optimum emulsifying properties with minimal influence on membrane performance., (Copyright © 2016 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Protein systems (PS) are routinely used by companies from Brazil and around the globe to improve the texture, yield, and palatability of processed foods. Understanding the synergistic behavior among the different protein structures of these systems during thermal treatment under the influence of pH can help to better define optimum conditions for products and processes. The interpretation of the reactions and interactions that occur simultaneously among the protein constituents of these systems as dispersions during thermal processing is still a major challenge. Here, using a rapid viscosity analyzer, we observed the rheological changes in the startup viscosities of 5 PS obtained by combining varying proportions of milk protein concentrate and whey protein concentrate under different conditions of pH (5.0, 6.5, and 7.0) and heat processing (85°C/15min and 95°C/5min). The solutions were standardized to 25% of total solids and 17% of protein. Ten analytical parameters were used to characterize each of the startup-viscosity ramps for 35 experiments conducted in a 2×3 × 5 mixed planning matrix, using principal component analysis to interpret behavioral similarities. The study showed the clear influence of pH 5.5 in the elevation of the initial temperature of the PS startup viscosity by at least 5°C, as well as the effect of different milk protein concentrate:whey protein concentrate ratios above 15:85 at pH 7.0 on the viscographic profile curves. These results suggested that the primary agent driving the changes was the synergism among the reactions and interactions of casein with whey proteins during processing. This study reinforces the importance of the rapid viscosity analyzer as an analytical tool for the simulation of industrial processes involving PS, and the use of the startup viscosity ramp as a means of interpreting the interactions of system components with respect to changes related to the treatment temperature., (Copyright © 2015 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Milk protein concentrate powders (MPC) with improved rehydration properties are often manufactured using processing steps, such as acidification and high-pressure processing, and with addition of other ingredients, such as sodium chloride, during their production. These steps are known to increase the amount of serum caseins or modify the mineral equilibrium, hence improving solubility of the retentates. The processing functionality of the micelles may be affected. The aim of this study was to investigate the effects of partial acidification by adding glucono-δ-lactone (GDL) to skim milk during membrane filtration on the structural changes of the casein micelles by observing their chymosin-induced coagulation behavior, as such coagulation is affected by both the supramolecular structure of the caseins and calcium equilibrium. Milk protein concentrates were prepared by preacidification with GDL to pH 6 using ultrafiltration (UF) and diafiltration (DF) followed by spray-drying. Reconstituted UF and DF samples (3.2% protein) treated with GDL showed significantly increased amounts of soluble calcium and nonsedimentable caseins compared with their respective controls, as measured by ion chromatography and sodium dodecyl sulfate-PAGE electrophoresis, respectively. The primary phase of chymosin-induced gelation was not significantly different between treatments as measured by the amount of caseino-macropeptide released. The rheological properties of the reconstituted MPC powders were determined immediately after addition of chymosin, both before and after dialysis against skim milk, to ensure similar serum composition for all samples. Reconstituted samples before dialysis showed no gelation (defined as tan δ=1), and after re-equilibration only control UF and DF samples showed gelation. The gelation properties of reconstituted MPC powders were negatively affected by the presence of soluble casein, and positively affected by the amount of both soluble and insoluble calcium present after reconstitution. This work, testing the chymosin-induced gelation behavior of various reconstituted MPC samples, clearly demonstrated that a decrease in pH to 6.0 during membrane filtration affects the integrity of the casein micelles supramolecular structure with important consequences to their processing functionality., (Copyright © 2015 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Dried milk protein concentrate is produced from skim milk using a combination of processes such as ultrafiltration (UF), evaporation or nanofiltration, and spray drying. It is well established that dried milk protein concentrate (MPC) that contains 80% (MPC80) and greater protein content (relative to dry matter) can lose solubility during storage as a result of protein-protein interactions and formation of insoluble complexes. Previous studies have shown that partial replacement of calcium with sodium improves MPC80 functionality and prevents the loss in solubility during storage. Those studies have used pH adjustment with the addition of acids, addition of monovalent salts, or ion exchange treatment of UF retentate. The objective of this study was to use carbon dioxide to produce MPC80 with improved functionality. In this study, reduced-calcium MPC80 (RCMPC) was produced from skim milk that was subjected to injection of 2,200 ppm of CO2 before UF, along with additional CO2 injection at a flow rate of 1.5 to 2 L/min during UF. A control MPC80 (CtrlMPC) was also produced from the same lot of skim milk without injection of CO2. The above processes were replicated 3 times, using different lots of skim milk for each replication. All the UF retentates were spray dried using a pilot-scale dryer. Skim milk and UF retentates were tested for ζ-potential (net negative charge), particle size, and viscosity. All the MPC were stored at room (22±1°C) and elevated (40°C) temperatures for 6 mo. Solubility was measured by dissolving the dried MPC in water at 22°C and at 10°C (cold solubility). Injection of CO2 and the resultant solubilization of calcium phosphate had a significant effect on UF performance, resulting in 10 and 20% loss in initial and average flux, respectively. Processing of skim milk with injection of CO2 also resulted in higher irreversible fouling resistances. Compared with control, the reduced-calcium MPC had 28 and 34% less ash and calcium, respectively. Injection of CO2 resulted in a significant decrease in ζ-potential and a significant increase in the size of the casein micelle. Moreover, RCMPC had a significantly higher solubility after storage at room temperature and at elevated temperature. This study demonstrates that MPC80 with a reduced calcium and mineral content can be produced with injection of CO2 before and during UF of skim milk., (Copyright © 2015 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Milk protein concentrates (MPCs) are complete dairy proteins (containing both caseins and whey proteins) that are available in protein concentrations ranging from 42% to 85%. As the protein content of MPCs increases, the lactose levels decrease. MPCs are produced by ultrafiltration or by blending different dairy ingredients. Although ultrafiltration is the preferred method for producing MPCs, they also can be produced by precipitating the proteins out of milk or by dry-blending the milk proteins with other milk components. MPCs are used for their nutritional and functional properties. For example, MPC is high in protein content and averages approximately 365 kcal/100 g. Higher-protein MPCs provide protein enhancement and a clean dairy flavor without adding significant amounts of lactose to food and beverage formulations. MPCs also contribute valuable minerals, such as calcium, magnesium, and phosphorus, to formulations, which may reduce the need for additional sources of these minerals. MPCs are multifunctional ingredients and provide benefits, such as water binding, gelling, foaming, emulsification, and heat stability. This article will review the development of MPCs and milk protein isolates including their composition, production, development, functional benefits, and ongoing research. The nutritional and functional attributes of MPCs are discussed in some detail in relation to their application as ingredients in major food categories., (© 2015 Institute of Food Technologists®)

