Influence of sodium hexametaphosphate addition on the functional properties of milk protein concentrate solutions containing transglutaminase cross-linked proteins

Micellar casein concentrate (MCC) is a high protein ingredient (obtained by microfiltration of skim milk) with an elevated level of casein as a percentage of total protein (TP) compared to skim milk. It can be used as an ingredient in cheese making. Feta-type cheese is a brined soft cheese with a salty taste and acid flavor. We theorize that Feta-type cheese can be produced from MCC instead of milk, which can improve the efficiency of manufacture and allow for the removal of whey proteins before manufacturing Feta-type cheese. The objectives of this study were to develop a process of producing Feta-type cheese from MCC and to determine the optimum protein content in MCC to make Feta-type cheese. MCC solutions with 3% (MCC-3), 6% (MCC-6), and 9% (MCC-9) protein were prepared and standardized by mixing water, MCC powder, milk permeate, and cream to produce a solution with 14.7% total solids (TS) and 3.3% fat. Thermophilic cultures were added at a rate of 0.4% to MCC solutions and incubated at 35 °C for 3 h to get a pH of 6.1. Subsequently, calcium chloride and rennet were added to set the curd in 20 min at 35 °C. The curd was then cut into cubes, drained for 20 h followed by brining in 23% sodium chloride solutions for 24 h. Compositional analysis of MCC solutions and cheese was carried out. The yield, color, textural, and rheological measurements of Feta-type cheese were evaluated. Feta-type cheese was also made from whole milk as a control. This experiment was repeated three times. The yield and adjusted yield of Feta-type cheese increased from 19.0 to 54.8 and 21.4 to 56.5, respectively, with increasing the protein content in MCC from 3% to 9%. However, increasing the protein content in MCC did not show significant differences in the hardness (9.2–9.7 kg) of Feta-type cheese. The color of Feta-type cheese was less white with increasing the protein content in MCC. While the yellowish and greenish colors were high in Feta-type cheese made from MCC with 3% and 6% protein, no visible differences were found in the overall cheese color. The rheological characteristics were improved in Feta-type cheese made from MCC with 6% protein. We conclude that MCC with different levels of protein can be utilized in the manufacture of Feta-type cheese.

“…A Minolta Spectrophotometer (CM-508d, Minolta camera Co., Ltd., Osaka, Japan) was used to measure the color of the cheese [ 36 , 37 ]. The color test was performed in triplicate.…”

Section: Methodsmentioning

confidence: 99%

“…The a* value represents a range of −60 (green) to +60 (red), while the b* value has a range of −60 (blue) to +60 (yellow). The color difference (ΔΕ), which refers to the change in visual perception of colors, was also calculated as described in Power’s study using Equation (3) [ 36 ]:

…”

Section: Methodsmentioning

confidence: 99%

Compositional and Functional Characteristics of Feta-Type Cheese Made from Micellar Casein Concentrate

Hammam

Kapoor

Salunke

et al. 2021

“…However, such mechanical processes are energy-intensive and require an adjustment in process lines, adding capital expenditure and processing complexity [3]. Although alteration of chemical interactions between caseins by chelating calcium using sodium hexametaphosphate and maintaining casein integrity by treatment with polygalacturonase enzyme [15], pH adjustment to an alkaline range [29], or by dry blending MPI powder with sodium caseinate [35] show promising results for enhanced rehydration, these techniques involve chemical addition or generate non-micellar caseins that are normally undesirable for many applications. The results from the present study show the potential that formulation of MCC solutions with GMP enhances powder particle disintegration during rehydration through the use of dairy-based food ingredients with potential benefits from a nutritional perspective.…”

Section: Casein and Glycomacropeptide Solubilization In Aqueous Phase During Powder Dispersionmentioning

confidence: 99%

“…Sun et al [13] added 0.3% salts (sodium citrate, sodium pyrophosphate, and sodium phosphate) to ultrafiltration retentate, reporting improved rehydration properties of resultant MPC powder. However, use of such additives generally impairs the processing characteristics (e.g., high viscosity), functionality (e.g., reduced casein micelle integrity) [14,15], or nutritional significance of protein enrichment.…”

Section: Introductionmentioning

confidence: 99%

Influence of Glycomacropeptide on Rehydration Characteristics of Micellar Casein Concentrate Powder

Panthi

Bot

O’Mahony

2021

Glycomacropeptide (GMP) shows potential for enhancing the rehydration properties of high-protein dairy powders due to its hydrophilic nature. This study involved formulating micellar casein concentrate (MCC) solutions (8.6% final protein content) with 0, 10, and 20% GMP as a percentage of total protein, and investigated the physicochemical and rehydration properties of the resultant freeze-dried powders (P-MCC-0G, P-MCC-10G, and P-MCC-20G, respectively). The surface charges of caseins in the control MCC and 10 or 20% GMP blended solutions were −25.8, −29.6, and −31.5 mV, respectively. Tablets prepared from P-MCC-10G or P-MCC-20G powders displayed enhanced wettability with contact angle values of 80.6° and 79.5°, respectively, compared with 85.5° for P-MCC-0G. Moreover, blending of GMP with MCC resulted in faster disintegration of powder particles during rehydration (i.e., dispersibility) compared to P-MCC-0G. Faster and more extensive release of caseins from powder particles into solution was evident with the increasing proportion of GMP, with the majority of GMP released within the first 15 min of rehydration. The results of this study will contribute to further development of formulation science for achieving enhanced solubility characteristics of high-protein dairy powder ingredients, such as MCC.

“…The studies relating to mTG crosslinking of micellar casein concentrate and the subsequent effects on its functional properties are limited; however, milk protein concentrate (MPC) powder crosslinked with mTG (0.5 g/L, 30 °C, 24 h) has been found to have improved wettability and water sorption [ 27 ]. Moreover, viscosity increase was also shown to be controlled in MPC suspension (10% w/w ) with added calcium chelating salts after crosslinking with mTG [ 28 ]. The activity of mTG on individual caseins is influenced by the accessibility of individual caseins within micellar systems [ 29 ].…”

Section: Introductionmentioning

confidence: 99%

Influence of Transglutaminase Crosslinking on Casein Protein Fractionation during Low Temperature Microfiltration

Puri

Bot

Singh³

et al. 2021

Low temperature microfiltration (MF) is applied in dairy processing to achieve higher protein and microbiological quality ingredients and to support ingredient innovation; however, low temperature reduces hydrophobic interactions between casein proteins and increases the solubility of colloidal calcium phosphate, promoting reversible dissociation of micellar β-casein into the serum phase, and thus into permeate, during MF. Crosslinking of casein proteins using transglutaminase was studied as an approach to reduce the permeation of casein monomers, which typically results in reduced yield of protein in the retentate fraction. Two treatments (a) 5 °C/24 h (TA) and (b) 40 °C/90 min (TB), were applied to the feed before filtration at 5 °C, with a 0.1 µm membrane. Flux was high for TA treatment possibly due to the stabilising effect of transglutaminase on casein micelles. It is likely that formation of isopeptide bonds within and on the surface of micelles results in the micelles being less readily available for protein-protein and protein–membrane interactions, resulting in less resistance to membrane pores and flow passage, thereby conferring higher permeate flux. The results also showed that permeation of casein monomers into the permeate was significantly reduced after both enzymatic treatments as compared to control feed due to the reduced molecular mobility of soluble casein, mainly β-casein, caused by transglutaminase crosslinking.