Advertisement

Molecular Biology Reports

, Volume 41, Issue 2, pp 1035–1048 | Cite as

Major proteins in goat milk: an updated overview on genetic variability

  • Maria Selvaggi
  • Vito Laudadio
  • Cataldo Dario
  • Vincenzo Tufarelli
Article

Abstract

Milk and dairy products are very important in Mediterranean diet because of their health promoting and organoleptic properties. In many developing countries, goat rearing has a key role in livestock production. What makes goats so popular is their ability to provide high quality food under diverse climatic conditions and resilience to extreme and capricious environments. In the last years, the interest concerning caprine milk has been increasing also to find a new exploitation for local breeds. To promote the goat dairy products there is a clear need to know the quality and the technological aspects of milk produced. That being so, the purpose of this study was to review the available literature on the major goat milk proteins with a particular attention to recent findings on their genetic variability. Moreover, the main effects of different protein variants on milk yield and composition were also discussed.

Keywords

Milk Casein Whey protein Dairy goats Polymorphism Genetic variants 

References

  1. 1.
    Haenlein GFW (2007) About the evolution of goat and sheep milk production. Small Rumin Res 68:3–6CrossRefGoogle Scholar
  2. 2.
    Silanikove N (2000) The physiological basis of adaptation in goats to harsh environments. Small Rumin Res 35:181–193CrossRefGoogle Scholar
  3. 3.
    Park YW, Juàrez M, Ramos M, Haenlein GFW (2007) Physicochemical characteristics of goat and sheep milk. Small Rumin Res 68:88–113CrossRefGoogle Scholar
  4. 4.
    Prosser CG, McLaren RD, Frost D, Agnew M, Lowry DJ (2008) Composition of the non-protein nitrogen fraction of goat whole milk powder and goat milk-based infant and follow-on formulae. Int J Food Sci Nutr 59:123–133PubMedCrossRefGoogle Scholar
  5. 5.
    Linderstrom-Lang K, Kodama SCR (1925) Studies on casein. I. On the solubility of caseins in hydrochloric acid. Comptes-Rendus des Travaux du Laboratoire Carlsberg 16:1–47Google Scholar
  6. 6.
    Mellander O (1939) Elektophoretische untersuchung von casein. Biochem Z 300:240Google Scholar
  7. 7.
    Wake RG, Baldwin RL (1961) Analysis of casein fractions by zone electrophoresis in concentrated urea. Biochim Biophys Acta 47:225–239PubMedCrossRefGoogle Scholar
  8. 8.
    Ng-Kwai Hang KF, Grosclaude F (1992) Genetic polymorphisms of milk proteins. In: Fox PF (ed) Advanced dairy chemistry. Elsevier, London, pp 405–455Google Scholar
  9. 9.
    Stewart AF, Bonsing J, Beattie CW, Shah F, Willis IM, Mackinlay AG (1987) Complete nucleotide sequences of bovine αs2- and β-casein cDNAs: comparisons with related sequences in other species. Mol Biol Evol 4:231–241PubMedGoogle Scholar
  10. 10.
    Rijnkels M (2002) Multispecies comparison of the casein gene loci and evolution of casein gene family. J Mammary Gland Biol 7:327–345CrossRefGoogle Scholar
  11. 11.
    Barth CA, Behnke U (1997) Nutritional significance of whey and whey components. Nahrung 41:2–12PubMedCrossRefGoogle Scholar
  12. 12.
    Farrell HM Jr, Jimenez-Flores R, Bleck GT, Brown EM, Butler JE, Creamer LK, Hicks CL, Hollar CM, Ng-Kwai-Hang KF, Swaisgood HE (2004) Nomenclature of the proteins of cows’ milk–sixth revision. J Dairy Sci 87:1641–1674PubMedCrossRefGoogle Scholar
  13. 13.
    Morr CV (1989) Whey proteins: manufacture. In: Fox PF (ed) Developments in dairy chemistry–4. Proteins. Elsevier, London, pp 245–248Google Scholar
  14. 14.
    Foldager J, Huber JT, Bergen WG (1977) Methionine and sulfur amino acid requirement in the preruminant calf. J Dairy Sci 60:1095–1104PubMedCrossRefGoogle Scholar
  15. 15.
    Oftedal OT (2012) The evolution of milk secretion and its ancient origins. Animal 6:355–368PubMedCrossRefGoogle Scholar
  16. 16.
    Evans EW (1982) Use of milk proteins in formulated foods. In: Hudson BJF (ed) Developments in food proteins. Applied Science, LondonGoogle Scholar
  17. 17.
    Hambraeus L (1982) Nutritional aspects of milk proteins. In: Fox PF (ed) Developments in dairy chemistry–1: proteins. Applied Science, London, pp 289–313Google Scholar
  18. 18.
    Sindayikengera S, Xia WS (2006) Nutritional evaluation of caseins and whey proteins and their hydrolysates from Protamex. J Zhejiang Univ Sci B 7:90–98PubMedPubMedCentralCrossRefGoogle Scholar
  19. 19.
    Stănciuc N (2009) Milk proteins. The structure-function relationship. Academica, GalaţiGoogle Scholar
  20. 20.
    Walstra P (1990) On the stability of casein micelles. J Dairy Sci 73:1965–1979CrossRefGoogle Scholar
  21. 21.
    Masoodi TA, Shafi G (2010) Analysis of casein alpha S1 & S2 proteins from different mammalian species. Bioinformation 4:430–435PubMedPubMedCentralCrossRefGoogle Scholar
  22. 22.
    Mercier JC (1981) Phosphorylation of caseins, present evidence for an amino acid triplet code post-translationally recognized by specific kinases. Biochimie 63:1–17PubMedCrossRefGoogle Scholar
  23. 23.
    Boisnard M, Pètrissant G (1985) Complete sequence of ovine alpha s2-casein messenger RNA. Biochimie 67:1043–1051PubMedCrossRefGoogle Scholar
  24. 24.
    Bouniol C (1992) Sequence of the goat as2-encoding cDNA. Gene 125:235–236CrossRefGoogle Scholar
  25. 25.
    Tziboula A, Horne DS (1999) The role of αS1-casein in the structure of caprine casein micelles. Int Dairy J 9:173–178CrossRefGoogle Scholar
  26. 26.
