Heat stability of reconstituted, protein-standardized skim milk powders

We determined the effects of standardization material, protein content, and pH on the heat stability of reconstituted milk made from low-heat (LH) and medium-heat (MH) nonfat dry milk (NDM). Low-heat and MH NDM were standardized downward from 35.5% to 34, 32, and 30% protein by adding either edible lactose powder (ELP) or permeate powder (PP) from skim milk ultrafiltration. These powders were called standardized skim milk powders (SSMP). The LH and MH NDM and SSMP were reconstituted to 9% total solids. Furthermore, subsamples of reconstituted NDM and SSMP samples were set aside to measure heat stability at native (unadjusted) pH, and the rest were adjusted to pH 6.3 to 7.0. Heat stability is defined as heat coagulation time at 140°C of the reconstituted LH or MH NDM and SSMP samples. The entire experiment was replicated 3 times at unadjusted pH values and 2 times at adjusted pH values. At an unadjusted pH, powder type, standardization material, and protein content influenced the heat stability of the samples. Heat stability for reconstituted LH NDM and SSMP was higher than reconstituted MH NDM and SSMP. Generally, decreased heat stability was observed in reconstituted LH or MH SSMP as protein content was decreased by standardization. However, adding ELP to MH SSMP did not significantly change its heat stability. When pH was adjusted to values between 6.3 and 7.0, powder type, standardization material, and pH had a significant effect on heat stability, whereas protein content did not. Maximum heat stability was noted at pH 6.7 for both reconstituted LH NDM and SSMP samples, and at pH 6.6 for both reconstituted MH NDM and SSMP samples. Furthermore, for samples with adjusted pH, higher heat stability was observed for reconstituted LH SSMP containing PP compared with reconstituted milk from LH SSMP containing ELP. However, no statistical difference was observed in the heat stability of reconstituted milk from MH NDM and MH SSMP samples. We conclude that powder type (LH or MH) and effect of standardization material (ELP or PP) can help explain differences in heat stability. The difference in the heat stability of powder type may be associated with the difference in the pH of maximum heat stability and compositional differences in the standardization material (ELP or PP).     

Effects of milk heat treatment and solvent composition on physicochemical and selected functional characteristics of milk protein concentrate

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.     

Short communication: influence of transglutaminase on the heat stability of milk.

Skim milk powders were prepared from control and transglutaminase-treated skimmed milk. The heat stability of reconstituted transglutaminase-treated skimmed milk (9.0% total solids) was markedly increased in the pH region of minimum stability (pH 6.8 to 7.1) compared with control milk, while the heat stability of reconstituted concentrated transglutaminase-treated skimmed milk (22.5% total solids) increased progressively as a function of pH relative to control milk. The effect of transglutaminase treatment on the heat stability of skimmed milk may have commercial applications, but extensive research is necessary to gain a better understanding of the mechanism by which transglutaminase improves heat stability.     

Acid gelation of reconstituted milk protein concentrate suspensions: Influence of lactose addition

Dispersions (4%, w/w, protein) of reconstituted milk protein concentrate (MPC) powders varying in protein content (35–90% protein on dry matter basis) were standardized to a lactose content that was either unadjusted, 5.6 or 11.2% (w/w) and then heated at 90 °C for 10 min at pH 6.7. Protein interactions in heated milk and rheological properties and microstructure of acid gels formed by the addition of glucono-delta-lactone (GDL) were studied. Heat-induced dissociation of κ-casein was influenced by the lactose content of dispersions made from high protein MPC powders. A decrease in elastic moduli (G′) of acid gels at pH 4.6 with increasing MPC protein content was offset by lactose standardization of the dispersions. An increase in gelation pH and in water holding capacity of acid gels was observed with lactose standardization of dispersions. Confocal microscopy revealed a decrease in porosity of acid gels with increasing lactose content of MPC dispersions.     

Thermal stability of soy protein isolate and hydrolysate ingredients

The objective of this study was to characterize the effects of pH, protein concentration and calcium supplementation on thermal stability, at 140 °C, of soy protein isolate (SPI) and soy protein hydrolysate (SPH) ingredients. Increasing pH between 6.4 and 7.5 led to significantly (p < 0.05) higher mean heat coagulation times (HCTs) at 140 °C, for all soy protein ingredients at 1.8, and 3.6% (w/v) protein. Increasing protein concentration from 1.8 to 7.2% (w/v) led to shorter HCTs for protein dispersions. Calcium supplementation up to 850 mg/L, except in the case of supplementation of SPI 1 with calcium citrate (CaCit), decreased HCT for soy protein ingredient dispersions, at pH 6.4 – 7.5. No significant differences (p < 0.05) were found in mean HCT for dispersions supplemented with calcium chloride (CaCl₂) and those supplemented with CaCit at 450, 650 and 850 mg/L Ca²⁺, in the pH range 6.4–7.5.     

