Stabilizers caseins

No cysteine residues are found for alpha(sl) and P-caseins do. If any S-S bonds occur within the micelle, they are not the driving force for stabilization. Caseins are among the most hydrophobic proteins, and there is some evidence to suggest that they play a role in the stability of the micelle. It must be remembered that hydrophobic interactions are very temperature sensitive. 

Sejersen, M.T., Salomonsen, T., Ipsen, R., Clark, R., Rolin, C., Engelsen, S.B. (2007). Zeta potential of pectin-stabilized casein aggregates in acidified milk drinks. International Dairy Journal, 17, 302-307. 

Carrageenans complex with protein under conditions where carboxyl-ated polysaccharides do not (Tolstoguzov, 1986). One of their major applications is to stabilize casein in evaporated milk and dairy foods. 

We chose to prepare 14C-methyl-K-casein (M-k-C) as a tracer because of the important role of K-casein in stabilizing casein micelles (8) and because K-casein is known to participate in heat-induced interactions with whey proteins, thereby influencing the heat stability of milk (9). The reductive methylation radiolabeling procedure used low concentrations of reagents (10) and resulted in M-k-C containing approximately 1 fiinol of 14C-methyl groups for every micromole of protein monomer (about 3 /xCi/mg). When tracer M-k-C was added to skim milk, and trichloroacetic acid was added to a concentration of 2%, about 1% of the radioactivity remained soluble. After clotting of the milk with excess... 

Cryodestabilization of casein limits the commercial feasibility of frozen milk, which may be attractive in certain circumstances. However, cryode-stabilized casein might be commercially viable, especially if applied to milks concentrated by ultrafiltration, which are less stable than normal milk. Cryodestabilized casein may be processed in the usual way. The product is dispersible in water and can be reconstituted as micelles in water at 40°C, The heat stability and rennet coagulability of these micelles are generally similar to those of normal micelles and casein produced by cryodestabilization may be suitable for the production of fast-ripening cheeses, e.g. Mozzarella or Camembert, when the supply of fresh milk is inadequate. As far as we are aware, casein is not produced commercially by cryodestabilization. 

Phosphates, which react with calcium to reduce the calcium ion activity, assist in stabilizing calcium-sensitive proteins, eg caseinate and soy proteinate, during processing. Phosphates also react with milk proteins. The extent of the reaction depends upon chain length. Casein precipitates upon addition of pyrophosphates, whereas whey proteins do not. Longer-chain polyphosphates cause the precipitation of both casein and whey proteins. These reactions are complex and not fully understood. Functions of phosphates in different types of dairy substitutes are summarized in Table 9 (see also Food additives). 

At the pH = Jt there is a balance of charge and there is no migration in an electric field. This is referred to as the isoelectric point and is determined by the relative dissociation constants of the acidic and basic side groups and does not necessarily correspond to neutrality on the pH scale. The isoelectric point for casein is about pH = 4.6 and at this point colloidal stability is at a minimum. This fact is utilised in the acid coagulation techniques for separating casein from skimmed milk. 

Colorant containing annatto and Ca caseinate as carrier mixed with water to be added directly to cheese milk yielding uniform colored cheese mass Water-dispersible beadlet of p-carotene is mixed with oil to attein composition that remains stable even in presence of polyphosphates and with antioxidant action even in absence of ascorbic acid Blending carotenoid pigment and soybean fiber (wifii tomato juice) as effective ingredient for dispersion stability... 

Horne, D. S. (2009). Casein micelles structure and stability. In "Milk Proteins From Expression to Food", (A. Thompson, M. Boland, and H. Singh, Eds), pp. 133-179. Academic Press, San Diego. 

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. 

The elastic modulus (G ) of MP, BCAS, and BLG5 rapidly rose to plateaus that corresponded to different G saturations (Gjat) (Table 2). MP and BCAS coagula showed the more important Gsat value (142 N/m ), meaning that the emulsions stabilized by skim milk proteins (mainly casein micelles) and 6-casein formed the coagula with the strongest protein network. 

Reconstituted milks with natural milk fat globules (CREAM) or emulsified milk fat droplets stabilized by jS-casein (BCAS), /i-lactoglobulin 5g/L (BLG5), skim milk proteins (MP). 

Y. Hemar, D. N. Pinder, R. J. Hunter, H. Singh, P. Hebraud, D. S. Home 2003, (Monitoring of flocculation and creaming of sodium-caseinate-stabilized emulsions using diffusing-wave spectroscopy), /. Colloid Interface Sd. 264, 502. 

The reason that the caseins, which constitute nearly 80% of bovine milk, are unfolded in their native states appears to be to facilitate digestion, since the open rheomorphic structures allow rapid and extensive degradation to smaller peptides by proteolytic enzymes. The natively unfolded structures of many cereal proteins may serve an analogous purpose since they provide nutrition for seedlings. The physiological function of the synucleins in the brain is as yet unclear, but tau is known to promote and stabilize the assembly of microtubules. 

Ice cream serves as a wonderful (and tasty) example of a complex, dynamically heterogeneous food system. A typical ice cream mix contains milk or cream (water, lactose, casein and whey proteins, lipids, vitamins, and minerals), sucrose, stabilizers and emulsifiers, and some type of flavor (e.g., vanilla). After the ingredients are combined, the mix is pasteurized and homogenized. Homogenization creates an oil-in-water emulsion, consisting of millions of tiny droplets of milk fat dispersed in the water phase, each surrounded by a layer of proteins and emulsifiers. The sucrose is dissolved in... 

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