    Martìn P, Brignon G, Furet JP, Leroux C (1996) The gene encoding αs1-casein is expressed in human mammary epithelial cells during lactation. Le Lait 76:526–537CrossRefGoogle Scholar
  27. 27.
    Rasmussen L, Hojrup P, Petersen TE (1992) Localization of two interchain disulfide bridges in otator of bovine αS2-casein. Parallel and antiparallel alignments of the polypeptide chains. Eur J Biochem 203:381–386PubMedCrossRefGoogle Scholar
  28. 28.
    Brignon G, Ribadeau-Dumas B, Mercier JC, Pélissier JP, Das BC (1977) Complete amino acid sequence of bovine alpha S2-casein. FEBS Lett 76:274–279PubMedCrossRefGoogle Scholar
  29. 29.
    Groenen MAM, Dijkhof RJM, Verstege AJM, van der Poel JJ (1993) The complete sequence of the gene encoding bovine alpha s2-casein. Gene 123:187–193PubMedCrossRefGoogle Scholar
  30. 30.
    Grosclaude F, Mahé MF, Mercier JC, Bonnemaire J, Theissier JH (1976) Polymorphisme des lactoprotéines de Bovinés Népalais. II. Polymorphisme des caséines “αS-mineures”: le locus αS2-CN est-il lié aux loci αS1-CN, β-CN et κ-CN. Ann Genet Sel Anim 8:481–491PubMedPubMedCentralGoogle Scholar
  31. 31.
    Grosclaude F, Joudrier P, Mahé MF (1978) Polymorphism de la caséine αS2 bovine: etroite liason du locus αS2-CN avec les loci αS1-CN, β-CN et κ-CN; mise en evidence d’une deletion dans le variant αS2-CND. Ann Genet Sel Anim 10:313–327PubMedPubMedCentralGoogle Scholar
  32. 32.
    Grosclaude F, Mahé MF, Accolas JP (1982) Note sur le polymorphisme génétique des lactoprotéines de bovines et de yaks Mongols. Ann Genet Sel Anim 14:545–550PubMedPubMedCentralGoogle Scholar
  33. 33.
    Grosclaude F, Joudrier P, Mahé MF (1979) A genetic and biochemical analysis of a polymorphism of bovine αS2-casein. J Dairy Res 46:211–213PubMedCrossRefGoogle Scholar
  34. 34.
    Erhardt G (1993) Allele frequencies of milk proteins in German cattle breeds and demonstration of αS2-casein variants by isoelectric focusing. Arch Tierzucht 36:145–152Google Scholar
  35. 35.
    Jann OC, Ibeagha-Awemu EM, Zbeyaz EO, Zaragoza P, Williams JL, Ajmone-Marsan P, Lenstra JA, Moazami-Goudarzi K, Erhardt G (2004) Geographic distribution of haplotype diversity at the bovine casein locus. Genet Sel Evol 36:243–257PubMedPubMedCentralCrossRefGoogle Scholar
  36. 36.
    Ibeagha-Awemu EM, Prinzenberg EM, Erhardt G (2005) High variability of milk protein genes in Bos indicus cattle breeds of Cameroon and Nigeria and characterization of a new αS1 promoter allele. J Dairy Res 72:1–9PubMedCrossRefGoogle Scholar
  37. 37.
    Jenness R (1980) Composition and characteristics of goat milk: review 1968–1979. J Dairy Sci 63:1605–1630CrossRefGoogle Scholar
  38. 38.
    Brignon G, Mahé MF, Grosclaude F, Ribadeau-Dumas B (1989) Sequence of caprine αs1 casein and characterization of those of its genetic variants which are synthesized at a high level, αs1-CN A B and C. Protein Seq Data Anal 2:181–188PubMedGoogle Scholar
  39. 39.
    Brignon G, Mahé MF, Ribadeau-Dumas B, Mercier JC, Grosclaude F (1990) Two of the three genetic variants of goat alpha s1-casein which are synthesized at a reduced level have an internal deletion possibly due to altered RNA splicing. Eur J Biochem 193:237–241PubMedCrossRefGoogle Scholar
  40. 40.
    Mora-Gutierrez A, Kumosinski TF, Farrell HM (1991) Quantification of αs1-casein in goat milk from French-Alpine and Anglo-Nubian breeds using reversed-phase high performance liquid chromatography. J Dairy Sci 74:3303–3307PubMedCrossRefGoogle Scholar
  41. 41.
    Grosclaude F, Mahé MF, Brignon G, Di Stasio L, Jeunet RA (1987) Mendelian polymorphism underlying quantitative variations of goat αs1-casein. Genet Sel Evol 19:399–412PubMedPubMedCentralCrossRefGoogle Scholar
  42. 42.
    Addeo F, Masi P, Rubino R (1987) The aptitude of caprine milk to cheesemaking. Relationship between αs1-casein content and rheological properties of curd and cheese. In: L’evaluation des ovis et des caprins mediterraneens, Symposium Philoetios, Fonte-Boa, PortugalGoogle Scholar
  43. 43.
    Moioli B, Pilla F, Tripaldi C (1998) Detection of milk protein genetic polymorphisms in order to improve dairy traits in sheep and goats: a review. Small Rumin Res 27:185–195CrossRefGoogle Scholar
  44. 44.
    Rando A, Ramunno L, Masina P (2000) Mutations in casein genes. Zoot Nutr Anim 26:105–114Google Scholar
  45. 45.
    Bevilacqua C, Ferranti P, Garro G, Veltri C, Lagonigro R, Leroux C, Pietrola E, Addeo F, Pilla F, Chianese L, Martìn P (2002) Interallelic recombination is likely responsible for the occurrence of a new rate (αs1-casein variant in the goat species). Eur J Biochem 269:1293–1303PubMedCrossRefGoogle Scholar
  46. 46.
    Ramunno L, Cosenza G, Rando A, Pauciullo A, Illario R, Gallo D, Di Berardino D, Masina P (2005) Comparative analysis of gene sequence of goat CSN1S1 F and N alleles and characterization of CSN1S1 transcript variants in mammary gland. Gene 345:289–299PubMedCrossRefGoogle Scholar
  47. 47.
