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<p><strong>Casein</strong> (from <a title="Latin" href="http://en.wikipedia.org/wiki/Latin">Latin</a> <em>caseus</em> "cheese") is the most predominant <a title="Phosphoprotein" href="http://en.wikipedia.org/wiki/Phosphoprotein">phosphoprotein</a> found in <a title="Milk" href="http://en.wikipedia.org/wiki/Milk">milk</a> and <a title="Cheese" href="http://en.wikipedia.org/wiki/Cheese">cheese</a>. When coagulated with <a title="Rennet" href="http://en.wikipedia.org/wiki/Rennet">rennet</a>, casein is sometimes called <strong>paracasein</strong>. 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 <a title="Salt (chemistry)" href="http://en.wikipedia.org/wiki/Salt_%28chemistry%29">salt</a> of <a title="Calcium" href="http://en.wikipedia.org/wiki/Calcium">calcium</a>. Casein is not coagulated by heat. It is precipitated by <a title="Acid" href="http://en.wikipedia.org/wiki/Acid">acids</a> and by rennet enzymes, a <a title="Proteolytic" href="http://en.wikipedia.org/wiki/Proteolytic">proteolytic</a> <a title="Enzyme" href="http://en.wikipedia.org/wiki/Enzyme">enzyme</a> typically obtained from the stomachs of <a title="Calf" href="http://en.wikipedia.org/wiki/Calf">calves</a>. The enzyme <a title="Trypsin" href="http://en.wikipedia.org/wiki/Trypsin">trypsin</a> can <a title="Hydrolysis" href="http://en.wikipedia.org/wiki/Hydrolysis">hydrolyze</a> off a <a title="Phosphate" href="http://en.wikipedia.org/wiki/Phosphate">phosphate</a>-containing <a title="Peptone" href="http://en.wikipedia.org/wiki/Peptone">peptone</a>.</p><p>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.</p><p>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.</p><script type="text/javascript">//<![CDATA[ if (window.showTocToggle) { var tocShowText = "show"; var tocHideText = "hide"; showTocToggle(); } //]]></script><p> </p><h2><span class="mw-headline">Applications</span></h2><p>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.</p><p> </p><h2><span class="mw-headline">Controversy</span></h2><p><font size="2"></font></p><h3><span class="mw-headline">Opioid</span></h3><p>Casein has been documented to break down to produce the peptide casomorphin, an opioid that appears to act primarily as a histamine releaser.<sup class="reference" id="_ref-0">[1]</sup> Casomorphine is suspected by some sources to aggravate the symptoms of autism<sup class="reference" id="_ref-1">[2]</sup> However, in a recent review it was concluded that insufficient evidence existed to support the use of elimination diets (i.e., casein or gluten free) in the treatment of autism spectrum disorders.<sup class="reference" id="_ref-2">[3]</sup> More importantly preliminary data from the first and only double-blind randomized control trial - reported in the Journal of autism and developmental disorders - of a gluten- and casein-free diet showed no changes in groups on an off the diet.<sup class="reference" id="_ref-3">[4]</sup> At this point it is premature to suggest that casein- or gluten-free diets can help children with autism spectrum disorders.</p><p> </p><h3><span class="mw-headline">Casein-free diet</span></h3><p>Casein has a molecular structure that is extremely similar to that of gluten. Thus, most gluten-free diets are combined with casein-free diets and referred to as a gluten-free, casein-free diet. Casein is also a major trigger of migraines and other types of headaches. In order to prevent headaches it is advised that headache sufferers should eliminate all dairy products from their diet. Casein is often listed as sodium caseinate, calcium caseinate or milk protein. These are often found in sports bars, drinks as well as packaged goods.</p><p> </p><h3><span class="mw-headline">Blocking positive effects of tea</span></h3><p>A study of Charité Hospital in Berlin showed that adding milk to tea will block some of the normal, healthful effects that tea has in protecting against cardiovascular disease (Lorenz 2007). It does this because casein from the milk binds to the molecules in tea that cause the arteries to relax, especially a catechin molecule called EGCG. One of the researchers told New Scientist magazine that "[i]t probably also blocks tea's effect on other things, such as cancer."