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Casein (pron.: // or //, from Latin caseus, "cheese") is the name for a family of related phosphoproteins (αS1, αS2, β, κ). These proteins are commonly found in mammalian milk, making up 80% of the proteins in cow milk and between 20% and 45% of the proteins in human milk. Casein has a wide variety of uses, from being a major component of cheese, to use as a food additive, to a binder for safety matches. As a food source, casein supplies amino acids; carbohydrates; and two inorganic elements, calcium and phosphorus.
Casein contains a fairly high number of proline residues, which do not interact. There are also no disulfide bridges. As a result, it has relatively little tertiary structure. 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 only limited resemblance with surfactant-type micellae in a sense that the hydrophilic parts reside at the surface and they are spherical. However, in sharp contrast to surfactant micelles, the interior of a casein micelle is highly hydrated. The caseins in the micelles are held together by calcium ions and hydrophobic interactions. Several models account for the special conformation of casein in the micelles. One of them proposes the micellar nucleus is formed by several submicelles, the periphery consisting of microvellosities of κ-casein. Another model suggests the nucleus is formed by casein-interlinked fibrils. Finally, the most recent model proposes a double link among the caseins for gelling to take place. All three 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. 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.
Human beta-casein is the major protein found in human milk. The protein binds to calcium at its phosphorylated regions, which in turn are highly conserved. The calcium then binds the caseins together and forms micelles, which better enable it to be ingested by infants. It also has opioid type effects on newborn sleeping patterns. The protein, as a whole, is disordered and is characterized as a random coil protein. This structure can be modified to some extent with an increase of temperature.
Casein paint is a fast-drying, water-soluble medium used by artists. Casein paint has been used since ancient Egyptian times as a form of tempera paint, and was widely used by commercial illustrators as the material of choice until the late 1960s when, with the advent of acrylic paint, casein became less popular. It is still widely used by scene painters, although acrylic has made inroads in that field as well.
Casein-based glues were popular for woodworking, including for aircraft, as late as the de Havilland Mosquito. Casein glue is also used in transformer manufacturing (specifically transformer board) due to its oil permeability. While largely replaced by synthetic resins, casein-based glues still have a use in certain niche applications, such as laminating fireproof doors and the labeling of bottles.
Cheese consists of proteins and fat from milk, usually the milk of cows, buffalo, goats, or sheep. It is produced by coagulation of casein. Typically, the milk is acidified and then coagulated by the addition of rennet, containing a proteolytic enzyme, typically obtained from the stomachs of calves. The solids are separated and pressed into final form.
Unlike many proteins, casein is not coagulated by heat. During the process of clotting, milk-clotting proteases act on the soluble portion of the caseins, κ-casein, thus originating an unstable micellar state that results in clot formation. When coagulated with chymosin, casein is sometimes called paracasein. Chymosin (EC 126.96.36.199) 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.
Plastics and fiber 
Some of the earliest plastics were based on casein. In particular, galalith was well known for use in buttons. Fiber can be made from extruded casein. Lanital, a fabric made from casein fiber (known as Aralac in the United States), was particularly popular in Italy during the 1930s. Recent innovations such as QMilch are offering a more refined use of the fiber for modern fabrics.
Protein supplements 
An attractive property of the casein molecule is its ability to form a gel or clot in the stomach, which makes it very efficient in nutrient supply. The clot is able to provide a sustained slow release of amino acids into the blood stream, sometimes lasting for several hours.
Medical and dental uses 
Casein-derived compounds are used in tooth remineralization products to stabilize amorphous calcium phosphate (ACP) and release the ACP onto tooth surfaces, where it can facilitate remineralization.
Although research has shown high rates of use of complementary and alternative therapies for children with autism, including gluten and/or casein exclusion diets, as of 2008[update] there is a lack of evidence for the efficacy of these diets. A 2006 review of seven studies indicated that, although all reported benefits of exclusion diets in reducing autism symptoms, all suffered design flaws, and there was not enough evidence overall to justify recommending exclusion diets to patients.
A1/A2 beta caseins in milk 
According to Food Standards Australia New Zealand (FSANZ), "Milk contains many types of proteins. The proportion of various proteins can be quite different in the milk from different breeds of cows and in the milk from other animals.
Of the six major protein types in cow's milk, four are casein proteins and the other two are whey proteins. The caseins usually make up about 80% of the protein in cow's milk. One of the major caseins is beta -casein. There are different beta casein types, but the most common are beta casein A1 (milk high in this type is known as A1 milk) and beta casein A2 (milk high in this type is known as A2 milk).
Certain breeds of cows, such as Friesians, produce mostly A1 milk, whereas other breeds, such as Guernseys, as well as sheep and goats, produce mostly A2 milk. Milk produced in Australia and New Zealand is normally a mix of A1 and A2 milks."
The European Food Safety Authority carried out a literature review in 2009 concluding "a cause and effect relationship is not established between the dietary intake of BCM7, related peptides or their possible protein precursors and non-communicable diseases" (see A2 milk). Studies supporting these claims have had significant flaws, and the data are inadequate to guide autism treatment recommendations.