    Sacchi P, Chessa S, Budelli E, Bolla P, Ceriotti G, Soglia D, Rasero R, Cauvin E, Caroli A (2005) Casein haplotype structure in five Italian goat breeds. J Dairy Sci 88:1561–1568PubMedCrossRefGoogle Scholar
  48. 48.
    Sztankóová Z, Mátlová V, Malá G (2007) Genetic polymorphism at the CSN1S1 gene in two Czech goat breeds. Czech J Anim Sci 52:199–202Google Scholar
  49. 49.
    Chianese L, Garro G, Mauriello R, Laezza P, Ferranti P, Addeo F (1997) Occurrence of three novel αs1 casein in goat’s milk. In: International Dairy Federation (ed) Milk protein Polymorphism, Special Issue, 9702Google Scholar
  50. 50.
    Grosclaude F, Martìn P (1997) Casein polymorphism in the goat. In: International Dairy Federation (ed), Milk protein polymorphism, special issue, 9702. Int Dairy Federation, Brussels, BelgiumGoogle Scholar
  51. 51.
    Storry JE, Grandison AS, Milliard D, Owen AJ, Ford GD (1983) Chemical composition and coagulating properties of renneted milks from different breeds and species of ruminant. J Dairy Res 50:215–229CrossRefGoogle Scholar
  52. 52.
    Remeuf F, Lenoir J (1986) Relationship between the physicochemical characteristics of goat’s milk and its rennetability. B Int Dairy Federation 202:68Google Scholar
  53. 53.
    Ambrosoli R, Di Stasio L, Mazzocco P (1988) Content of alphas1-casein and coagulation properties in goat milk. J Dairy Sci 71:24–28PubMedCrossRefGoogle Scholar
  54. 54.
    Risch E (1992) Rheological properties of goat milk cheese: methods of true axial stress versus apparent axial stress. J Texture Stud 23:403–413CrossRefGoogle Scholar
  55. 55.
    Clark S, Sherbon JW (2000) Genetic variants of alphas1-CN in goat milk: breed distribution and associations with milk composition and coagulation properties. Small Rumin Res 38:135–143CrossRefGoogle Scholar
  56. 56.
    Leroux C, Martìn P, Mahé M-F, Levèziel H, Mercier JC (1990) Restriction fragment length polymorphism identification of goat αS1-casein alleles. A potential tool in selection of individuals carrying alleles associated with a high level protein synthesis. Anim Genet 21:341–351PubMedCrossRefGoogle Scholar
  57. 57.
    Roncada P, Gaviraghi A, Liberatori S, Canas B, Bini L, Greppi GF (2002) Identification of caseins in goat milk. Proteomics 2:723–726PubMedCrossRefGoogle Scholar
  58. 58.
    Ahmed S (2006) Identification of Egyptian goat α S1-casein alleles using PCR-RFLP method. Int J Dairy Sci 1:27–31CrossRefGoogle Scholar
  59. 59.
    Grosclaude F (1988) Le polymorphisme genetique des principales 1actoproteines bovines. Relations avec la quantite’, la composition et les aptitudes fromageres du lait. Prod Anim 1:5–17Google Scholar
  60. 60.
    Remeuf F, Verdalet-Guzman I, Lenoir J (1995) Technological adjustment of goat milk containing low synthesis rate αS1-casein variants. Int Dairy J 5:381–392CrossRefGoogle Scholar
  61. 61.
    Mora-Gutierrez A, Kumosinski TF, Farrell HM Jr (1997) Oxygen-17 nuclear magnetic resonance studies of bovine and caprine casein hydration and activity in deuterated sugar solutions. J Agr Food Chem 45:4545–4553CrossRefGoogle Scholar
  62. 62.
    Boulanger A, Grosclaude F, Mahé MF (1984) Polymorphisme des caséines αs1 et αs2 de la chèvre (Capra hircus). Genet Sel Evol 16:157–176PubMedPubMedCentralGoogle Scholar
  63. 63.
    Bouniol C, Brignon G, Mahé MF, Printz C (1994) Biochemical and genetic analysis of variant C of caprine αs2-casein (Capra hircus). Anim Genet 25:173–177PubMedCrossRefGoogle Scholar
  64. 64.
    Martìn P, Addeo F (1995) Genetic polymorphisms of casein in the milk of goats and sheep. IDF/FIL Publ 9603:45–58Google Scholar
  65. 65.
    Lagonigro R, Pietrosa E, D’Andrea M, Veltri C, Pilla F (2001) Molecular genetic characterization of the goat αs2-casein E allele. Anim Genet 32:391–393PubMedCrossRefGoogle Scholar
  66. 66.
    Ramunno L, Cosenza G, Pappalardo M, Longobardi E, Gallo D, Pastore N, Di Gregorio P, Rando A (2001) Characterization of two new alleles at the goat CSN1S2 locus. Anim Genet 32:264–268PubMedCrossRefGoogle Scholar
  67. 67.
    Erhardt G, Jaeger S, Budelli E, Caroli A (2002) Genetic polymorphism of goat αs2-casein and evidence for a further allele. Milchwissenschaft 57:137–140Google Scholar
  68. 68.
    Ramunno L, Longobardi E, Pappalardo M, Rando A, Di Gregorio P, Cosenza G, Mariani P, Pastore N, Masina P (2001) An allele associated with a non detectable amount of αs2 casein in goat milk. Anim Genet 32:19–26PubMedCrossRefGoogle Scholar
  69. 69.
    Marletta D, Bordonaro S, Guastella AM, Falagiani P, Crimi N, D’Urso G (2004) Goat milk with different αs2-casein content: analysis of allergenic potency by REAST inhibition assay. Small Rumin Res 52:19–24CrossRefGoogle Scholar
  70. 70.
    Ferranti P, Lilla S, Chianese L, Addeo F (2000) Qualitative and quantitative variation of deleted protein forms in goat αs1 and αs2 casein phenotypes. In: Proceedings 7th International Conference on GoatsGoogle Scholar
  71. 71.
    Cunsolo V, Muccilli V, Saletti R, Marletta D, Foti S (2006) Detection and characterization by high-performance liquid chromatography and mass spectrometry of two truncated goat αs2-caseins. Rap Commun Mass Sp 20:1061–1070CrossRefGoogle Scholar
  72. 72.
