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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]

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. [ABSTRACT FROM AUTHOR]

Introduction: Beetroot (Beta vulgaris L.) is a good source of dietary fibers, minerals, vitamins, antioxidants, betalains and phenolic compounds. Drying is one of the oldest ways to preserve food and increase its shelf life. Drying with normal methods causes a lot of damage to the flavor and nutrients due to the long time of the drying process and high temperature. Drying with microwave can significantly remove these disadvantages. The use of microwaves in drying significantly reduces the process time and improves the reabsorption and shrinkage characteristics of the product. Foam \mat drying is a new method that takes place in a shorter and faster time than the traditional method of drying with hot air. This method is used to dry liquid or semi-liquid food such as fruit juice and fruit puree or vegetables. The subject of this research is to produce beetroot powder using the foammat method in order to improve the nutritional value and increase the shelf life.Materials and methods: 15 treatments were defined using Design Expert version 11 software and considering three independent variables [maltodextrin (MD), milk protein concerate (MPC], microwave power). The foam produced from maltodextrin and MPC with the same concentration (0-10%) was dissolved in 100 ml of distilled water and then added to 200 g of chopped beet pulp and the mixture and prepared foam was spread in a special tray with a thickness of 1 cm. Drying operation was done in a microwave with power intensity (400-800). Then the produced powder of beetroot was evaluated in terms of some physicochemical characteristics and the responses of the treatments were analyzed by the response surface method (RSM) and the central composite design (CCD) and the optimal sample was obtained.

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.

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]

Plant proteases, including actinidin, papain and bromelain, have been widely used in the food industry but with limited application in dairy systems. This research aimed to establish and compare operational parameters (kinetics, temperature, enzyme type, time and thermodynamics) relevant to the applications of these enzymes in the hydrolysis of whey protein isolates (WPI), whey protein concentrates (WPC) or milk protein concentrates (MPC). The degree of hydrolysis (DH) increased with the rise in temperature, and the maximum DH was achieved at 60 °C for all three dairy systems. The addition of papain resulted in a greater %DH of whey proteins in comparison to bromelain. The cleavage of proteins was clearly time-dependent (p < 0.05), while the pH did not change significantly (p > 0.05) during this time. PAGE analysis revealed that all three enzymes mainly acted on α-lactalbumin and αs-casein in WPI and MPC, respectively. Kinetic parameters from the Lineweaver–Burk plot at 60 °C using WPC and MPC as a substrate varied widely, establishing that WPC hydrolysis was characterised by a lower KM, higher kcat, kcat/KM and Vmax compared to MPC in the case of all three enzymes. The difference in kcat/KM values amongst all enzymes (actinidin > papain > bromelain) indicated the difference in the strength of substrate binding sites. The thermodynamic parameters of these enzymes with MPC and WPC were also determined at a temperature range of 15–60 °C, and the results indicate the potential application of papain and actinidin in the dairy industry. [ABSTRACT FROM AUTHOR]

This study investigated the impact of calcium chloride (CaCl2) and magnesium chloride (MgCl2) at varying concentrations on a model milk formulation's physical and chemical properties after thermal treatment. The model milk was subjected to two-stage homogenization and pasteurization before being supplemented with different concentrations of CaCl2 or MgCl2. The findings revealed that elevating the concentration of either calcium or magnesium resulted in the milk emulsion having a higher viscosity and median particle size following heating. CaCl2 had a slightly stronger impact than MgCl2, particularly at higher concentrations. The milk samples also exhibited a reduction in the zeta potential as the ionic strength of the salt solution increased, with the CaCl2-fortified milk displaying a slightly lower negative surface charge than the MgCl2-fortified milk at the same dose. The model milk's viscosity was evaluated after adding various salt concentrations and a temperature ramp from 20 to 80 °C. Notably, the viscosity and particle size changes demonstrated a non-linear relationship with increasing mineral levels, where a significant increase was observed at or above 5.0 mM. An emulsion stability analysis also revealed that the de-stabilization pattern of the high salt concentration sample differed significantly from its low salt concentration counterparts. These findings could serve as a basis for the future development of fortified UHT milk with nutritionally beneficial calcium and magnesium in industrial applications. [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 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: 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 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]

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).