Impact of source and level of calcium fortification on the heat stability of reconstituted skim milk powder

Calcium enrichment of food and dairy products has gained interest with the increased awareness about the importance of higher calcium intake. Calcium plays many important roles in the human body. Dairy products are an excellent source of dietary calcium, which can be further fortified with calcium salts to achieve higher calcium intake per serving. However, the addition of calcium salts can destabilize food systems unless conditions are carefully controlled. The effect of calcium fortification on the heat stability of reconstituted skim milk was evaluated, using reconstituted skim milks with 2 protein levels: 1.75 and 3.5% (wt/wt) prepared using low and high heat powders. Calcium carbonate, phosphate, lactate, and citrate were used for fortification at 0.15, 0.18, and 0.24% (wt/wt). Each sample was analyzed for solubility, heat stability, and pH. The addition of phosphate and lactate salts lowered the pH of milk, citrate did not have any major effect, and carbonate for the 1.75% protein samples increased the pH. In general, changes in solubility and heat stability were associated with changes in pH. Calcium addition decreased the solubility and heat stability. However, interestingly, the presence of carbonate salt greatly increased the heat stability for 1.75% protein samples. This is due to the neutralizing effect of calcium carbonate when it goes into solution. The results suggested that the heat stability of milk can be affected by the type of calcium salt used. This may be applied to the development of milk-based calcium enriched beverages.     

Changes in the physical properties,solubility, and heat stability of milk protein concentrates prepared from partially acidified milk

A limiting factor in using milk protein concentrates (MPC) as a high-quality protein source for different food applications is their poor reconstitutability. Solubilization of colloidal calcium phosphate (CCP) from casein micelles during membrane filtration (e.g., through acidification) may affect the structural organization of these protein particles and consequently the rehydration and functional properties of the resulting MPC powder. The main objective of this study was to investigate the effects of acidification of milk by glucono-δ-lactone (GDL) before ultrafiltration (UF) on the composition, physical properties, solubility, and thermal stability (after reconstitution) of MPC powders. The MPC samples were manufactured in duplicate, either by UF (65% protein, MPC65) or by UF followed by diafiltration (80% protein, MPC80), using pasteurized skim milk, at either the native milk pH (~pH 6.6) or at pH 6.0 after addition of GDL, followed by spray drying. Samples of different treatments were reconstituted at 5% (wt/wt) protein to compare their solubility and thermal stability. Powders were tested in duplicate for basic composition, calcium content, reconstitutability, particle size, particle density, and microstructure. Acidification of milk did not have any significant effect on the proximate composition, particle size, particle density, or surface morphology of the MPC powders; however, the total calcium content of MPC80 decreased significantly with acidification (from 1.84 ± 0.03 to 1.59 ± 0.03 g/100 g of powder). Calcium-depleted MPC80 powders were also more soluble than the control powders. Diafiltered dispersions were significantly less heat stable (at 120°C) than UF samples when dissolved at 5% solids. The present work contributes to a better understanding of the differences in MPC commonly observed during processing.     

Preservation of raw milk with CO2

The effect of CO₂ on the growth of psychrotrophic milk spoilage organisms was studied, both in raw fresh milk and in pure cultures of three species ofPseudomonas growing in sterilised milk. Changes of sensory properties of CO₂-treated samples after heat treatment were also analysed. Inhibition of psychrotrophic growth at 7 °C in milk treated with CO₂ to a pH 6.2 or 6.0 was impaired by a gradual reduction of the CO₂ content during storage. Growth inhibition was considerably improved by pH adjustment at 24-h intervals. Sensory analysis showed significant differences between non-acidified and acidified samples after heat treatment at 75 °C for 20 s or 110 °C for 5 min. No sensory differences were found between non-acidified and acidified milks degassed before heat treatment.     

