Casein micelle system

Van der Waals forces There has been some success in relating these forces to micellar stability. However, the steric stabilization has been found to be also of some importance. Especially, the hairy layer interferes with the interparticle approach. There are several factors that will affect the stability of the casein micelle system ... 

The major defect, which limits exploitation of frozen milk concentrates as consumer products, is the instability of the casein micelle system (Keeney and Kroger 1974 Morr 1975). The casein micelles gradually destabilize during storage of the frozen milk concentrate. 

The physical stability of the casein micelle system is closely related to the degree of lactose crystallization from the unfrozen phase of the frozen concentrate. Crystallization of lactose from the unfrozen solution temporarily raises its freezing point, causing additional water to freeze, thus increasing the concentration and promoting destabilization of casein micelles. 

The effect of protein methylation (20% modification) on the stability of casein micelles was evaluated. The stability of the clJk micelle system towards Ca2+ precipitation was decreased when either or both proteins were methylated (see Figure 1). Methylation also resulted in a slight reduction in the stability of the /3-k casein micelle system (see Figure 2). 

The temperature-sensitive precipitation of unmodified and methylated /3-caseins in the presence of calcium was measured also (see Figure 3). Methylation caused an increase of up to 3°C in the precipitation temperature of calcium /3-caseinate. Results from rennet clotting of an asi-K casein micelle system indicated that replacing native asi-casein with the reductively methylated protein had little influence on clotting time, while replacing K-casein with its reductively methylated derivative re-... 

K-casein also contains two Cys residues per monomer subunit and is thus capable of interacting with the whey proteins, e.g., mainly g-lactoglobulin, via the disulfide interchange mechanism at temperatures at or above 65°C. This latter phenomenon is believed to be important in providing colloidal stability to the milk casein micelle system, as well as to the whey proteins, in high temperature processed milk products. It has also been postulated that this latter interaction with g-lactoglobulin may alter the availability of K-casein in the micelle, and thus has a detrimental effect upon the cheese making properties of milk (4). 

Schmidt, D. G., and Poll, J. K. (1986). Electrophoretic measurements of unheated and heated casein micelle systems. Neth. Milk Dairy J. 40, 269-280. 

Spagnuolo, P. A., Dalgleish, D. G., Goff, H. D., and Morris, E. R. (2005). Kappa-carrageenan interactions in systems containing casein micelles and polysaccharide stabilizers. Food Hydrocolloids 19,371-377. 

Nature itself gives us a spectacular example of a biopolymer-based delivery system in the form of the native casein micelle of mammalian milk (Lemay et al, 2007). This is primarily a colloidal delivery system for calcium, where the micronutrient is in the form of calcium phosphate, which does not give a bitter taste, and which provides good bioavailability owing to its colloidal size, amorphous state and quick dissolution in gastric conditions (pH 1-2). Nevertheless, the casein micelle structure is unique there are no other readily available natural delivery systems for most nutraceuticals. Therefore some new designs are clearly required (Velikov and Pelan, 2008 McClements et al, 2008, 2009). 

We have seen earlier in this chapter how the self-assembly of casein systems is sensitively affected by temperature. Another thermodynamic variable that can affect protein-protein interactions in aqueous media is the hydrostatic pressure. Static high-pressure treatment causes the disintegration of casein micelles due to the dismption of internal hydro-phobic interactions and the dissociation of colloidal calcium phosphate. This phenomenon has been used to modify the gelation ability of casein without acidification as a consequence of exposure of hydrophobic parts of the casein molecules into the aqueous medium from the interior of the native casein micelles (Dickinson, 2006). High-pressure treatment leads to a reduction in the casein concentration required for gelation under neutral conditions, especially in the presence of cosolutes such as sucrose (Abbasi and Dickinson, 2001, 2002, 2004 Keenan et al., 2001). 

Experiments on interactions of polysaccharides with casein micelles show similar trends to those with casein-coated droplets. For example, Maroziene and de Kruif (2000) demonstrated the pH-reversible adsorption of pectin molecules onto casein micelles at pH = 5.3, with bridging flocculation of casein micelles observed at low polysaccharide concentrations. In turn, Tromp et al. (2004) have found that complexes of casein micelles with adsorbed high-methoxy pectin (DE = 72.2%) form a self-supporting network which can provide colloidal stability in acidified milk drinks. It was inferred that non-adsorbed pectin in the serum was linked to this network owing to the absence of mobility of all the pectin in the micellar casein dispersion. Hence it seems that the presence of non-adsorbed pectin is not needed to maintain stability of an acid milk drink system. It was stated by Tromp et al. (2004) that the adsorption of pectin was irreversible in practical terms, i.e., the polysaccharide did not desorb under the influence of thermal motion. 