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. [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]

The performance of nanofiltration (NF) as influenced by hydrodynamic cavitation (HC) and filtration temperature during the concentration of milk protein concentrate (MPC) was investigated. Pasteurised skim milk was concentrated using ultrafiltration (UF) to prepare UF retentate (MPC80, 20% total solids, TS), which was then further concentrated using NF at 22°C and 50°C with or without HC treatments until permeate flux declined to 0.1 L/m2/h. Results showed that UF retentate can be concentrated to higher TS (up to 31.5%) at higher filtration temperature or by applying HC, with synergistic effect in combination of both treatments, during NF. [ABSTRACT FROM AUTHOR]

ABSTRACT: Milk protein concentrate was hydrolyzed using one-step enzymatic hydrolysis. Both the peptide profiles and antioxidant activities of the resulting extensive hydrolysates of milk protein concentrate (EMPH) were analyzed using a peptidomics approach based on liquid chromatography–tandem mass spectrometry. The results demonstrated that the degrees of hydrolysis of the 4 EMPH by Alcalase-Protamex, Alcalase-Protease A 2SD, Alcalase-Flavorzyme, and Alcalase-ProteAXH were 12.02%, 16.85%, 15.87%, and 15.77%, respectively. Using size exclusion chromatography, 99.85% of the peptides in the Alcalase-Protease A 2SD hydrolysate were shown to have a molecular weight of

ABSTRACT: 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.

Bulk nanobubbles (BNBs) have widespread applications in various fields of science due to numerous peculiar characteristics. Despite significant applications, only limited investigations are available on the application of BNBs in food processing. In the present study, a continuous acoustic cavitation technique was used to generate bulk nanobubbles (BNBs). The aim of this study was to evaluate the influence of BNB incorporation on the processability and spray drying of milk protein concentrate (MPC) dispersions. MPC powders were reconstituted to the desired total solids and incorporated with BNBs using acoustic cavitation as per the experimental design. The control MPC (C-MPC) and BNB-incorporated MPC (BNB-MPC) dispersions were analyzed for rheological, functional, and microstructural properties. The viscosity significantly decreased (p < 0.05) at all the amplitudes studied. The microscopic observations of BNB-MPC dispersions showed less aggregated microstructures and greater structural differences compared with C-MPC dispersions, therefore lowering the viscosity. The viscosity of BNB incorporated (90% amplitude) MPC dispersions at 19% total solids at a shear rate of 100 s−1 significantly decreased to 15.43 mPa·s (C-MPC: 201 mPa·s), a net decrease in viscosity by ~90% with the BNB treatment. The control and BNB incorporated MPC dispersions were spray-dried, and the resultant powders were characterized in terms of powder microstructure and rehydration characteristics. Focused beam reflectance measurement of the BNB-MPC powders indicated higher counts of fine particles (<10 μm) during dissolution, signifying that BNB-MPC powders exhibited better rehydration properties than the C-MPC powders. The enhanced powder rehydration with the BNB incorporation was attributed to the powder microstructure. Overall, reducing the viscosity of feed by BNB incorporation can enhance the performance of the evaporator. This study, therefore, recommends the possibility of using BNB treatment for more efficient drying while improving the functional properties of the resultant MPC powders. [ABSTRACT FROM AUTHOR]