Effect of Fortification with Various Types of Milk Proteins on the Rheological Properties and Permeability of Nonfat Set Yogurt

ABSTRACT: Yogurt base was prepared from reconstituted skim milk powder (SMP) with 2.5% protein and fortified with additional 1% protein (wt/wt) from 4 different milk protein sources: SMP, milk protein isolate (MPI), micellar casein (MC), and sodium caseinate (NaCN). Heat‐treated yogurt mixes were fermented at 40 °C with a commercial yogurt culture until pH 4.6. During fermentation pH was monitored, and storage modulus (G′) and loss tangent (LT) were measured using dynamic oscillatory rheology. Yield stress (σ_yield) and permeability of gels were analyzed at pH 4.6. Addition of NaCN significantly reduced buffering capacity of yogurt mix by apparently solubilizing part of the indigenous colloidal calcium phosphate (CCP) in reconstituted SMP. Use of different types of milk protein did not affect pH development except for MC, which had the slowest fermentation due to its very high buffering. NaCN‐fortified yogurt had the highest G′ and σ_yield values at pH 4.6, as well as maximum LT values. Partial removal of CCP by NaCN before fermentation may have increased rearrangements in yogurt gel. Soluble casein molecules in NaCN‐fortified milks may have helped to increase G′ and LT values of yogurt gels by increasing the number of cross‐links between strands. Use of MC increased the CCP content but resulted in low G′ and σ_yield at pH 4.6, high LT and high permeability. The G′ value at pH 4.6 of yogurts increased in the order: SMP = MC < MPI < NaCN. Type of milk protein used to standardize the protein content had a significant impact on physical properties of yogurt. Practical Application: In yogurt processing, it is common to add additional milk solids to improve viscosity and textural attributes. There are many different types of milk protein powders that could potentially be used for fortification purposes. This study suggests that the type of milk protein used for fortification impacts yogurt properties and sodium caseinate gave the best textural results.     

Rheological properties of rennet gels containing milk protein concentrates

Different milk protein concentrates (MPC), with protein concentrations of 56, 70, and 90%, were dispersed in water under different treatments (hydration, shear, heat, and overnight storage at 4°C), as well as in a combination of all the treatments in a factorial design. The particle size distribution of the dispersions was then measured to determine the optimal conditions for the dispersion. Heating at 60°C for 30 min with 5 min of shear was chosen as the best condition to dissolve MPC powders. The samples were also characterized for composition, presence of protein aggregates, and ratio of calcium to protein. The total calcium present in MPC increased with increasing concentration of protein; however, the total calcium-to-protein ratio was lower in MPC90 than in MPC56 and MPC70. The level of whey protein denaturation, the presence of κ-casein-whey protein aggregates in the supernatant after centrifugation, and the amount of caseins dissociated from the micelle increased as the protein concentration in the powder increased. The total amount of casein macropeptide released was lower in samples from powders with a higher protein concentration than for MPC56 or the skim milk control. The gelation behavior of reconstituted MPC was tested in systems dispersed in water (5% protein) as well as in systems dispersed in skim milk (6% protein). The gelation time of MPC dispersions was considerably lower and the gel modulus was higher than those of reconstituted skim milk with the same protein concentration. When MPC dispersions were dialyzed against skim milk, a significant decrease in the gelation time and modulus were shown, with a complete loss of gelling functionality in MPC90 dispersed in water. This demonstrated that the ionic equilibrium was key to the functionality of MPC.     

Effect of pH at heat treatment on the hydrolysis of κ-casein and the gelation of skim milk by chymosin

Skim milk was adjusted to pH values between 6.5 and 7.1 and heated at 90 °C for times from 0 to 30 min. After heat treatment, the samples were re-adjusted to the natural pH (pH 6.67) and allowed to re-equilibrate. High levels of denatured whey proteins associated with the casein micelles during heating at pH 6.5 (about 70-80% of the total after 30 min of heating). This level decreased as the pH at heating was increased, so that about 30%, 20% and 10% of the denatured whey protein was associated with the casein micelles after 30 min of heating at pH 6.7, 6.9 and 7.1, respectively. Increasing levels of κ-casein were transferred to the serum as the pH at heating was increased. The loss of κ-casein and the formation of para-κ-casein with time as a consequence of the chymosin treatment of the milk samples were monitored by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The loss of κ-casein and the formation of para-κ-casein were similar for the unheated and heated samples, regardless of the pH at heating or the heat treatment applied. Monitoring the gelation properties with time for the chymosin-treated milk samples indicated that the heat treatment of the milk markedly increased the gelation time and decreased the firmness (G^′) of the gels formed, regardless of whether the denatured whey proteins were associated with the casein micelles or in the milk serum. There was no effect of pH at heat treatment. These results suggest that the heat treatment of milk has only a small effect on the primary stage of the chymosin reaction (enzymatic phase). However, heat treatment has a marked effect on the secondary stage of this reaction (aggregation phase), and the effect is similar regardless of whether the denatured whey proteins are associated with the casein micelles or in the milk serum as nonsedimentable aggregates.     