Co-preclpltate is an insoluble milk protein product that is produced by heating skinimllk to high temperatures ( > 90 C) to denature the whey proteins and complex them with the casein micelles. The heated system is subsequently adjusted to isoelectric point conditions of pH 4.5-5 to precipitate the complexed whey protein-casein micelles, centrifuged or filtered to recover the precipitate, washed and dryed. The resulting product, which is virtually insoluble, exhibits only minor functionality in most typical emulsification applications. 

Stability of the complex protein system of milk or whey is decreased by concentration (Fox 1982 Muir and Sweetsur 1978 Sweetsur and Muir 1980B). In addition to closer packing of casein micelles and other proteins in concentrated milk, calcium phosphate is precipitated so that the pH decreases (Fox 1982). The pH effect causes protein which would be soluble at a normal solids concentration to precipitate. Casein in milk concentrated to three times its original solids level forms a flocculent after 1 to 3 weeks at -8°C (Lonergan 1978). 

It is necessary to forewarm milk to impart adequate heat stability to the concentrate to permit it to withstand subsequent sterilization treatments. The heat-induced casein micelle-whey protein complexes in forewarmed milk are less sensitive to heat than native whey proteins and thus provide the required stability to the concentrate. The forewarming treatment also stabilizes the milk mineral system by com-plexing Ca and Mg ions with casein micelles and by converting ionic forms to the less reactive form of colloidal phosphate (Morr 1975). 

The concentrated milk is homogenized at 140 to 210 kg/cm2 (2000 to 3000 lb/in2) at about 48°C (Hall and Hedrick 1966). This process is essential to provide adequate physical stability to the milk fat emulsion system to withstand prolonged storage at room temperature (Brunner 1974). However, homogenization lowers the heat stability of concentrated milk products (Parry 1974), which may be due to increased adsorption of casein micelles onto the newly created milk fat globule surfaces, thus making them more sensitive to heat-induced aggregation. 

The ageing at 5°C of whippable emulsions such as ice cream mix will enhance the hydration of milk proteins in the system. This is due to a property of casein micelles in milk. At low temperatures, the hydration or voluminosity of casein increases. The voluminosity is the volume of hydrated protein per gram of protein. This can be studied by analyzing the protein and water content in the sedimented casein pellet after centrifugation of skimmed milk. 

Data analysis methods depend upon the level of order in the sample. The degree of order, in turn, depends upon the scale of distance on which the sample is viewed. For example, casein micelles show great variation in size (20 to 300 nm diameter) and so must be treated as a polydisperse system. However, the density variations ( submicelles ) within the whole micelle are much more uniform in size. They can be treated as a quasi-monodisperse system (Stothart and Cebula, 1982) and analyzed in terms of inter-particle interference (Stothart, 1989). 

It is difficult to obtain meaningful results on colloidal interactions unless the samples have low polydispersity. Studies of colloidal interactions between whole casein micelles can be affected by the polydispersity of native casein micelles. (Stothart,1987b). To circumvent the problem of polydispersity, the food system can be deposited on monodisperse silica spheres (Rouw and de Kruif,1989). 

Generally a decrease in the pH of milk systems prior to heating results in more association of the denatured whey proteins to the casein micelle (Corredig and Dalgleish, 1996 Oldfield et al., 2000 Vasbinder and de Kruif, 2003). Even small changes in pH can shift the distribution of the association of the denatured whey protein with the casein micelle. For example, at a level of 95% whey protein denaturation, there is 70% of the denatured whey proteins associated with the casein micelle at pH 6.55 and this is decreased to 30% when the pH of milk prior to heating was... 

Citrate salts have long been used in the processed cheese industry as "emulsifying salts," and there is still interest in the mechanism of their action. Shirashoji et al. (2006) examined the effects of trisodium citrate on the properties of processed cheese. Increasing concentration of sodium citrate decreased the size droplets of the cheese. This effect is typical when emulsifying properties of a system are improved. This is expected as the complexation of calcium by citrate causes dissociation of the casein micelle, making the casein more available for emulsifying fat droplets. This possibly contributed to the reinforcement of the structure of the processed cheese. 

---