Physicochemical properties of micellar casein retentates generated at different microfiltration temperatures.

Processing temperature has a significant influence on the composition and functionality of the resulting streams following microfiltration (MF) of skim milk. In this study, MF and diafiltration (DF) were performed at 4 or 50°C to produce ß-casein (ß-CN)-depleted and nondepleted (i.e., native casein profile) micellar casein isolate retentates, respectively. Microfiltration combined with extensive DF resulted in a 40% depletion of ß-CN at 4°C, whereas no ß-CN depletion occurred at 50°C. Microfiltration at 4°C led to higher transmission of calcium into permeates, with retentate generated at 4°C containing less total calcium compared with retentate generated at 50°C, based on the volume of retentate remaining. Higher heat stability at 120°C was measured for retentates generated at 4°C compared with those at 50°C, across all pH values measured. Retentates generated at 4°C also had significantly lower ionic calcium values at each pH compared with those generated at 50°C. Higher apparent viscosities at 4°C were measured for retentates generated at 4°C compared with retentates generated at 50°C, likely due to increased voluminosity of ß-CN-depleted casein micelles. The results of this study provide new information on how changing the composition of MF retentate, by appropriate control of processing temperature and DF, can alter physicochemical properties of casein micelles, with potential implications for ingredient functionality.

Plant-Based Alternatives to Cheese Formulated Using Blends of Zein and Chickpea Protein Ingredients.

In this study, zein protein isolate (ZPI) and chickpea protein concentrate (CPC) ingredients were used to formulate five plant-based cheese alternatives. Ingredient ratios based on protein contributions of 0:100, 25:75, 50:50, 75:25 and 100:0 from ZPI and CPC, respectively, were used. Formulations were developed at pH ~4.5, with a moisture target of 59%. Shea butter was used to target 15% fat, while tapioca starch was added to target the same carbohydrate content for all samples. Microstructural analysis showed differences among samples, with samples containing ZPI displaying a protein-rich layer surrounding the fat globules. Schreiber meltability and dynamic low amplitude oscillatory shear rheological analyses showed that increasing the proportion of ZPI was associated with increasing meltability and greater ability to flow at high temperatures. In addition, the sample containing only CPC showed the highest adhesiveness, springiness and cohesiveness values from the texture profile analysis, while the sample containing only ZPI exhibited the highest hardness. Furthermore, stretchability increased with increasing ZPI proportions. This work will help understanding of the role and potential of promising plant-protein-ingredient blends in formulating plant-based alternatives to cheese with desirable functional properties.

Structural, Binding and Functional Properties of Milk Protein-Polyphenol Systems: A Review.

Polyphenols (PP) are linked to health benefits (e.g., prevention of cancer, cardiovascular disease and obesity), which are mainly attributed to their antioxidant activity. During digestion, PP are oxidised to a significant degree reducing their bio-functionality. In recent years, the potential of various milk protein systems, including ß-casein micelles, ß-lactoglobulin aggregates, blood serum albumin aggregates, native casein micelles and re-assembled casein micelles, to bind and protect PP have been investigated. These studies have yet to be systematically reviewed. The functional properties of the milk protein-PP systems depend on the type and concentration of both PP and protein, as well as the structure of the resultant complexes, with environmental and processing factors also having an influence. Milk protein systems protect PP from degradation during digestion, resulting in a higher bioaccessibility and bioavailability, which improve the functional properties of PP upon consumption. This review compares different milk protein systems in terms of physicochemical properties, PP binding performance and ability to enhance the bio-functional properties of PP. The goal is to provide a comprehensive overview on the structural, binding, and functional properties of milk protein-polyphenol systems. It is concluded that milk protein complexes function effectively as delivery systems for PP, protecting PP from oxidation during digestion.

Cold Microfiltration as an Enabler of Sustainable Dairy Protein Ingredient Innovation.

Classically, microfiltration (0.1-0.5 µm) of bovine skim milk is performed at warm temperatures (45-55 °C), to produce micellar casein and milk-derived whey protein ingredients. Microfiltration at these temperatures is associated with high initial permeate flux and allows for the retention of the casein fraction, resulting in a whey protein fraction of high purity. Increasingly, however, the microfiltration of skim milk and other dairy streams at low temperatures (≤20 °C) is being used in the dairy industry. The trend towards cold filtration has arisen due to associated benefits of improved microbial quality and reduced fouling, allowing for extended processing times, improved product quality and opportunities for more sustainable processing. Performing microfiltration of skim milk at low temperatures also alters the protein profile and mineral composition of the resulting processing streams, allowing for the generation of new ingredients. However, the use of low processing temperatures is associated with high mechanical energy consumption to compensate for the increased viscosity, and thermal energy consumption for inline cooling, impacting the sustainability of the process. This review will examine the differences between warm and cold microfiltration in terms of membrane performance, partitioning of bovine milk constituents, microbial growth, ingredient innovation and process sustainability.

The Effect of Compositional Changes Due to Seasonal Variation on Milk Density and the Determination of Season-Based Density Conversion Factors for Use in the Dairy Industry.