The impact of whey protein (WP) denaturation on the in vitro digestibility and biological activity of milk protein concentrate-85 (MPC85) was investigated. MPC85S1 and MPC85S2 having undenatured WP levels equal to 16.6 and 6.0 g/100 g overall protein, respectively, had similar in vitro protein digestibility corrected amino acid scores equal to 1.14. The samples were subjected to in vitro simulated gastrointestinal digestion while sampling was performed every 30 min during gastric (GD) followed by intestinal (GID) digestion. Liquid chromatography–mass spectroscopy showed that MPC85S1-GD, MPC85S2-GD, MPC85S1-GID and MPC85S2-GID had 50, 38, 47 and 66 unique peptides, respectively. The degree of hydrolysis, molecular mass distribution, dipeptidyl peptidase-IV inhibition, oxygen radical absorbance capacity and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical scavenging activity of the digests were compared. Overall, the results showed higher digestibility and bioactivities for low-denatured MPC85 compared to high-denatured MPC85 upon GD, however, following GID, both samples were digested to a similar extent.

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.

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.

Plant proteases, including actinidin, papain and bromelain, have been widely used in the food industry but with limited application in dairy systems. This research aimed to establish and compare operational parameters (kinetics, temperature, enzyme type, time and thermodynamics) relevant to the applications of these enzymes in the hydrolysis of whey protein isolates (WPI), whey protein concentrates (WPC) or milk protein concentrates (MPC). The degree of hydrolysis (DH) increased with the rise in temperature, and the maximum DH was achieved at 60 °C for all three dairy systems. The addition of papain resulted in a greater %DH of whey proteins in comparison to bromelain. The cleavage of proteins was clearly time-dependent (p < 0.05), while the pH did not change significantly (p > 0.05) during this time. PAGE analysis revealed that all three enzymes mainly acted on α-lactalbumin and αs-casein in WPI and MPC, respectively. Kinetic parameters from the Lineweaver–Burk plot at 60 °C using WPC and MPC as a substrate varied widely, establishing that WPC hydrolysis was characterised by a lower KM, higher kcat, kcat/KM and Vmax compared to MPC in the case of all three enzymes. The difference in kcat/KM values amongst all enzymes (actinidin > papain > bromelain) indicated the difference in the strength of substrate binding sites. The thermodynamic parameters of these enzymes with MPC and WPC were also determined at a temperature range of 15–60 °C, and the results indicate the potential application of papain and actinidin in the dairy industry.

This study investigated the impact of calcium chloride (CaCl2) and magnesium chloride (MgCl2) at varying concentrations on a model milk formulation’s physical and chemical properties after thermal treatment. The model milk was subjected to two-stage homogenization and pasteurization before being supplemented with different concentrations of CaCl2 or MgCl2. The findings revealed that elevating the concentration of either calcium or magnesium resulted in the milk emulsion having a higher viscosity and median particle size following heating. CaCl2 had a slightly stronger impact than MgCl2, particularly at higher concentrations. The milk samples also exhibited a reduction in the zeta potential as the ionic strength of the salt solution increased, with the CaCl2-fortified milk displaying a slightly lower negative surface charge than the MgCl2-fortified milk at the same dose. The model milk’s viscosity was evaluated after adding various salt concentrations and a temperature ramp from 20 to 80 °C. Notably, the viscosity and particle size changes demonstrated a non-linear relationship with increasing mineral levels, where a significant increase was observed at or above 5.0 mM. An emulsion stability analysis also revealed that the de-stabilization pattern of the high salt concentration sample differed significantly from its low salt concentration counterparts. These findings could serve as a basis for the future development of fortified UHT milk with nutritionally beneficial calcium and magnesium in industrial applications.