    Pearse MJ, Linklater PM, Hall RJ, Mackinlay AG (1986) The effect of casein composition and casein dephosphorylation on the coagulation and syneresis of artificial micelle milk. J Dairy Res 53:381–390CrossRefGoogle Scholar
  73. 73.
    Greenberg R, Groves ML, Dower HJ (1984) Human β-casein. Amino acid sequence and identification of phosphorylation sites. J Biol Chem 259:5132–5138PubMedGoogle Scholar
  74. 74.
    Bonsing J, Ring JM, Stewart AF, Mackinlay AG (1988) Complete nucleotide sequence of the bovine β-casein gene. Australian J Biol Sci 41:527–537Google Scholar
  75. 75.
    Provot C, Persuy MA, Mercier JC (1989) Complete nucleotide sequence of ovine beta-casein cDNA: inter-species comparison. Biochimie 71:827–832PubMedCrossRefGoogle Scholar
  76. 76.
    Alexander LJ, Beattie CW (1992) The sequence of porcine β-casein cDNA. Anim Genet 23:369–371PubMedCrossRefGoogle Scholar
  77. 77.
    Collet C, Joseph R, Nicholas K (1992) Molecular characterization and in vitro hormonal requirements for expression of two casein genes from a marsupial. J Mol Endocrinol 8:13–20PubMedCrossRefGoogle Scholar
  78. 78.
    Ginger MR, Grigor MR (1999) Comparative aspects of milk caseins. Comp Biochem Phys B 124:133–145CrossRefGoogle Scholar
  79. 79.
    Lien S, Kantanen J, Olsaker I, Holm L-E, Eythorsdottir E, Sandberg K, Dalsgard B, Adalsteinsson S (1999) Comparison of milk protein allele frequencies in Nordic cattle breeds. Anim Genet 30:85–91PubMedCrossRefGoogle Scholar
  80. 80.
    Jensen HB, Holland JW, Poulsen NA, Larsen LB (2012) Milk protein variants and isoforms identified in bovine milk representing extremes in coagulation properties. J Dairy Sci 95:2891–2903PubMedCrossRefGoogle Scholar
  81. 81.
    Chianese L, Garro G, Nicola MA, Mauriello R, Ferranti P, Pizzano R, Cappuccio U, Laezza P, Addeo F, Ramunno L, Rando A, Rubino R (1993) The nature of β-casein heterogeneity in caprine. Le Lait 73:533–547CrossRefGoogle Scholar
  82. 82.
    Richardson BC, Creamer LK (1974) Comparative micelle structure III. The isolation and chemical characterization of caprine β1-casein and β2-casein. Biochim Biophy Acta 365:133–137CrossRefGoogle Scholar
  83. 83.
    Dall’Olio S, Davoli R, Russo V (1989) Una nuova variante di β caseina caprina. Sci Tecnol Latt-Casearia 40:24–28Google Scholar
  84. 84.
    Mahé MF, Grosclaude F (1993) Polymorphism of β-casein in the Creole goat of Guadeloupe, evidence for a null allele. Genet Sel Evol 25:403–408PubMedCentralCrossRefGoogle Scholar
  85. 85.
    Neveu C, Mollé D, Moreno J, Martìn P, Léonid J (2002) Heterogeneity of caprine beta-casein elucidated by RP-HPLC/MS: genetic variants and phosphorylation. J Protein Chem 21:557–567PubMedCrossRefGoogle Scholar
  86. 86.
    Chessa S, Budelli E, Chiatti F, Cito AM, Bolla P, Caroli A (2005) Predominance of β-casein (CSN2) C allele in goat breeds reared in Italy. J Dairy Sci 88:1878–1881PubMedCrossRefGoogle Scholar
  87. 87.
    Ramunno L, Mariani P, Pappalardo M, Rando A, Capuano M, Di Gregorio P, Cosenza G (1995) Un gene ad effetto maggiore sul contenuto di caseina β nel latte di capra. XI Convegno ASPA Grado (GO) ItalyGoogle Scholar
  88. 88.
    Persuy MA, Printz C, Medrano JF, Mercier JC (1999) A single nucleotide deletion resulting in a premature stop codon is associated with marked reduction of transcripts from a goat beta-casein null allele. Anim Genet 30:444–451PubMedCrossRefGoogle Scholar
  89. 89.
    Galliano F, Saletti R, Cunsolo V, Foti S, Marletta D, Bordonaro S, D’Urso G (2004) Identification and characterization of a new beta-casein variant in goat milk by high-performance liquid chromatography with electrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun Mass Sp 18:1972–1982CrossRefGoogle Scholar
  90. 90.
    Cosenza G, Pauciullo A, Gallo D, Di Berardino D, Ramunno L (2005) A SspI PCR-RFLP detecting a silent allele at the goat CSN2 locus. J Dairy Res 72:456–459PubMedCrossRefGoogle Scholar
  91. 91.
    Caroli A, Chiatti F, Chessa S, Rignanese D, Bolla P, Pagnacco G (2006) Focusing on the goat casein complex. J Dairy Sci 89:3178–3187PubMedCrossRefGoogle Scholar
  92. 92.
    Mercier JC, Brignon G, Ribadeau-Duman B (1973) Structure primaire de la caséine κ B bovine. Sequence complete. Eur J Biochem 35:222–235PubMedCrossRefGoogle Scholar
  93. 93.
    Mercier JC, Addeo F, Pelissier JP (1976) Primary structure of the casein macropeptide of caprine κ-casein. Biochimie 58:1303–1310PubMedCrossRefGoogle Scholar
  94. 94.
    Brignon G, Chtourou A, Ribadeau-Dumas B (1985) Preparation and amino acid sequence of human κ-casein. FEBS Lett 188:48–54PubMedCrossRefGoogle Scholar
  95. 95.
    Bonsing J, Mackinlay AG (1987) Recent studies on nucleotide sequences encoding the caseins. J Dairy Res 54:447–461PubMedCrossRefGoogle Scholar
  96. 96.
    Gorodetskii SI, Kaledin AS (1987) Analysis of nucleotide sequence of bovine κ-casein cDNA. Genetika 23:398–404Google Scholar
  97. 97.