The aim of this work was to evaluate the effects of nanofiltration and evaporation concentration technologies on the physiochemical properties of milk protein concentrate (MPC) during processing. Skim milk, ultrafiltered milk, evaporated milk, nanofiltered milk, evaporated MPC, and nanofiltered MPC samples were collected at different processing stages. Chemical composition, microstructure of casein micelles, free sulfhydryl content, and surface hydrophobicity of the samples were determined. The insolubility index of MPC was also determined. Casein micelles aggregated compactly after evaporation while surface hydrophobicity increased and free sulfhydryl content decreased in evaporated milk compared with skim milk. However, the microstructure of the casein micelles was relatively undisturbed after nanofiltration, with reduced surface hydrophobicity and free sulfhydryl content. No significant difference was found in chemical composition between the 2 MPC preparations: approximately 61.40% protein and 28.49% lactose. In addition, the particulate microstructures of both MPC were similar. However, the insolubility index of evaporated MPC was significantly (0.58mL) higher than that of nanofiltered MPC. Nanofiltration may be an effective way to improve the solubility of MPC products., (Copyright © 2015 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.)

Background: The use of power ultrasound as a pretreatment to enhance the hydrolysis of milk protein concentrate (MPC) and subsequent angiotensin converting enzyme (ACE) inhibitory activity has been studied. Liquid chromatography was used to analyse peptide profiles of Neutrase-derived MPC hydrolysates after pretreatment at 0, 1, 3, 5 and 8 min at an ultrasound power level of 800 W., Results: The peptide profiles indicated an increase in number of peptides when ultrasound pretreatment was applied. There was also an increase in the degree of hydrolysis of MPC hydrolysates. The profiles indicated that new small peptides in ultrasound pretreated samples (1-5 min) which were not present in the control samples and 8 min pretreated samples, could be responsible for increased ACE inhibitory activity. These small peptides were digested in the 8 min pretreated samples., Conclusion: Ultrasound pretreatment of MPC increases the ACE inhibitory activity of the hydrolysates because of the production of new small peptides. This can be used as a means to derive potent ACE inhibitory peptides at industrial scale in complex protein sources., (© 2014 Society of Chemical Industry.)