Fouling is an important problem in the dairy industry where heat treatment is necessary for food safety and quality. The fouling may affect product quality and food safety. This study aimed to investigate the effects of different fouling temperatures and calcium addition on the fouling amount of milk protein concentrate on stainless steel surfaces. For these purposes, laboratory-scale fouling model was applied at three different temperatures (~65, 90, 110°C) on the surfaces. Then, the efficiencies of rinsing with water, alkaline and enzymatic cleaning methods were evaluated. The addition of calcium and an increase in the applied temperature increased the fouling amount while decreasing cleaning efficiency. The lowest cleaning efficiency was determined in the rinsing method, whereas the highest was observed using enzymatic cleaning method. The study showed the potential of applying FTIR-ATR combined with multivariate analysis to discriminate the classes of fouled with milk protein concetrate or cleaned surfaces. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

This study elucidated the reactive role of the supercritical fluid extrusion (SCFX) process along with calcium chelation by added sodium hexametaphosphate (SHMP) in altering the physicochemical properties of milk protein concentrate (MPC) with added sucrose (MPC‐S) to make expanded extrudates of defined microstructure that self‐disintegrate in the mouth. Calcium chelation by SHMP and temporarily induced acidity (pH 4.75) due to the formation of carbonic acid via SC‐CO2 incorporation during SCFX prevented protein–protein interactions involving calcium bridging and disulfide bonding in MPC‐S extrudates. The electrophoretic patterns demonstrated increased solubility of caseins in MPC‐S‐SHMP extrudates when compared to MPC‐S‐control. MPC‐S‐SHMP extrudates absorbed three times more water than MPC‐S‐control extrudates after 30 s of hydration. Textural analysis demonstrated that the compression strength of MPC‐S‐SHMP extrudates reduced by 93% on hydration as compared to 31% for MPC‐S‐control samples. During hydration, increased water absorption by MPC‐S‐SHMP extrudates resulted in weakened extrudate structure and decreased mechanical strength contributing to self‐disintegration in less than 30 s in the mouth which was confirmed by sensory evaluation. Practical Applications: The developed and demonstrated process led to the manufacture of nutritious, milk protein‐based convenient and quick in‐mouth disintegrating puffs that can be used as a valuable replacement for starch‐based first finger foods intended for toddlers. They also provide the opportunity to practice baby led weaning along with being rich in protein and essential amino acids. Additionally, the developed product should be suitable for consumption by elderly as well as for patients with other conditions such as dysphagia. [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: 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.

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. [ABSTRACT FROM AUTHOR]

Milk protein concentrate was hydrolyzed using one-step enzymatic hydrolysis. Both the peptide profiles and antioxidant activities of the resulting extensive hydrolysates of milk protein concentrate (EMPH) were analyzed using a peptidomics approach based on liquid chromatography–tandem mass spectrometry. The results demonstrated that the degrees of hydrolysis of the 4 EMPH by Alcalase-Protamex, Alcalase-Protease A 2SD, Alcalase-Flavorzyme, and Alcalase-ProteAXH were 12.02%, 16.85%, 15.87%, and 15.77%, respectively. Using size exclusion chromatography, 99.85% of the peptides in the Alcalase-Protease A 2SD hydrolysate were shown to have a molecular weight of <3 kDa. A total of 33 common peptides were identified in the EMPH by liquid chromatography–tandem mass spectrometry, 16 of which were identified as bioactive peptides using bioinformatics. The peptide profiles and the coverage of master proteins of the 4 EMPH were different. The EMPH also exhibited strong free radical scavenging capacity, as indicated by the results of the 1,1-diphenyl-2-picrylhydrazyl radical, 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid), hydroxyl radical, and reducing power assays. The results of this study provided useful information on the peptide profiles and antioxidant activity of EMPH. [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.

