ingredient information
Calcium Sodium Caseinate
Casein (from Latin caseus "cheese") is the predominant phosphoprotein (aS1, aS2, ß, ?) that accounts for nearly 80% of proteins in cow milk and cheese. Milk-clotting proteases act on the soluble portion of the caseins, K-Casein, thus originating an unstable micellar state that results in clot formation. When coagulated with rennin, casein is sometimes called paracasein. Chymosin (EC is an aspartic protease that specifically hydrolyzes the peptide bond in Phe105-Met106 of ?-casein and is considered to be the most efficient protease for the cheese-making industry (Rao et al., 1998). British terminology, on the other hand, uses the term caseinogen for the uncoagulated protein and casein for the coagulated protein. As it exists in milk, it is a salt of calcium. Casein is not coagulated by heat. It is precipitated by acids and by rennet enzymes, a proteolytic enzyme typically obtained from the stomachs of calves. The enzyme trypsin can hydrolyze off a phosphate-containing peptone. Casein consists of a fairly high number of proline peptides, which do not interact. There are also no disulfide bridges. As a result, it has relatively little tertiary structure. Because of this, it cannot denature. It is relatively hydrophobic, making it poorly soluble in water. It is found in milk as a suspension of particles called casein micelles which show some resemblance with surfactant-type micellae in a sense that the hydrophilic parts reside at the surface. The caseins in the micelles are held together by calcium ions and hydrophobic interactions. There are several models that account for the special conformation of casein in the micelles (Dalgleish, 1998). One of them proposes that the micellar nucleus is formed by several submicelles, the periphery consisting of microvellosities of ?-casein (Walstra, 1979; Lucey, 2002). Another model suggests that the nucleus is formed by casein-interlinked fibrils (Holt, 1992). Finally, the most recent model (Horne, 1998) proposes a double link among the caseins for gelling to take place. All 3 models consider micelles as colloidal particles formed by casein aggregates wrapped up in soluble ?-casein molecules. The isoelectric point of casein is 4.6. Since milk's pH is 6.6, casein has a negative charge in milk. The purified protein is water insoluble. While it is also insoluble in neutral salt solutions, it is readily dispersible in dilute alkalis and in salt solutions such as sodium oxalate and sodium acetate. Casein has been reported to reduce tooth decay