Casein (from Latin caseus "cheese") is the predominant phosphoprotein (αS1, αS2, β, κ) that accounts for nearly 80% of proteins in 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 rennet, casein is sometimes called paracasein. Chymosin (EC 220.127.116.11) is an aspartic protease that specifically hydrolyzes the peptide bond in Phe105-Met106 of κ-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 secondary structure or 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 κ-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 κ-casein molecules.
The isoelectric point of casein is 4.6. 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.
In addition to being consumed in milk, casein is used in the manufacture of adhesives, binders, protective coatings, plastics (such as for knife handles and knitting needles), fabrics, food additives and many other products. It is commonly used by bodybuilders as a slow-digesting source of amino acids as opposed to the fast-digesting whey protein, and also as an extremely high source of glutamine (post-workout). Another reason it is used in bodybuilding is because of its anti-catabolic effect, meaning that casein consumption inhibits protein breakdown in the body. Casein is frequently found in otherwise nondairy cheese substitutes to improve consistency, especially when melted. An enzymatic hydrolysate of casein to its individual amino acids, called "NZ-Amine" is commonly used as a constituent of agar plates in molecular biology or to supplement the protein content of foods. Purified casein is also frequently used as a blocking agent in Western blotting and ELISA protocols.
Substitution of Casein by [beta]-Casein or of Whey Protein Isolate by [alpha]-Lactalbumin Does Not Affect Mineral Balance in Growing Rats1
Jun 01, 2005; ABSTRACT Bovine milk protein fractions that enable modification of the protein composition and amino acid profile of infant...