<sup class="reference" id="_ref-4">[5]</sup> However a similar study by Reddy et. al. (2005) suggests that the addition of milk to tea does not alter the antioxidant activity in vivo.<sup class="reference" id="_ref-5">[6]</sup> and the cardiovascular effect remains controversial.<sup class="reference" id="_ref-6">[7]</sup><sup class="reference" id="_ref-7">[8]</sup></p><p> </p><h2><span class="mw-headline">Notes</span></h2><div class="references-small"><ol class="references"> <li id="_note-0"><strong>^</strong> Kurek et al. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1374738&dopt=Abstract A naturally occurring opioid peptide from cow's milk, beta-casomorphine-7, is a direct histamine releaser in man. ] Retrieved on January 21, 2008. </li> <li id="_note-1"><strong>^</strong> Casein-Free Diet and Children with Autism. Retrieved on January 21, 2008. </li> <li id="_note-2"><strong>^</strong> Christison, GW. Elimination diets in autism spectrum disorders: any wheat amidst the chaff?. Retrieved on January 21, 2008. </li> <li id="_note-3"><strong>^</strong> The gluten-free, casein-free diet in autism: results of a preliminary double blind clinical trial. Retrieved on January 21, 2008. </li> <li id="_note-4"><strong>^</strong> Milk wrecks the health benefits of tea. Retrieved on January 21, 2008. </li> <li id="_note-5"><strong>^</strong> [1] </li> <li id="_note-6"><strong>^</strong> Prabhakar, Vijay R. Milk casein and its benefits on cardiovascular risk. Retrieved on January 21, 2008. </li> <li id="_note-7"><strong>^</strong> Lorenz, Mario. Milk casein and its benefits on cardiovascular risk: reply. Retrieved on January 21, 2008. </li></ol></div><p> </p><h2><span class="mw-headline">Sources</span></h2><ul> <li>Green, V., et al. 2006. "Internet Survey of Treatments Used by Parents of Children with Autism." Research in Developmental Disabilities. 27 (1):70-84 </li> <li>Lucarelli, S., et al. 1995. "Food allergy and infantile autism." Panminerva Med. 37(3):137-141. </li> <li>Lorenz, M., et al. 2007. "Addition of milk prevents vascular protective effects of tea." European Heart Journal (DOI: 10.1093/eurheartj/ehl442) (PMID: 17213230) </li></ul><p> </p><h2><span class="mw-headline">See also</span></h2><ul> <li>A2 milk - High in β-casein </li> <li>Casomorphin </li> <li>Cheese </li> <li>Dairy </li></ul><p> </p><h2><span class="mw-headline">External links</span></h2><ul> <li><a class="external text" title="http://autism.HealingThresholds.com/" href="http://autism.healingthresholds.com/" rel="nofollow">Healing Thresholds</a> summarizes scientific evidence on casein-free diets and other therapies for autism </li> <li><a class="external text" title="http://www.gfcfdiet.com/" href="http://www.gfcfdiet.com/" rel="nofollow">GFCF Diet Support Group</a> </li> <li><a class="external text" title="http://www.foodalergy.org/" href="http://www.foodalergy.org/" rel="nofollow">Food Allergy and Anaphylaxis Network</a> </li> <li><a class="external text" title="http://www.metabolism.com/healthbytes/2001-07-25/" href="http://www.metabolism.com/healthbytes/2001-07-25/" rel="nofollow">Casein causing headaches</a> </li> <li><a title="Medical Subject Headings" href="http://en.wikipedia.org/wiki/Medical_Subject_Headings">MeSH</a> <em><a class="external text" title="http://www.nlm.nih.gov/cgi/mesh/2007/MB_cgi?mode=&term=Caseins" href="http://www.nlm.nih.gov/cgi/mesh/2007/MB_cgi?mode=&term=Caseins" rel="nofollow">Caseins</a></em> </li></ul><!--NewPP limit reportPreprocessor node count: 207/1000000Post-expand include size: 1449/2048000 bytesTemplate argument size: 519/2048000 bytes#ifexist count: 0/500--><!-- Saved in parser cache with key enwiki:pcache:idhash:88935-0!1!0!default!!en!2 and timestamp 20080127203852 --><div class="printfooter"></div><br />1. 카세인<br />2. -우유속에 들어 있는 흰색의 가루 단백<br /> -모든 필수 아미노산이 들어있어 완전단백으로 여긴다.