Effects of reverse CO2 acidification cycles,calcium supplementation,pH adjustment and chilled storage on physico-chemical and rennet coagulation properties of reconstituted low- and medium-heat skim milk powders

The reversibility extent of one and two reverse CO₂ acidification cycles on the physico-chemical and rennet coagulation properties of milks reconstituted from low- (LH) or medium- (MH) heat skim powder, enriched or not with calcium and pH adjusted or not was investigated. The ionized calcium concentration, buffering properties and average casein micelle size of untreated and CO₂-treated milks were evaluated before and after a chilled storage for 2 days. The ionized calcium concentration and buffering properties have been modified by the CO₂-treatment, particularly after a second CO₂-cycle. These modifications were highly dependent on the initial milk properties and chilled storage. Inversely, the average casein micelle size was not significantly changed. In addition, the rennet-clotting behaviour checked by near infrared spectroscopy (NIR-S) and rheology (SAOR) indicated the main factors responsible for changes in the casein micelles environment and dynamic casein micellar calcium phosphate reorganization, especially after two CO₂-cycles. A single CO₂-cycle induced a better rennetability for non Ca-enriched milk reconstituted from MH-powder. A second CO₂-cycle was particularly efficient to improve Ca-enriched pH-adjusted milks.     

Study on the compositional factors involved in the variable sensitivity of caprine milk to high-temperature processing

The heat sensitivity of individual caprine milk displayed considerable variation from one sample to another. Compared to heat-unstable milk samples, heat-stable milk samples were characterised by a higher pH, a lower soluble calcium concentration, a higher phosphorus concentration, and a higher whey protein content. The heat stability of caprine milk showed a marked pH dependence, but different patterns of heat stability vs. pH were observed between heat-stable and heat-unstable samples. Heat-stable milk samples had a maximum heat stability at pH 6.8, i.e. close to their natural pH, while heat-unstable milk samples had a maximum heat stability at pH 7–7.1, i.e. higher than their natural pH. The dependence on pH is discussed with respect to both the milk salt balance and the interaction of whey protein with casein.     

Heat stability of transglutaminase-treated milk

Heat-induced coagulation of unconcentrated (9%, w/w) and concentrated (18%, w/w) reconstituted skim milk was determined after incubation with transglutaminase (TGase). Cross-linking ∼20% of κ-casein strongly increased the heat stability of unconcentrated milk at pH >6.9, presumably by preventing heat-induced dissociation of κ-casein, whereas increased heat stability of unconcentrated milk at pH 6.6–6.8 was only observed when >80% of casein was cross-linked. Treatment with TGase reduced heat stability of unconcentrated milk at pH <6.6, presumably due to the increased susceptibility of partially cross-linked casein micelles to coagulation arising from heat-induced acidification. A low degree of cross-linking increased the heat stability of concentrated milk at pH >6.8, but more extensive cross-linking progressively reduced heat stability. The degree of cross-linking studied did not increase the heat-stability of concentrated milk at its natural pH. The outcomes of this study substantiate the crucial roles of heat-induced acidification and casein dissociation in heat stability of milk.     

INFLUENCE OF SODIUM PHOSPHATE ON THE HEAT STABILITY OF BUFFALO MILK AND ITS CONCENTRATE

The influence of three different concentrations, 0.05%, 0.10% and 0.15% of monobasic sodium phosphate on the heat stability (at 130°C) and pH of buffalo milk and its 2:1 concentrate was determined. It was observed that sodium phosphate caused a considerable increase in the heat stability, determined as heat coagulation time (HCT) of concentrated buffalo milk. The optimum concentration of sodium phosphate for imparting maximum stability to the concentrate was different for different samples. However, with the addition of an appropriate concentration of sodium phosphate it was possible to manufacture evaporated milk up to 36% total solids. Depending on the HCT/pH profile, some of the samples of fluid (unconcentrated) milk were stabilized while the others were destabilized due to the addition of sodium phosphate. Addition of monobasic sodium phosphate caused a decrease in the pH of fluid milk and its concentrate.     

