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Sandbox WWCAlpha-S1-Casein

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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. In addition to providing nutritive protein to mammalian neonates, these micelles supply calcium and inorganic phosphate at levels much higher than would be expected if were simply dissolved in the milk.<ref>McSweeney, P. (2009). Nutritional Aspects of Milk Proteins. In Advanced dairy chemistry (3rd ed., Vol. 1). New York: Springer-Verlag.</ref>
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. In addition to providing nutritive protein to mammalian neonates, these micelles supply calcium and inorganic phosphate at levels much higher than would be expected if were simply dissolved in the milk.<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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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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Unlike whey proteins (all non-casein 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>
<ref>Masoodi, T. A., & Shafi, G. (2010). Analysis of casein alpha S1 & S2 proteins from different mammalian species. Bioinformation, 4(9), 430–435.</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>

Revision as of 02:14, 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. In addition to providing nutritive protein to mammalian neonates, these micelles supply calcium and inorganic phosphate at levels much higher than would be expected if were simply dissolved in the milk.[4]

Unlike whey proteins (all non-casein 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.[5]

[6]

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. ↑ McSweeney, P. (2009). Nutritional Aspects of Milk Proteins. In Advanced dairy chemistry (3rd ed., Vol. 1). New York: Springer-Verlag.
  5. ↑ Fennema, O. (1996). Characteristics of Milk. In Food chemistry (3rd ed., p. 865). New York: Marcel Dekker.
  6. ↑ 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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