In dairy-based imitation mozzarella cheese (IMC) formulations, intact casein is critical and imparts IMC with a firm and elastic, stringy, melted texture. Rennet casein (RCN) is the desired ingredient to provide intact casein in IMC and is preferred over milk protein concentrate (MPC) and micellar casein concentrate (MCC). Transglutaminase (TGase), a crosslinking enzyme, alters the physical properties of MPC or MCC and may change IMC functionality. The objective of this study was to determine the effect of TGase-crosslinked MPC and MCC powders on the functionality of IMCs. The TGase treatment included TGase at 0.3 (L) and 3.0 (H) units/g of protein and a control (C) with no TGase addition. Each IMC formulation was balanced for constituents and was produced in a Rapid Visco Analyzer (RVA). The MCC or MPC powder with high TGase enzyme in IMC formulation did not form an emulsion. The IMC containing TGase-treated powders had a significantly (p ≤ 0.05) higher RVA-viscosity during manufacture and transition temperature (TT), and a significantly (p ≤ 0.05) lower Schreiber melt test area. The IMC made from MPC (with or without TGase) had lower TT values and Schreiber melt test area as compared with that made from MCC. The TGase-treated MPC and MCC, when used for IMC manufacture, were comparable to IMC manufactured with RCN in texture and some measured melted characteristics. In conclusion, TGase treatment alters the melt characteristics of MCC and MPC in IMC applications. [ABSTRACT FROM AUTHOR]

The effect of shear on heat-induced changes in milk protein concentrate suspensions was examined at different pH levels, revealing novel insights into micellar dissociation and protein aggregation dynamics. Milk protein concentrate suspensions, adjusted to pH of 6.1, 6.4, 6.8, or 7.5, underwent combined heat (90 °C for 5 min or 121 °C for 2.6 min) and shear (0, 100, or 1000 s−1) treatment. The fragmentation of protein aggregates induced by shear was evident in the control MPC suspensions at pH 6.8, irrespective of the temperature. At pH 7.5, shear increased the heat-induced micellar dissociation. This effect was particularly pronounced at 121 °C and 1000 s−1, resulting in reduced particle size and an elevated concentration of κ-casein (κ-CN) in the non-sedimentable phase. At pH 6.1 or 6.4, shear effects were dependent on sample pH, thereby modifying electrostatic interactions and the extent of whey protein association with the micelles. At pH 6.1, shear promoted heat-induced aggregation, evidenced by an increase in particle size and a significant decline in both whey proteins and caseins in the non-sedimentable phase. At pH 6.4, shear-induced fragmentation of aggregates was observed, prominently due to comparatively higher electrostatic repulsions and fewer protein interactions. The influence of shear on heat-induced changes was considerably impacted by initial pH. [ABSTRACT FROM AUTHOR]

Protein–protein and protein–mineral interactions can result in defects, such as sedimentation and age gelation, during the storage of high-protein beverages. It is well known that age gelation can be delayed by adding cyclic polyphosphates such as sodium hexametaphosphate (SHMP). This study aims to assess the influence of different phosphate chain lengths of SHMP on the physicochemical properties of high-protein dispersions. The effect of adding different SHMP concentrations at 0%, 0.15%, and 0.25% (w/w) before and after heating of 6%, 8%, and 10% (w/w) milk protein concentrate dispersions was studied. The phosphate chain lengths of SHMPs used in this study were 16.47, 13.31, and 9.88, and they were classified as long-, medium-, and short-chain SHMPs, respectively. Apparent viscosity, particle size, heat coagulation time (HCT), color, and turbidity were evaluated. It was observed that the addition of SHMP (0.15% and 0.25%) increased the apparent viscosity of MPC dispersions. However, the chain length and the concentration of the added SHMP had no significant (p > 0.05) effect on the apparent viscosity after heating the dispersions. The HCT of a dispersion containing 6%, 8%, and 10% protein with no SHMP added was 15.28, 15.61, and 11.35 min, respectively. The addition of SHMP at both levels (0.15% and 0.25%) significantly increased the HCT. Protein dispersions (6%, 8%, and 10%) containing 0.25% short-chain SHMP had the highest HCT at 19.29, 19.61, and 16.09 min, respectively. Therefore, the chain length and concentration of added SHMP significantly affected the HCT of unheated protein dispersion (p < 0.05). [ABSTRACT FROM AUTHOR]