Bulk nanobubbles (BNBs) have widespread applications in various fields of science due to numerous peculiar characteristics. Despite significant applications, only limited investigations are available on the application of BNBs in food processing. In the present study, a continuous acoustic cavitation technique was used to generate bulk nanobubbles (BNBs). The aim of this study was to evaluate the influence of BNB incorporation on the processability and spray drying of milk protein concentrate (MPC) dispersions. MPC powders were reconstituted to the desired total solids and incorporated with BNBs using acoustic cavitation as per the experimental design. The control MPC (C-MPC) and BNB-incorporated MPC (BNB-MPC) dispersions were analyzed for rheological, functional, and microstructural properties. The viscosity significantly decreased (p < 0.05) at all the amplitudes studied. The microscopic observations of BNB-MPC dispersions showed less aggregated microstructures and greater structural differences compared with C-MPC dispersions, therefore lowering the viscosity. The viscosity of BNB incorporated (90% amplitude) MPC dispersions at 19% total solids at a shear rate of 100 s−1 significantly decreased to 15.43 mPa·s (C-MPC: 201 mPa·s), a net decrease in viscosity by ~90% with the BNB treatment. The control and BNB incorporated MPC dispersions were spray-dried, and the resultant powders were characterized in terms of powder microstructure and rehydration characteristics. Focused beam reflectance measurement of the BNB-MPC powders indicated higher counts of fine particles (

In this study, the properties of whey-less Feta cheese (WLFC) manufactured from milk protein concentrate (MPC) with the addition of soy protein isolate (SPI) were investigated. Six treatments were made using different ratios of MPC:SPI (12:0, 10:2, 9:3, 8:4, 7:5, 6:6% w/v) and stored for 45 days. Then, the textural properties, rheological behavior of samples, and microstructural and sensory features were evaluated. Furthermore, FTIR spectroscopy was used to provide spectral data on the protein, acids, carbohydrates, lipids, and water. The results showed that different concentrations of SPI significantly affected pH, acidity, total solids (TS), and color parameters. So that, by increasing SPI concentration, the lightness and greenness decreased, and the yellowness increased. The viscoelastic behavior of all samples demonstrated a higher G′ compared to G″. The replacement of MPC with SPI decreased G′, G″, and texture parameters. The images of the microstructure indicated a weak structure with a more open protein network in WLFCs fortified with high levels of SPI (5, 6%). In conclusion, results showed that SPI could be a good substitution for MPC at a 2–3% concentration without negative effects on WLFCs. [ABSTRACT FROM AUTHOR]

Hydrocolloids are often added as functional ingredients in foods, to better design the structure of the matrix and ensure food quality and optimal sensory properties. However, much less is known about their influence on the physical and chemical changes during gastric digestion. In this study, semi-continuous in vitro gastric digestion was applied on a model food system, prepared with milk protein concentrate (MPC) (3% w/v) and 1% alginate, pectin, guar gum, as well as a 1:1 mixture of alginate and pectin. The dynamics during simulated gastric digestion were observed by measuring particle size distributions, structuring at various length scales, as well as by evaluating differences in protein breakdown. Immediately after contact with the simulated gastric fluids, all samples showed extensive aggregation and formation of different structures. MPC control dispersions (no polysaccharide) and MPC containing alginate formed large inhomogeneous aggregates. The lack of structural homogeneity affected the simulated gastric emptying: there were marked differences in the type of aggregates present at various times of emptying depending on the hydrocolloid present in the mixture. MPC containing pectin or guar gum formed macroscopically homogeneous dispersion, with rather small protein aggregates showing a large population of particles between 60 and 100 ​μm of diameter, with marked differences in microstructure. Pectin created large coacervates, while guar microscopic phase separated systems. These dispersions showed a higher extent of protein digestion, due to the larger surface area created for enzyme activity compared to the macroscopically phase separated matrices. In all cases, there was a large undigested fraction at the end point of 140 ​min. SDS PAGE demonstrated differences in the casein peptides distribution depending on the type of polysaccharide present during simulated gastric emptying. This in spite of similarities in cumulative protein emptied. It was concluded that in this semi-continuous in vitro gastric digestion model, structuring with polysaccharides has a significant impact on gastric emptying and protein digestion kinetics.