    Furet JP, Mercier JC, Soulier S, Gaye P, Hue-Delahaie D, Vilotte JL (1990) Nucleotide sequence of ovine κ-casein cDNA. Nucleic Acids Res 18:5286PubMedPubMedCentralCrossRefGoogle Scholar
  98. 98.
    Jollés P, Loucheux-Lefebvre MH, Henschen A (1978) Structural relatedness of k-casein and fibrinogen g-chain. J Mol Evol 11:271–277PubMedCrossRefGoogle Scholar
  99. 99.
    Mercier JC, Vilotte JL (1993) Structure and function of milk protein genes. J Dairy Sci 76:3079–3098PubMedCrossRefGoogle Scholar
  100. 100.
    Nakhasi HL, Grantham FH, Gullino PM (1984) Expression of k-casein in normal and neoplastic rat mammary gland is under the control of prolactin. J Biol Chem 259:14894–14898PubMedGoogle Scholar
  101. 101.
    Herskovitis TT (1966) On the conformation of caseins. Optical otator properties. Biochemistry 5:1018–1026CrossRefGoogle Scholar
  102. 102.
    Takeuchi M, Tsuda E, Yoshikawa M, Sasaki R, Chiba H (1984) Post-translational modification of κ-casein in the Golgi apparatus of mid-lactating mammary gland from rat and cow. Agr Biol Chem 48:2789–2797Google Scholar
  103. 103.
    Mepham TB, Gaye P, Martìn P, Mercier JC (1992) Biosynthesis of milk protein. In: Fox PF (ed) Advanced dairy chemistry. Elsevier, London, pp 491–543Google Scholar
  104. 104.
    Dziuba J, Minkiewicz P (1996) Influence of glycosylation on micelle stabilizing ability and biological properties of C-terminal fragments of cow’sk-casein. Int Dairy J 6:1017–1044CrossRefGoogle Scholar
  105. 105.
    Dev BC, Sood SM, DeWind S, Slattery CW (1993) Characterization of human κ-casein purified by FPLC. Prep Biochem Biotech 23:389–407Google Scholar
  106. 106.
    Jollés P, Fiat A (1979) The carbohydrate portions of milk glycoproteins. J Dairy Res 46:187–191PubMedCrossRefGoogle Scholar
  107. 107.
    Fiat AM, Jolles J, Aubert JP, Loucheux-Lefebvre M-H, Jolles P (1980) Localisation and importance of the sugar part of human casein. Eur J Biochem 111:333–339PubMedCrossRefGoogle Scholar
  108. 108.
    Yamauchi K, Azuma N, Kobayashi H, Kaminogawa S (1981) Isolation and properties of human κ-casein. J Biochem 90:1005–1012PubMedGoogle Scholar
  109. 109.
    Wong DWS, Camirand WM, Pavlath AE (1996) Structures and functionalities of milk proteins. Cr Rev Food Sci 36:807–844CrossRefGoogle Scholar
  110. 110.
    Mercier JC, Chobert JM, Addeo (1976) Comparative study of the amino acid sequences of the casein-macropeptides from seven species. FEBS Lett 72:208–214PubMedCrossRefGoogle Scholar
  111. 111.
    Walstra P, Jenness R, Badings HT (1984) Dairy chemistry and physics. Wiley, New YorkGoogle Scholar
  112. 112.
    Minkiewicz P, Dziuba J, Muzinska B (1993) The contribution of N-acetylneuraminic acid in the stabilization of micellar casein. Polish J Food Nutr Sci 433:39–48Google Scholar
  113. 113.
    Van Hooydonk ACM, Olieman C, Hagedoorn HG (1984) Kinetics of the chymosin-catalysed proteolysis of kappa casein in milk. Neth Milk Dairy J 38:207–222Google Scholar
  114. 114.
    Vreeman HJ, Visser S, Slangen KJ, van Riel JAM (1986) Characterization of bovine κ-casein fractions and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high performance gel-permeation chromatography. Biochem J 240:87–97PubMedPubMedCentralCrossRefGoogle Scholar
  115. 115.
    Pinders J, Perryc BN, Skidmoraend J, Sawa D (1991) Analysis of polymorphism in the bovine casein genes by use of the polymerase chain reaction. Anim Genet 22:11–20CrossRefGoogle Scholar
  116. 116.
    Huang W, Penagaricano F, Ahmad KR, Lucey JA, Weigel KA, Khatib H (2012) Association between milk protein gene variants and protein composition traits in dairy cattle. J Dairy Sci 95:440–449PubMedCrossRefGoogle Scholar
  117. 117.
    Pipalia DL, Ladani DD, Brahmkshtri BP, Rank DN, Joshi CG, Vataliya PH, Solanki JV (2001) Kappa-casein genotyping of Indian buffalo breed using PCR-RFLP. Buffalo J 2:195–202Google Scholar
  118. 118.
    Otaviano AR, Tonhati H, Sena JAD, Munoz MFC (2005) Kappa-casein gene study with molecular markers in female buffaloes (Bubalus bubalis). Genet Mol Biol 28:237–241CrossRefGoogle Scholar
  119. 119.
    Patel RK, Chauhan JB, Singh KM, Soni KJ (2007) Genotyping and allelic frequencies of κ-CN and β-LG in Indian river buffalo bulls. Buffalo B 26:63–66Google Scholar
  120. 120.
    Angiolillo A, Yahyaoui MH, Sanchez A, Pilla F, Folch JM (2002) Characterization of a new genetic variant in the caprine kappa casein gene. J Dairy Sci 85:2679–2680PubMedCrossRefGoogle Scholar
  121. 121.
    Yahyaoui MH, Angiolillo A, Pilla F, Sanchez A, Folch JM (2003) Characterization and genotyping of the caprine kappa casein variants. J Dairy Sci 86:2715–2720PubMedCrossRefGoogle Scholar
  122. 122.
    Prinzenberg EM, Gutscher K, Chessa S, Caroli A, Erhardt G (2005) Caprine κ-casein (CSN3) polymorphisms: new developments in molecular knowledge. J Dairy Sci 88:1490–1498PubMedCrossRefGoogle Scholar
  123. 123.