The objective of this study is to produce red beet root powder by using foam mat drying by microwave-assisted method and evaluate the effect of process parameters (Maltodextrin and milk protein concentrate (MPC) as the foaming agent concentration (0–10% w/w) and the power of microwave (400–800 W) on the foam and powder properties (foam density and foam expansion, unit density and bulk density, flowability and porosity, color and betalain content of powder, water soluble index and water absorption index. The optimal process condition was determined using response surface methodology. The optimum conditions for the foam mat process were 9.92% of maltodextrin, 10% of MPC concentration, and a microwave power of 400W. In optimal conditions, higher amounts of betalain (119.678 mg/100 g) and solubility (41.12%) were seen compared to the control sample (powder produced with a hot air dryer at 70 °C). Also, the color of the optimal sample had a higher level of Lightness compared to the control sample, and the high browning index belongs to the control sample (98.52). The Scanning electron microscopy images show that the optimal sample has finer particles and smooth, softer, flaky surfaces. The Fourier transform infrared spectra of the optimal and control showed remarkable similarities. Intensifying and shifting some absorption peaks of the FTIR spectra pattern confirmed the interaction of functional groups of amide and carbonyl groups in the control sample so that the decrease in the number of amide groups in the control sample was more significant. [ABSTRACT FROM AUTHOR]

Milk protein concentrates (MPCs) possess significant potential for diverse applications in the food industry. However, their heat stability may be a limitation to achieving optimal functional performance. Shearing, an inherent process in food manufacturing, can also influence the functionality of proteins. The aim of this research was to examine the heat stability of reconstituted MPCs prepared at two protein concentrations (4% and 8% w/w protein) when subjected to varying levels of shearing (100, 1000, or 1500 s−1) during heating at 90 °C for 5 min or 121 °C for 2.6 min. While the impact of shear was relatively minor at 4% protein, it was more pronounced in 8% protein MPC suspensions, leading to a considerable decline in heat stability. An increase in protein concentration to 8% amplified protein interactions, intensified by shearing. This, in turn, resulted in comparatively higher aggregation at elevated temperatures and subsequently reduced the heat stability of the reconstituted MPCs. [ABSTRACT FROM AUTHOR]

This study evaluated the economic feasibility and environmental sustainability of producing nutritionally superior snacks on an industrial scale by supercritical fluid extrusion (SCFX) using milk protein concentrate (MPC81-AP) or starch (Starch-AP)-based formulations enriched with apple pomace powder. Selected nutrient contents and antioxidant attributes were also studied to highlight the nutritional qualities of the final products. For large-scale implementation using a low-temperature (85 °C) and low-shear SCFX system, capital budgeting, breakeven point, and profitability ratios were determined. During a standard 12-hour production run, a substantial margin of safety of 29.03% and a breakeven point of 0.71 years were estimated, indicating resilience against potential losses and a swift return on investment. The projected prices for MPC81-AP and Starch-AP-based products were $30.13/kg (Similar market snacks, $32-150/kg) and $26.29/kg, respectively. In summary, both formulations exhibited superior nutritional qualities, better gross profit margins and return on investment with environmentally sustainability, compared with the conventional extrudate snack foods available in the market today. [ABSTRACT FROM AUTHOR]

The purpose of this study was to produce whey-less Lighvan cheese (WLC) and characterize the cheese's physical, chemical, and textural characteristics as well as its fatty acid and amino acid composition. WLC was made using sheep milk cream (17.04%), milk protein concentrate (MPC) (12.50%), whey protein concentrate (WPC) (1.745%) and compared with the typical Lighvan cheese (LC) during the 75-day ripening period at 4 °C. The results showed that the production yield of WLC (76.54%) was higher than LC (30.00%). WLC had a higher dry matter, protein, fat, and ash than the LC, while the moisture and salt content of the LC was higher. During the ripening period, cheese moisture content and pH decreased. The values of dry matter, protein, fat, ash, salt, acidity, hardness, chewiness, gumminess, and adhesiveness increased significantly (p < 0.05). The LC had the firmest texture compared to the WLC. Analyzing the cheese's fatty acids and amino acids composition also showed an increase in lipolysis and proteolysis processes during the ripening period of Lighvan cheese. The values of all fatty acids in the WLC were higher than in the LC. Different values of amino acids were observed in the LC and WLC samples. The sensory evaluation results showed that both the LC and the WLC had high sensory acceptance and scored well. In summary, it is possible to produce whey-less Lighvan cheese with favorable quality characteristics by combining optimal levels of sheep milk cream, MPC, and WPC. [ABSTRACT FROM AUTHOR]