The objective of this study was to determine the effect of seasonal variation on milk composition and establish an algorithm to predict density based on milk composition to enable the calculation of season-based density conversion calculations. A total of 1035 raw whole milk samples were collected from morning and evening milking of 60 spring-calving individual cows of different genetic groups, namely Jersey, Elite HF (Holstein-Friesian) and National Average HF, once every two weeks for a period of 9 months (March-November, 2018). The average mean and standard deviation for milk compositional traits were 4.72 ± 1.30% fat, 3.85 ± 0.61% protein and 4.69 ± 0.30% lactose and density was estimated at 1.0308 ± 0.002 g/cm3. The density of the milk samples was evaluated using three methods: a portable density meter, DMA 35; a standard desktop version, DMA 4500M; and an Association of Official Agricultural Chemists (AOAC) method using 100-mL glass pycnometers. Statistical analysis using a linear mixed model showed a significant difference in density of milk samples (p < 0.05) across seasonal and compositional variations adjusted for the effects of days in milk, parity, the feeding treatment, the genetic group and the measurement technique. The mean density values and standard error of mean estimated for milk samples in each season, i.e., spring, summer and autumn were 1.0304 ± 0.00008 g/cm3, 1.0314 ± 0.00005 g/cm3 and 1.0309 ± 0.00007 g/cm3, respectively.

Colloidal properties of protein complexes formed in ß-casein concentrate solutions as influenced by heating and cooling in the presence of different solutes.

Monomeric bovine ß-casein self-associates into micelles under appropriate conditions of protein concentration, serum composition and temperature. The present study investigated self-association characteristics of a ß-casein concentrate (BCC) prepared from milk at pilot-scale using membrane filtration. The BCC had a casein:whey protein ratio of 77:23, with ∼95% of casein consisting of ß-casein, and the remainder being mostly κ-CN. BCC was reconstituted to 1.2% protein (a typical level in infant formula) in various liquid media at pH 6.8 and incubated at different temperatures from 4 to 63 °C for 30 min. Self-association of ß-casein on heating was thermo-reversible in deionised water, lactose (4, 6 or 8%) or calcium (9 mM) solutions. In most serum phases, BCC became highly opaque after incubation at 63 °C, but clarified rapidly during cooling to 25 °C. However, in simulated milk ultrafiltrate (SMUF), which has a high ionic strength and is supersaturated in calcium phosphate (CaP), BCC remained opaque during cooling to 25 °C, and retained residual turbidity after 15 h of holding at 4 °C; if SMUF was prepared without phosphate then turbidity development in BCC solutions was markedly reduced. The complexes responsible for this turbidity development were successfully dissociated with 50 mM trisodium citrate. Analysis of pH during heating and holding at 60 °C indicated that SMUF acidified continuously under the period of study, while acidification in BCC/SMUF mixtures terminated after a short period, indicating that the type of CaP formed on heating is altered in the presence of BCC. This study demonstrates that BCC ingredients exhibit pronounced temperature-dependant changes in colloidal properties that are strongly affected by the presence of minerals commonly found in nutritional product formulations.

Short communication: Multi-component interactions causing solidification during industrial-scale manufacture of pre-crystallized acid whey powders.

Acid whey (AW) is the liquid co-product arising from acid-induced precipitation of casein from skim milk. Further processing of AW is often challenging due to its high mineral content, which can promote aggregation of whey proteins, which contributes to high viscosity of the liquid concentrate during subsequent lactose crystallization and drying steps. This study focuses on mineral precipitation, protein aggregation, and lactose crystallization in liquid AW concentrates (∼55% total solids), and on the microstructure of the final powders from 2 independent industrial-scale trials. These AW concentrates were observed to solidify either during processing or during storage (24 h) of pre-crystallized concentrate. The more rapid solidification in the former was associated with a greater extent of lactose crystallization and a higher ash-to-protein ratio in that concentrate. Confocal laser scanning microscopy analysis indicated the presence of a loose network of protein aggregates (≤10 µm) and lactose crystals (100-300 µm) distributed throughout the solidified AW concentrate. Mineral-based precipitate was also evident, using scanning electron microscopy, at the surface of AW powder particles, indicating the formation of insoluble calcium phosphate during processing. These results provide new information on the composition- and process-dependent physicochemical changes that are useful in designing and optimizing processes for AW.

Impact of α-lactalbumin:ß-lactoglobulin ratio on the heat stability of model infant milk formula protein systems.

Model infant milk formula systems (5.5% protein) were formulated to contain α-lactalbumin:ß-lactoglobulin ratios of 0.1, 0.5, 1.3, 2.1 or 4.6 and assessed for heat stability and heat-induced changes. 'Humanising' the model formulas by increasing α-lactalbumin:ß-lactoglobulin enhanced heat stability at 140°C in the pH range 6.6-6.9. The model formulas were analysed after lab-scale high-temperature short-time heating at pH 6.8. Gel electrophoresis indicated that increased heat stability in high α-lactalbumin:ß-lactoglobulin samples was due to decreased covalent interactions between proteins. In low α-lactalbumin:ß-lactoglobulin formulas, protein-protein interactions caused marked increases in protein particle size and viscosity of the heated systems; conversely, covalent interactions between proteins were minimal in high α-lactalbumin:ß-lactoglobulin formulas. Reduced protein-protein interactions with increasing α-lactalbumin:ß-lactoglobulin has important implications for subsequent processing; for example, lower viscosity post-heating may affect bulk density in spray-dried products or physical stability in ready-to-feed products.