    Kiplagat SK, Agaba M, Kosgey IS, Okeyo M, Indetie D, Hanotte O, Limo MK (2010) Genetic polymorphism of kappa-casein gene in indigenous Eastern Africa goat populations. Int J Genet Mol Biol 2:1–5Google Scholar
  124. 124.
    Moioli B, D’Andrea M, Pilla F (2007) Candidate genes affecting sheep and goat milk quality. Small Rumin Res 68:179–192CrossRefGoogle Scholar
  125. 125.
    Prinzenberg EM, Jianlin H, Erhardt G (2008) Genetic variation in the kappa-casein gene (CSN3) of Chinese yak (Bos grunniens) and phylogenetic analysis of CSN3 sequences in the Genus Bos. J Dairy Sci 91:1198–1203PubMedCrossRefGoogle Scholar
  126. 126.
    Hobor S, Kunej T, Dovc P (2008) Polymorphisms in the kappa casein (CSN3) gene in horse and comparative analysis of its promoter and coding region. Anim Genet 39:520–530PubMedCrossRefGoogle Scholar
  127. 127.
    Selvaggi M, Pesce Delfino AR, Dario C (2010) Exon 1 polymorphisms in the equine CSN3 gene: SNPs distribution analysis in Murgese horse breed. Anim Biotechnol 21:252–256PubMedCrossRefGoogle Scholar
  128. 128.
    Selvaggi M, Dario C (2011) Analysis of two single-nucleotide polymorphisms (SNPs) located in exon 1 of kappa-casein gene (CSN3) in Martina Franca donkey breed. Afr J Biotechnol 10:5118–5120Google Scholar
  129. 129.
    Erhardt G (1989) κ-casein in Rindermilch-Nachweis eines weiteren Alleles (k-CnE) in Verschiedenen Rassen. J Anim Breed Genet 106:225–231CrossRefGoogle Scholar
  130. 130.
    Ikonen T, Ruottinen O, Erhardt G, Ojala M (1996) Allele frequencies of the major milk proteins in the Finnish Ayrshire and detection of a new k-casein variant. Anim Genet 27:179–181PubMedCrossRefGoogle Scholar
  131. 131.
    Grosclaude F, Mahé MF, Mercier JC, Ribadeau-Dumas B (1972) Localisation des substitutions d’acides aminés différenciant les variants a et b de la caséine × bovine. Ann Genet Sel Anim 4:515–521PubMedPubMedCentralGoogle Scholar
  132. 132.
    Bovenhuis H, van Arendonk JAM, Kerver S (1992) Associations between milk protein polymorphism and milk production traits. J of Dairy Sci 75:2549–2559CrossRefGoogle Scholar
  133. 133.
    Verdier-Metz I, Coulon JB, Pradel P (2001) Relationship between milk fat and protein contents and cheese yield. Anim Res 50:365–371CrossRefGoogle Scholar
  134. 134.
    Boettcher PJ, Caroli A, Stella A, Chessa S, Budelli E, Canavesi F, Ghiroldi S, Pagnacco G (2004) Effects of casein haplotypes on milk production traits in Italian Holstein and Brown Swiss cattle. J Dairy Sci 87:4311–4317PubMedCrossRefGoogle Scholar
  135. 135.
    Kűbarsepp I, Henno M, Viinalass H, Sabre D (2005) Effect of κ-casein and β-lactoglobulin genotypes on the milk rennet coagulation properties. Agr Res 1:55–64Google Scholar
  136. 136.
    Zittle CA, Custer JH (1966) Identification of the k-casein among the components of whole goat casein. J Dairy Sci 49:788–791PubMedCrossRefGoogle Scholar
  137. 137.
    Coll A, Folch JM, Sanchez A (1993) Nucleotide sequence of the goat k-casein cDNA. J Anim Sci 71:2833PubMedGoogle Scholar
  138. 138.
    Coll A, Folch JM, Sanchez A (1995) Structural features of the 5′ flanking region of the caprine k-casein gene. J Dairy Sci 79:973–977CrossRefGoogle Scholar
  139. 139.
    Yahyaoui MH, Coll A, Sanchez A, Folch JM (2001) Genetic polymorphism of the caprine kappa casein gene. J Dairy Res 78:209–216CrossRefGoogle Scholar
  140. 140.
    Caroli A, Jann O, Budelli E, Bolla P, Jager S, Erhardt G (2001) Genetic polymorphism of goat κ-casein (CSN3) in different breeds and characterization at DNA level. Anim Genet 32:226–230PubMedCrossRefGoogle Scholar
  141. 141.
    Jann OC, Prinzenberg EM, Luikart G, Caroli A, Erhardt G (2004) High polymorphism in the k-casein (CSN3) gene from wild and domestic caprine species revealed by DNA sequencing. J Dairy Res 71:188–195PubMedCrossRefGoogle Scholar
  142. 142.
    Caravaca F, Carrizosa J, Urrutia B, Baena F, Jordana J, Amillis M, Badaoui B, Sánchez A, Angiolillo A, Serradilla JM (2009) Effect of αS1-casein (CSN1S1) and κ-casein (CSN3) genotypes on milk composition in Murciano-Granadina goats. J Dairy Sci 92:2960–2964PubMedCrossRefGoogle Scholar
  143. 143.
    Reale S, Yahyaoui MH, Folch YM, Sanchez A, Pilla F, Angiolillo A (2005) Genetic polymorphism of the κ-casein (CSN3) gene in goats reared in Southern Italy. Ital J Anim Sci 4:97–101CrossRefGoogle Scholar
  144. 144.
    Othman EO, Ahmed S (2007) Genotyping of the caprine Kappa-casein variants in Egyptian breeds. Int J Dairy Sci 2:90–94CrossRefGoogle Scholar
  145. 145.
    Caravaca F, Ares JL, Carrizosa J, Urrutia B, Baena F, Jordana J, Badaoui B, Sànchez B, Angiolillo A, Amills M, Serradilla JM (2011) Effects of αs1-casein (CSN1S1) and κ-casein (CSN3) genotypes on milk coagulation properties in Murciano-Granadina goats. J Dairy Res 78:32–37PubMedCrossRefGoogle Scholar
  146. 146.
