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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 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 does not denature easily. Another effect is that hydrophobic groups end up on the outside of the protein, making it insoluble in water. It is found in milk as a suspension of particles called micellae, which are held together by calcium ions.
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.
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.
Some people with autism and Asperger's syndrome are sensitive to casein and gluten. See more at gluten-free, casein-free diet.
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