Casein

See Casein paint for information about casein usage in artistic painting.

Casein is the predominant phosphoprotein found in fresh milk. When coagulated with rennet, casein is sometimes called paracasein. 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, 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 disulphide 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.

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.

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 dispersable in dilute alkalis and in salt solutions such as sodium oxalate and sodium acetate.

In a comprehensive 1989 nutrition study in China, known as [The China Project,] casein was found to have a direct correlation with tumor growth; it was suggested that casein may be a tumor promoter, though this is controversial. [link]

Casein

See also