"A2 Milk" is a trademark of the A2 Corporation Ltd. of New Zealand.
T. Colin Campbell's The China Study (2005), a book, describes a direct correlation between casein administered to rats and the promotion of cancer cell growth when exposed to carcinogens. Aflatoxin (a potent carcinogen) was administered to these rats over a 2 week dosing period. The rats were given a 1 week post-dosing period before beginning the test (promotion period). During the promotion period, one group of rats was put on a 5% casein protein diet and another group on a 20% casein protein diet. None of the rats on 5% casein protein developed foci, precursors to cancerous cell growth, and every rat on 20% casein protein developed the pre-cancer foci. It should be noted that all test groups were fed a 20% casein diet for a total of 5 weeks (2-wk acclimation, 2-wk dosing, 1-wk post-dosing) prior to the 12 week promotion period in order to survive the initial aflatoxin B1 (AFB1) dosing, regardless of whether they were in the 5% or 20% test groups. Campbell has performed additional studies using a range of different carcinogens and other experimental animals, and claims to have found a consistent correlation between cancer growth and the amount of casein protein in diet. A 2001 study suggests another milk protein, whey protein, may play a protective role against colon tumors in rats. According to a study from the Australian Dairy Council, casein has antimutagenic effects.
Casein-free diet 
Casein has a molecular structure quite similar to that of gluten. Thus, some gluten-free diets are combined with casein-free diets and referred to as a gluten-free, casein-free diet. Casein is often listed as sodium caseinate, calcium caseinate or milk protein. These are often found in energy bars, drinks, and packaged goods. A small fraction of the population is allergic to casein.
Altering the effects of polyphenols 
A study of Charité Hospital in Berlin by Lorenzo et al., published in The European Heart Journal, showed adding milk to tea causes the casein to bind to the molecules in tea that cause the arteries to relax, especially a catechin molecule called EGCG, although a more recent study by Reddy et al. (2005) suggests the addition of milk to tea does not alter the antioxidant activity in vivo, and the cardiovascular effect remains controversial. A study published in the journal Free Radical Biology and Medicine found that consuming 200 mL of whole milk (vs. water control beverage) abolished the 6.1% increase in plasma reducing and chain-breaking antioxidant potential that resulted from consuming 200 g of blueberries, and reduced the peak plasma concentrations of caffeic and ferulic acids, "as well as the overall absorption (AUC) of caffeic acid." The authors did not specifically associate this with the milk's casein content, however. Reviewing previous studies on the impact of milk on absorption of polyphenols, the authors say, "It is a matter of fact that the discrepancy of the results in humans is remarkable, with half the reports suggesting a lack of effect and the other half suggesting an inhibitory effect of milk."
Drug-casein interaction 
Caseinate salts have been shown to reduce the bioavailability of some drugs, including phenytoin. A patient on this drug should consult their doctor about altering their diet so that the efficacy of the drug is not diminished.
See also 
- A2 milk - high in β-casein
- Galalith - a casein-derived plastic
- Milk skin
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Further reading 
- Campbell, T. Colin and Campbell, Thomas M. The China Study. Benbella Books, 2006.
- Green VA, Pituch KA, Itchon J, Choi A, O'Reilly M, Sigafoos J (2006). "Internet survey of treatments used by parents of children with autism". Res Dev Disabil 27 (1): 70–84. doi:10.1016/j.ridd.2004.12.002. PMID 15919178.
- Lucarelli S, Frediani T, Zingoni AM, et al. (September 1995). "Food allergy and infantile autism". Panminerva Med 37 (3): 137–41. PMID 8869369.
- Rao MB, Tanksale AM, Ghatge MS, Deshpande VV (1 September 1998). "Molecular and biotechnological aspects of microbial proteases". Microbiol Mol Biol Rev. 62 (3): 597–635. PMC 98927. PMID 9729602.
- Engel RW, Copeland DH (1 December 1952). "The influence of dietary casein level on tumor induction with 2-acetylaminofluorene". Cancer Res. 12 (12): 905–8. PMID 13009679.
- Manninen, A.H. (2002). Protein metabolism in exercising humans with special reference to protein supplementation. Master thesis. Department of Physiology, Faculty of Medicine, University of Kuopio, Finland.
- Robert H. Demling, Leslie DeSanti (2000). "Effect of a Hypocaloric Diet, Increased Protein Intake and Resistance Training on Lean Mass Gains and Fat Mass Loss in Overweight Police Officers". Annals of Nutrition & Metabolism 44 (44): 21–29. doi:10.1159/000012817.
- Healing Thresholds - summarizes scientific evidence on casein-free diets and other therapies for autism
- Eating without Casein a practical guide to eating and living without casein
- Caseins at the US National Library of Medicine Medical Subject Headings (MeSH)
- Time Magazine, Monday, December 6, 1936 Lanital
- Time Magazine, Monday, August 29, 1938 Wool from Cows