    Jenness R (1982) Inter-species comparison of milk proteins. In: Developments in dairy chemistry, vol 1, PF Fox (ed) Proteins. Applied Science, New YorkGoogle Scholar
  147. 147.
    Permyakov EA, Berliner L (2000) α-Lactalbumin: structure and function. FEBS Lett 473:269–274PubMedCrossRefGoogle Scholar
  148. 148.
    Ebner KE, Brodbeck U (1968) Biological role of α-lactalbumin: a review. J Dairy Sci 51:317–322PubMedCrossRefGoogle Scholar
  149. 149.
    Kuhn NJ (1983) The biosynthesis of lactose. In: TB Mepham (ed) Biochemistry of Lactation. Elsevier, AmsterdamGoogle Scholar
  150. 150.
    Hayssen V, Blackburn DG (1985) α-Lactalbumin and the origins of lactation. Evolution 39:1147–1149CrossRefGoogle Scholar
  151. 151.
    Brew K, Grobler JA (1992) α-lactalbumin. In PF Fox (ed) Advanced dairy chemistry, vol 1 (Proteins). Elsevier, New YorkGoogle Scholar
  152. 152.
    Heine WE, Klein PD, Reeds PJ (1991) The importance of α-lactalbumin in infant nutrition. J Nutr 121:277–283PubMedGoogle Scholar
  153. 153.
    Qasba PK, Safaya SK (1984) Similarity of nucleotide sequences of rat a-lactalbumin and chicken lysozyme genes. Nature 308:377–380PubMedCrossRefGoogle Scholar
  154. 154.
    Hall L, Emery DC, Davies MS, Parker D, Craig RK (1987) Organization and sequence of the human alpha-lactalbumin gene. Biochem J 242:735–742PubMedPubMedCentralCrossRefGoogle Scholar
  155. 155.
    Vilotte JL, Soulier S, Mercier JC, Gaye P, Hue-Delahaie D, Furet JP (1987) Complete nucleotide sequence of bovine α-lactalbumin gene. Comparison with its rat counterpart. Biochimie 69:609–620PubMedCrossRefGoogle Scholar
  156. 156.
    Vilotte JL, Soulier S, Printz C, Mercier JC (1991) Sequence of the goat α-lactalbumin-encoding gene: comparison with the bovine gene and evidence of related sequences in the goat genome. Gene 98:271–276PubMedCrossRefGoogle Scholar
  157. 157.
    Laird JE, Jack L, Hall L, Boulton AP, Parker D, Craig RK (1988) Structure and expression of the guinea-pig alpha-lactalbumin gene. Biochem J 254:85–94PubMedPubMedCentralCrossRefGoogle Scholar
  158. 158.
    Peters CW, Kruse U, Pollwein R, Grzeschik KH, Sippel A (1989) The human lysozyme gene: sequence organization and chromosomal localization. Eur J Biochem 182:507–516PubMedCrossRefGoogle Scholar
  159. 159.
    Threadgill DW, Womack JE (1990) Genomic analysis of the major bovine milk protein genes. Nucleic Acids Res 18:6935–6942PubMedPubMedCentralCrossRefGoogle Scholar
  160. 160.
    Hayes H, Popescu P, Dutrilaux B (1993) Comparative gene mapping of lactoperoxidase, retinoblastoma, and alpha-lactalbumin genes in cattle, sheep and goat. Mamm Genome 4:593–597PubMedCrossRefGoogle Scholar
  161. 161.
    Bleck GT, Bremel RD (1993) Sequence and single-base polymorphisms of the bovine α-lactalbumin 5`-flanking region. Gene 126:213–218PubMedCrossRefGoogle Scholar
  162. 162.
    Blumberg BS, Tombs MP (1958) Possible polymorphism of bovine α-lactalbumin. Nature 181:683–684PubMedCrossRefGoogle Scholar
  163. 163.
    Bhattacharya SD, Roy Choudhury AK, Sinha NK, Sen A (1963) Inherited α-lactalbumin and β-lactoglobulin polymorphism in Indian Zebu cattle. Comparison of zebu and buffalo α-lactalbumins Nature 197:797–799PubMedGoogle Scholar
  164. 164.
    Bell K, Hopper KE, Mckenzie HA, Murphy WH, Shaw DC (1970) A comparison of bovine α-lactalbumin A and B of droughtmaster. Biochim Biophys Acta 214:437–444PubMedCrossRefGoogle Scholar
  165. 165.
    Jenness R (1974) The composition of milk. In: Larson BL, Smith VR (eds) Lactation: a comprehensive treatise, vol 3. Academic Press, NewYorkGoogle Scholar
  166. 166.
    Osterhoff DR, Pretorius AMG (1966) Inherited biochemical polymorphism in milk proteins. Proc S Afr Soc Anim Prod 5:166–173Google Scholar
  167. 167.
    Mariani P, Russo V (1977) Polimorfismo genetico della α–lattoalbumina nelle razze bovine. Rivista di Zootecnia e Veterinaria 6:603–610Google Scholar
  168. 168.
    Gordon WG (1971) α-Lactalbumin. In: HA McKenzie (ed) Milk proteins, vol II. Academic Press, New YorkGoogle Scholar
  169. 169.
    Bleck GT, Bremel RD (1993) Correlation of the α-lactalbumin 5′ flanking region. J Dairy Sci 76:2292–2298PubMedCrossRefGoogle Scholar
  170. 170.
    Bell K, Hopper KE, McKenzie HA (1981) Bovine α-lactalbumin C and αs1-, β- and κ-caseins of Bali (Banteng) Cattle, Bos (Bibos) javanicus. Austr J Biol Sci 34:149–159Google Scholar
  171. 171.
    Visker MH, Heck JM, van Valenberg HJ, van Arendonk JA, Bovenhuis HJ (2012) A new bovine milk-protein variant: α-lactalbumin variant D. J Dairy Sci 95:2165–2169PubMedCrossRefGoogle Scholar
  172. 172.
    Cosenza G, Gallo D, Illario R, Gregorio D, Senese P, Ferrara LC, Ramunno L (2003) A Mval PCR-RFLP detecting a silent allele at the goat α-lactalbumin locus. J Dairy Res 70:355–357PubMedCrossRefGoogle Scholar
  173. 173.
