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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>
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<h2><span class="mw-headline">Applications</span></h2>
<h2><span class="mw-headline">External links</span></h2>
<ul>
<li><a class="external text" title="http://autism.HealingThresholds.com/" rel="nofollow" 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/" rel="nofollow" href="http://www.gfcfdiet.com/" rel="nofollow">GFCF Diet Support Group</a> </li> <li><a class="external text" title="http://www.foodalergy.org/" rel="nofollow" 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/" rel="nofollow" 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" rel="nofollow" href="http://www.nlm.nih.gov/cgi/mesh/2007/MB_cgi?mode=&term=Caseins" rel="nofollow">Caseins</a></em> </li>
</ul>
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