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Sandbox WWCAlpha-S1-Casein

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'''Alpha-S1-Casein (αs1-CN)''' is a calcium phosphate (CaP) binding protein found in bovine milk along with other caseins, including αs2- and β-casein (calcium-sensitive), and κ-casein (calcium insensitive).<ref>J. Dairy Sci., 67, 1599-1631, 1984, and from Table 1, J. Dairy Sci., 68, 2195-2205, 1985</ref> Although αs1-CN is the predominant casein (and protein overall) in bovine milk, the ratios of caseins vary considerably by species.<ref>doi: 10.1093/molbev/msr020</ref>
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'''Casein''' consists of a group of proteins found in all mammal milks, including αs1-, αs2-, and β-casein (calcium-sensitive caseins), κ-casein (calcium insensitive).<ref>J. Dairy Sci., 67, 1599-1631, 1984, and from Table 1, J. Dairy Sci., 68, 2195-2205, 1985</ref> Although αs1-CN is the predominant casein in bovine milk, the ratios of caseins vary considerably by species, and in human milk β-casein is predominant.<ref>doi: 10.1093/molbev/msr020</ref><ref>McSweeney, P. (2009). Nutritional Aspects of Milk Proteins. In Advanced dairy chemistry (3rd ed., Vol. 1). New York: Springer-Verlag.</ref>
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Calcium-sensitive caseins such as αs1-CN bind with CaP, but will precipitate at high concentrations of CaP. In milk, huge complexes are formed by calcium-sensitive caseins, CaP, and calcium-insensitive caseins. Precipitation of the calcium-sensitive caseins is prevented by the calcium-insensitive caseins stabilizing the complex to form a micelle. These micelles function to deliver calcium, phosphate, and protein to mammalian neonates. Unlike the whey proteins (all non-casein protein found in milk), caseins in micelles are relatively heat stable, although denaturation of the whey protein β-lactoglobulin at high temperatures can result in interactions with micelle κ-casein that alters the structure of the micelle surface <ref>Fennema, O. (1996). Characteristics of Milk. In Food chemistry (3rd ed., p. 865). New York: Marcel Dekker.</ref> <ref>Masoodi, T. A., & Shafi, G. (2010). Analysis of casein alpha S1 & S2 proteins from different mammalian species. Bioinformation, 4(9), 430–435.</ref>
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Calcium-sensitive caseins such as αs1-CN bind calcium phosphate (CaP), and high concentrations of CaP will cause these caseins to precipitate. In milk, huge complexes are formed from CaP, calcium-sensitive caseins, and calcium-insensitive caseins. Precipitation of the calcium-sensitive caseins in these complexes is prevented by calcium-insensitive caseins stabilizing the complex to form a micelle. These casein micelles function to deliver calcium, phosphate, and protein to mammalian neonates. Unlike whey proteins (all other proteins present in milk), casein micelles are relatively heat stable, although denaturation of the whey protein β-lactoglobulin at high temperatures can result in interactions with micelle κ-casein that alters the structure of the micelle surface.<ref>Fennema, O. (1996). Characteristics of Milk. In Food chemistry (3rd ed., p. 865). New York: Marcel Dekker.</ref>
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<ref>Masoodi, T. A., & Shafi, G. (2010). Analysis of casein alpha S1 & S2 proteins from different mammalian species. Bioinformation, 4(9), 430–435.</ref>
== Function ==
== Function ==

Revision as of 01:46, 10 April 2015

Casein consists of a group of proteins found in all mammal milks, including αs1-, αs2-, and β-casein (calcium-sensitive caseins), κ-casein (calcium insensitive).[1] Although αs1-CN is the predominant casein in bovine milk, the ratios of caseins vary considerably by species, and in human milk β-casein is predominant.[2][3]

Calcium-sensitive caseins such as αs1-CN bind calcium phosphate (CaP), and high concentrations of CaP will cause these caseins to precipitate. In milk, huge complexes are formed from CaP, calcium-sensitive caseins, and calcium-insensitive caseins. Precipitation of the calcium-sensitive caseins in these complexes is prevented by calcium-insensitive caseins stabilizing the complex to form a micelle. These casein micelles function to deliver calcium, phosphate, and protein to mammalian neonates. Unlike whey proteins (all other proteins present in milk), casein micelles are relatively heat stable, although denaturation of the whey protein β-lactoglobulin at high temperatures can result in interactions with micelle κ-casein that alters the structure of the micelle surface.[4]

[5]

Contents

Function

Disease

Relevance

Structural highlights

References

  1. ↑ J. Dairy Sci., 67, 1599-1631, 1984, and from Table 1, J. Dairy Sci., 68, 2195-2205, 1985
  2. ↑ Kawasaki K, Lafont AG, Sire JY. The evolution of milk casein genes from tooth genes before the origin of mammals. Mol Biol Evol. 2011 Jul;28(7):2053-61. doi: 10.1093/molbev/msr020. Epub 2011 Jan , 18. PMID:21245413 doi:http://dx.doi.org/10.1093/molbev/msr020
  3. ↑ McSweeney, P. (2009). Nutritional Aspects of Milk Proteins. In Advanced dairy chemistry (3rd ed., Vol. 1). New York: Springer-Verlag.
  4. ↑ Fennema, O. (1996). Characteristics of Milk. In Food chemistry (3rd ed., p. 865). New York: Marcel Dekker.
  5. ↑ Masoodi, T. A., & Shafi, G. (2010). Analysis of casein alpha S1 & S2 proteins from different mammalian species. Bioinformation, 4(9), 430–435.
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