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 m M 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 m M , thermally irreversible gels were observed with relative strength dependent on the salt and protein content. [ABSTRACT FROM AUTHOR]

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This study was aimed to evaluate the effect of milk protein concentrate (MPC) on the broiler chicken performance and meat quality. Two experiments were conducted to this study. In the first study 250 1- day old broiler chicks (VINITIP-1 cross bred) were assigned into 5 groups (control, 5% Fishmeal, 1% MPC, 3% MPC and 5% MPC) and placed in the separated cages for 7th weeks. By daily monitoring of the chickens and their feed intake and weighing of individual birds at the ages of 4th and 7th weeks of age, animal viability, feed efficiency, body weight (BW) and weight gain were evaluated. In the second experiment, 200 1-day old chicks were assigned into four groups (control, 5% fishmeal, 1% MPC and 3% MPC) and placed into the separated cages for 8 weeks. In order to we could not significantly found difference between the groups were fed 3% and 5% MPC, thus we eliminated the group was supplemented 5% MPC in this experiment. At the end of this experiment 5 chickens from each groups were slaughtered for meat quantitative and qualitative analysis of breast and drumstick meat. The current studies revealed that 3% MPC significantly improved the animal performance, viability, live weight and meat quality. Increment of MPC had no beneficial impacts on the chicken meat quality and their performances. In conclusion, MPC as a byproducts of milk processing is a good alternative source of protein in the chicken diet that can improve their body weights and the carcasses quality. [ABSTRACT FROM AUTHOR]

Soy proteins are used in foods as non-dairy alternatives and they play significant role in human health. The use of different concentrations of soy protein isolate (SPI) (0–6% w/v dry basis) in the development of bacteriologically acidified feta type (BAF) cheeses applied with milk protein concentrate (MPC) was investigated during 45 days of storage. The results showed that substitution of MPC by SPI increased acidity and the time of coagulation. With an increase in the SPI concentration, the viscoelastic behavior of all samples demonstrated the higher Gʹ compared to Gʺ, showing a solid-like behavior of the manufactured samples. The addition of SPI led to the reduction of Gʹ, Gʺ and texture parameters (hardness, cohesiveness, gumminess and springiness). The images of microstructure indicated a more open protein network and weaker structure in BAF cheeses fortified with high levels of SPI. Microbiological results showed that the use of MPC and SPI was able to obtain a matrix that could provide a protection to the starter bacteria. In conclusion, MPC can be substituted by SPI to the rate of 3% without adversely effecting on the sensory properties of BAF cheese. [ABSTRACT FROM AUTHOR]

The effects of water and supercritical CO2 (SC–CO2) addition rate, and pressure at SC–CO2 injection (PCO2) on physical and rheological properties of milk protein concentrate (MPC81) and MPC81‐sucrose (MPC81‐S) extrudates were investigated. As PCO2 increased, extrudate expansion decreased and storage modulus and hardness increased. PCO2 for MPC81 and MPC81‐S was optimised as 13.78 MPa and 11.03 MPa, respectively, whereas water rate of 40 (wt. % dry feed) and SC–CO2 rate of 2.25 (wt. % dry feed) were optimised for both formulations. Elucidating the association of extrusion parameters and extrudate properties will facilitate the development of MPC extrudates of commercial utility. [ABSTRACT FROM AUTHOR]

The primary objective of the present study was to investigate the effectiveness of ultrasonic treatment time on the particle size, molecular weight, microstructure and solubility of milk fat globule membrane (rich in phospholipid, MPL) and milk protein concentrate (MPC). The mimicking human fat emulsions were prepared using modified proteins and compound vegetable oil and the structural, emulsifying properties and encapsulation efficiency of emulsions were evaluated. After ultrasonic treatment, the cavitation caused particle size decreased and structure change of both MPL and MPC, resulting in the enhancement of protein solubility. While, there was no significant change in molecular weight. Modified proteins by ultrasonic may cause a reduction in particle size and an improvement in emulsifying stability and encapsulation efficiency of emulsions. The optimal ultrasonic time to improve functional properties of MPL emulsion and MPC emulsion were 3 min and 6 min, respectively. The emulsifying stability of MPL emulsion was superior to MPC emulsion, which indicated that MPL is more suitable as membrane material to simulate human fat. Therefore, the obtained results can provide basis for quality control of infant formula.