    Lan XY, Pan CY, Chen H, Zhang CL, Zhang AL, Zhang L, Li JY, Lei CZ (2007) An MspI PCR-RFLP detecting a single nucleotide polymorphism at alpha-lactalbumin gene in goat. Czech J Anim Sci 52:138–142Google Scholar
  174. 174.
    Shewale JG, Sinha SK, Brew K (1984) Evolution of α-lactalbumins. The complete amino acid sequence of the α-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat α-lactalbumins. J Biol Chem 259:4947–4956PubMedGoogle Scholar
  175. 175.
    Jain A, Gour DS, Bisen PS, Prashant, Dubey PP, Sharma DK, Joshi BK, Kumar D (2009) Single nucleotide polymorphism (SNP) in alpha-lactalbumin gene of Indian Jamunapari breed of Capra hircus. Small Rumin Res 82:156–160CrossRefGoogle Scholar
  176. 176.
    Perez MD, Calvo M (1995) Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review. J Dairy Sci 78:978–988PubMedCrossRefGoogle Scholar
  177. 177.
    Flower DR (1996) The lipocalin protein family: structure and function. Biochem J 318:1–14PubMedPubMedCentralCrossRefGoogle Scholar
  178. 178.
    Businco L, Bellanti J (1993) Food allergy in childhood. Hypersensitivity to cow’s milk allergens. Clin Exp Allergy 23:481–483PubMedCrossRefGoogle Scholar
  179. 179.
    Folch JM, Coll A, Hayes HC, Sánchez A (1996) Characterization of a caprine beta-lactoglobulin pseudogene, identification and chromosomal localization by in situ hybridization in goat, sheep and cow. Gene 177:87–91PubMedCrossRefGoogle Scholar
  180. 180.
    Lunden A, Nilsson M, Janson L (1997) Marked effect of β-lactoglobulin polymorphism on the ratio of casein to total protein in milk. J Dairy Sci 80:2996–3005PubMedCrossRefGoogle Scholar
  181. 181.
    Yang F, Li L, Liu H, Cai Y, Wang G (2012) Polymorphism in the exon 4 of β-lactoglobulin variant B precursor gene and its association with milk traits and protein structure in Chinese Holstein. Mol Biol Rep 29:3957–3964CrossRefGoogle Scholar
  182. 182.
    Medrano JF, Aquilar-Cordova E (1990) Polymerase chain reaction amplification of bovine β-lactoglobulin genomic sequences and identification of genetic variants by RFLP analysis. Anim Biotechnol 1:73–77CrossRefGoogle Scholar
  183. 183.
    Martìn P, Szymanowska M, Zwierzchowski L, Leroux C (2002) The impact of genetic polymorphisms on the protein composition of ruminant milks. Reprod Nutr Dev 42:433–459PubMedCrossRefGoogle Scholar
  184. 184.
    Folch JM, Coll A, Sánchez A (1993) Rapid communication: cloning and sequencing of the cDNA encoding goat b-lactoglobulin. J Anim Sci 71:2832PubMedGoogle Scholar
  185. 185.
    Folch JM, Coll A, Sanchez A (1994) Complete sequence of the caprine β-lactoglobulin gene. J Dairy Sci 77:3493–3497PubMedCrossRefGoogle Scholar
  186. 186.
    Hayes H, Petit E (1993) Mapping of the β-lactoglobulin gene and of an immunoglobulin M heavy chain-like sequence to homologous cattle, sheep, and goat chromosomes. Mamm Genome 4:207–210PubMedCrossRefGoogle Scholar
  187. 187.
    Yahyaoui MH, Pena RN, Sánchez A, Folch JM (2000) Rapid communication: polymorphism in the goat β-lactoglobulin proximal promoter region. J Anim Sci 78:1100–1101PubMedGoogle Scholar
  188. 188.
    Chianese L, Portolano B, Troncone E, Pizzolongo F, Ferranti P, Addeo F, Alicata ML, Pilla F, Calagna G (2000) The quality of Girgentana goat milk. In: Proceedings of the 7th International Conference on GoatsGoogle Scholar
  189. 189.
    Graziano M, D’Andrea M, Angiolillo A, Lagonigro R, Pilla F (2003) A new polymorphism in goat β-lactoglobulin promoter region. Ital J Anim Sci 2:67–70Google Scholar
  190. 190.
    Pena RN, Sánchez A, Folch JM (2000) Characterization of genetic polymorphism in the goat β-lactoglobulin gene. J Dairy Res 67:217–224PubMedCrossRefGoogle Scholar
  191. 191.
    Ballester M, Sánchez A, Folch JM (2005) Polymorphisms in the goat b-lactoglobulin gene. J Dairy Res 72:379–384PubMedCrossRefGoogle Scholar
  192. 192.
    Kumar A, Rout PK, Roy R (2006) Polymorphism of beta-lactoglobulin gene in Indian goats and its effect on milk yield. J Appl Genet 47:49–53PubMedCrossRefGoogle Scholar
  193. 193.
    Renner E, Schaafsma G, Scott KJ (1989) Micronutrients in milk. In: E Renner (ed) Micronutrients in milk and milk—Based products. Elsevier, New YorkGoogle Scholar
  194. 194.
    Silanikove N, Leitner G, Merin U, Prosser CG (2010) Recent advances in exploiting goat’s milk: quality, safety and production aspects. Small Rumin Res 89:110–124CrossRefGoogle Scholar
  195. 195.
    Selvaggi M, Dario C, Normanno G, Celano GV, Dario M (2009) Genetic polymorphism of STAT5A protein: relationships with production traits and milk composition in Italian Brown cattle. J Dairy Res 76:441–445PubMedCrossRefGoogle Scholar
  196. 196.
    Dario C, Selvaggi M (2011) Study on the STAT5A/AvaI polymorphism in Jersey cows and association with milk production traits. Mol Biol Rep 38:5387–5392PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Maria Selvaggi
    • 1
  • Vito Laudadio
    • 1
  • Cataldo Dario
    • 1
  • Vincenzo Tufarelli
    • 1
  1. 1.Department of DETO—Section of Veterinary Science and Animal ProductionUniversity of Bari ‘Aldo Moro’ValenzanoItaly

Personalised recommendations