Milk protein dispersions containing added cocoa powder (1.5% (w/w)) and sucrose (7% (w/w)) and varying levels of κ-carrageenan (0.01, 0.03, or 0.05% w/w) were subjected to combined heat treatment (90 °C/5 min or 121 °C/2.6 min) and shear (100 or 1000 s−1) to investigate the heat stability of milk proteins. The application of shear led to a notable reduction in non-sedimentable proteins, resulting in an increase in the average particle size and apparent viscosity of the dispersions, particularly at high concentrations of k-carrageenan and elevated temperatures. This indicates that shear forces induced prominent protein aggregation, especially at higher κ-carrageenan concentrations. This aggregation was primarily attributed to the destabilisation of micelles and presence of loosely bound caseins within the κ-carrageenan network, which exhibited increased susceptibility to aggregation as collision frequencies increased due to shear. [ABSTRACT FROM AUTHOR]

The present study investigated types of bacterial endospores in powdered dairy ingredients. For enumeration, the samples were heat‐treated at 80°C/12 min for regular spore type, 100°C/30 min for high‐heat‐resistant spores (HHRS), and 106°C/30 min for specially thermoresistant spores (STS), followed by incubation for 24 h at 37°C (for mesophiles) and 55°C (for thermophiles). Of the three types, the regular spore type (80°C/12 min) was observed to be the most prominent endospore type, and Bacillus licheniformis as the predominant bacterial species in the tested dairy ingredients. This study would be helpful to utilise dry ingredients based on the potential activation of endospores during the product manufacturing processes. [ABSTRACT FROM AUTHOR]

The main aim of the study was to establish the impact of limited proteolysis by actinidin on the functionality of selected milk protein systems. The plant protease actinidin was used to produce hydrolysates (MPHs) from milk protein concentrate (MPC) and whey protein concentrate (WPC) to 0, 5, 10 or 15% of the degree of hydrolysis (DH) at an enzyme-to-substrate ratio of 1:100 (5.21 units of actinidin activity g−1 of protein). The functionalities assessed included solubility, heat stability, emulsification and foaming properties. In general, significant changes in the functionalities of MPH were associated with the extent of hydrolysis. Solubility of hydrolysates increased with increasing %DH, with WPC showing about 97% solubility at 15% DH. Emulsifying properties were negatively affected by hydrolysis, whereas heat stability was improved in the case of WPC (~25% of heat stability increased with an increase in DH to 15%). Hydrolysates from both WPC and MPC had improved foaming properties in comparison to unhydrolysed controls. These results were also supported by changes in the FTIR spectra. Further adjustment of hydrolysis parameters, processing conditions and pH control could be a promising approach to manipulate selected functionalities of MPHs obtained using actinidin. [ABSTRACT FROM AUTHOR]

Grape and apple pomace powders, a good source of dietary fiber and nutrients, were incorporated in formulations containing milk protein concentrate with over 81% milk protein (MPC-81) to produce puffed products using supercritical fluid extrusion (SCFX). The cellular structure and cell nucleation dynamics in the extruded samples were evaluated as function of pressure drop and supercritical CO2 (SCCO2) injection rates. Results showed that SCFX generated pomace-based extruded products had an expansion ratio up to 12.3 and microcellular structure (ranging in cell size from 278 to 540 µm) and cell density of the order of 104–105 cells/cm3. The general trend of increased cell density and decreased cell size of extrudates was observed by increasing pressure drop rate and SCCO2 content and exhibited a uniform cellular architecture when the injected SCCO2 level was close its saturation solubility in the aqueous phase of the dough, and the pressure drop rate was high, up to 141.04 MPa/s. Beyond these values, some structural collapse was observed in both extrudates. Although the extrudates had the same level of expansion, their hardness values gradually decreased, indicating that the textural qualities and microcellular structure in extrudates can be controlled by regulating the SCCO2 injection and pressure drop rates. It is thus reasonable to suggest that the SCFX technology provides a unique strategy to control cellular morphology, expansion, and physicochemical characteristics of nutritionally superior extruded products. [ABSTRACT FROM AUTHOR]

Membrane filtration, especially in combination with diafiltration, can affect the colloidal structure of casein micelles in milk and concentrated milks. The partial dissociation of casein proteins from the casein micelles into the serum phase has been shown to depend on diafiltration conditions. This dissociation can affect the technological functionality of the milk concentrates. The present study aimed at determining the contribution of the gel layer deposited onto the membrane during filtration in the colloidal equilibrium between soluble and micellar caseins. Skimmed milk was concentrated by microfiltration combined with diafiltration using a cross-flow spiral-wound membrane at two transmembrane pressure (TMP) levels, causing differences in the extent of the gel layer formed. Non-sedimentable casein aggregates were formed to a greater extent at a low TMP compared to a high operating TMP. This difference was attributed to the greater compression of the deposit layer during filtration at a high TMP. This study contributes new knowledge to the understanding of how to modulate the functionality of milk concentrates through the control of processing conditions. [ABSTRACT FROM AUTHOR]