Summary: Supercritical fluid extrusion (SCFX) process has opened up a new way of extruding heat‐sensitive materials such as milk protein concentrate (MPC) into novel nutritional porous extrudates. Three formulations (30%:66.5%, 60%:36.5% and 90%:6.5% of MPC: rice flour, w/w) with 1% Dimodan, 1% lecithin and 1.5% salt were extruded by using SCFX. The physical, rheological and thermal properties of the extrudates were evaluated. The results showed that the increased MPC contents decreased gelatinisation enthalpy and increased the viscosity of the extrudates, which contributed to develop stable porous extrudates; and the increased MPC contents also helped to form a stronger gel network existed in dispersion of the extrudate samples, which resulted in a higher stress to break the gel and flow. The radial and overall expansions, crispness, porosity, rehydration ratio, moisture content and water activity increased while the axial expansion, hardness, piece density, apparent density, bulk density, decreased with higher amounts of MPC contents in extrudates. The overall results indicated that 90% MPC‐containing extrudate was very suitable for developing highly nutritional and healthy cereals/snacks. [ABSTRACT FROM AUTHOR]

In this work, the formation of anisotropic, layered structures from milk protein concentrates was investigated using high moisture extrusion. These structures were obtained in combination with three concentrations of starch (0 %, 14 %, and 33 %, d.b), and at three different moisture levels: 58 %, 63 %, and 68 %. Two different temperature profiles were investigated, reaching a maximum barrel temperature of 80 and 115 °C (and maximum melt temperature of 56 and 64 °C, respectively), with a constant screw speed and feed rate. In situ monitoring of torque, as well as the evaluation of water partitioning via proton relaxometry highlighted the interplay between moisture content and barrel temperature in starch transitions and water intake. For example, the presence of starch displayed water populations of distinct mobility, featured by higher relaxation times, and the apparition (or intensification) of new peaks representing free water in the system. The extruded samples showed a multi-phase system with swollen starch granules embedded in a protein network when 14 % starch was used, at moisture <63 %, as depicted by confocal microscopy. Tensile strength and cutting force tests showed a broad range of textures, from more brittle at high starch concentration, to softer and mushier when extruded at high moisture. Increasing starch and moisture content disrupted the protein network structure. This work demonstrated that milk protein concentrates show great potential to create novel anisotropic structures by extrusion, with tunable texture properties depending on starch, moisture and temperature conditions. [Display omitted] • The formation of anisotropic structures from milk protein concentrates was studied. • There was a competition between protein hydration and denaturation and starch gelation. • Tensile and cutting tests showed a broad range of textures, from tough to mushy. • Increasing starch and moisture content disrupted the protein network. • Texture was tunable by starch, barrel moisture and temperature conditions. [ABSTRACT FROM AUTHOR]

Thermal stability and physicochemical properties as a function of heating temperature, pH and salt addition was compared between caprine and bovine milk protein concentrate dispersions. Caprine milk protein concentrate (MPC) had a lower amount of heat coagulation time and a higher percentage of sediments than bovine MPC. Calcium ion activity of caprine MPC was higher than that of bovine. The amount of κ-casein in the serum of caprine MPC dispersions was higher than that of bovine, and increased with increasing temperatures, pH and the addition of NaCl and citrate. The amount of whey protein in serum was also higher in heated caprine MPC compared with bovine. Particle size of caprine MPC was larger than bovine MPC and was more susceptible to induced aggregation. The lower thermal stability of caprine MPC might be associated with the higher calcium ion activity and the higher amount of κ-casein dissociation promoted by whey protein denaturation and complexation in serum. [ABSTRACT FROM AUTHOR]