Fortification of milk protein content with different dairy protein powders alters its compositional,rennet gelation,heat stability and ethanol stability characteristics

Skim milk (SM) was fortified from 3.3 to 4.1% protein using different milk protein powders: skim milk powder (SMP), native phosphocasein (NPC), calcium-reduced phosphocasein (CaRPC), sodium caseinate (NaCas) or calcium caseinate (CaCas). Compared with SMP or NPC, fortification with NaCas and CaRPC, and to a lesser extent CaCas, resulted in milk samples having higher proportions of non-sedimentable casein and calcium, and lower- and higher-levels of κ- and α_S1-casein, respectively, as a proportion of non-sedimentable casein. These changes coincided in milk samples fortified with NaCas, CaRPC or CaCas failing to undergo rennet-induced gelation, and having higher heat stability in the region 6.7–7.2 and ethanol stability at pH 6.4. The study demonstrates that the aggregation behaviour of protein-fortified milk samples is strongly influenced by the degree of mineralisation of the protein powder used in fortification, which affects the partitioning of casein and calcium in the sedimentable and non-sedimentable phases.     

Manufacture of cheese made from CO2-treated milk

Cheeses were manufactured from pasteurised milk (control), pasteurised milk acidified to pH 6.0 with CO₂, and milk acidified to pH 6.0 with CO₂ prior to pasteurisation. Production of cheese from CO₂-treated milk at pH 6.0 reduced the amount of rennet necessary for coagulation by about 75%. Although acidification reduces the amount of lactic acid produced by starter during incubation of milk, no significant differences in lactic acid content were detected between cheeses manufactured from non-acidified or CO₂-acidified milks. Cheeses produced from CO₂-treated milk showed less proteolysis than control cheeses, but no significant differences in sensory characteristics between cheeses were detected.     

Effect of NaCl on some physico-chemical properties of concentrated bovine milk

The influence of added NaCl (75–850 mmol L⁻¹) on some physicochemical properties of 2× or 3× concentrated milk (18 or 27%, w/v, total solids, respectively) was investigated. Adding NaCl did not influence average casein micelle size, but reduced the net-negative charge on the casein micelles and milk pH. The level of soluble and ionic calcium was increased by addition of NaCl, but the level of soluble inorganic phosphorus was not influenced. Addition of NaCl shifted the maximum in the pH–heat coagulation time (HCT) profile of 2× or 3× concentrated milk to a higher pH value and certain concentrations increased the maximum HCT, probably due to the fact that NaCl reduced the extent of heat-induced dissociation of κ-casein. Added NaCl reduced the ethanol stability, with the extent of this effect increasing with the concentration of NaCl. The key-mechanism though which added NaCl induces changes in the physico-chemical stability of casein micelles appears to be through changes in the charge on the casein micelles.     

Influence of added lyophilized butter serum on the heat stability of unconcentrated and concentrated bovine milk

The influence of added lyophilized butter serum on the heat stability of milk was investigated. The addition of lyophilized serum from salted butter to unconcentrated skimmed milk (SM) reduced the heat coagulation time (HCT) at, and increased the pH of, the maximum in the pH–HCT profile and caused disappearance of the minimum. NaCl had similar effects on the heat stability of SM as lyophilized salted butter serum, whereas lyophilized serum from unsalted butter had little effect. The addition of lyophilized salted butter serum to concentrated skimmed milk (CSM) also shifted the pH of maximum heat stability to a higher value and, at certain concentrations, increased the maximum HCT; similar effects were obtained on addition of NaCl, but lyophilized serum from unsalted butter had little effect. These results suggest that the effects of lyophilized serum from salted butter on the heat stability of SM or CSM are due primarily to the presence of a high level of NaCl in this serum.     

The two-stage coagulation of milk proteins in the minimum of the heat coagulation time-pH profile of milk: effect of casein micelle size

Milks with casein micelles larger or smaller than control milk were prepared by differential centrifugation. The heat stability of these modified milks increased markedly throughout the pH range 6.4 to 7.1 with decreasing casein micelle size. Within the region of the minimum in the heat coagulation time-pH profile, the control milk coagulated by a two-stage process, but the modified milks, because of their narrower casein micelle size distribution, coagulated by a single-stage process at the pH of minimum stability. The content of kappa-CN and protein hydration increased as the size of the casein micelles decreased, and the level of glycosylation of kappa-CN and protein surface hydrophobicity increased as a function of micelle size. The effect of casein micelle size on the heat stability of milk is likely to be related to changes in the above physico-chemical properties.