Hostname: page-component-77c89778f8-gvh9x Total loading time: 0 Render date: 2024-07-16T17:11:25.610Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of the A and B variants of both αs1- and κ-casein on bovine casein micelle solvation and κ-casein content

Published online by Cambridge University Press:  01 June 2009

Skelte G. Anema  and
Lawrence K. Creamer
Skelte G. Anema
Affiliation:
New Zealand Dairy Research Institute, Palmerston North, New Zealand
Lawrence K. Creamer
Affiliation:
New Zealand Dairy Research Institute, Palmerston North, New Zealand
Get access Rights & Permissions [Opens in a new window]

Summary

Casein micelle solvation, a micelle characteristic that is sensitive to many factors, has been measured by a centrifugation technique at 30 °C for a series of uncooled fresh skim milks at pH 6·3, 6·6, 6·9 and 7·1. The relative αs-(αs1- plus αs2-), β– and κ-casein contents of all centrifuge pellets and supernatants were determined by a standardized electrophoretic method. The calcium and phosphate contents of a number of the pellets and milk samples were also determined. Solvation of micelles from milks with various genetic variants of β-lactoglobulin (A and B), αs1-casein (A and B) and κ-casein (A and B) was often found to be lower for milks containing either the B variant of αs1-casein or the A variant of κ-casein. It was also found that these two variant caseins were associated with a lower κ-casein content of the milks and the micelles, which is consistent with the lower solvation as κ-casein is associated with smaller micelle size and greater solvation. The solvations also seemed to increase during the lactation period. It is possible that some of the other features of milk and its products that have been ascribed to the differences in functional character between the A and B variants of αs1-casein may be partly caused by the increased level of κ-casein. The reason for the association of the A variant of αs1-casein with higher concentrations of κ-casein (and micelle solvation) is not obvious but possibly the haplotype αs1-casein A, β-casein A1, κ-casein A contains a controlling sequence in the chromosomal DNA that enhances expression of the κ-casein gene.

Type
Original Articles
Information
Journal of Dairy Research , Volume 60 , Issue 4 , November 1993 , pp. 505 - 516
Copyright
Copyright © Proprietors of Journal of Dairy Research 1993

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Aschaffenburg, R. & Drewry, J. 1957 Genetics of the β-lactoglobulins of cow's milk. Nature 180 376–378CrossRefGoogle ScholarPubMed
Creamer, L. K. 1985 Water absorption by renneted casein micelles. Milchwissenschaft 40 589–591Google Scholar
Creamer, L. K. 1991 a Some aspects of casein micelle structure. In Interactions of Food Proteins, pp. 148–163 (Eds Parris, N. and Barford, R.). Washington, DC: American Chemical Society (ACS Symposium Series 454)CrossRefGoogle Scholar
Creamer, L. K. 1991 b Eleotrophoresis of cheese. International Dairy Federation Bulletin Document 261 14–28Google Scholar
Creamer, L. K. & Matheson, A. R. 1980 Effect of heat treatment on the proteins of pasteurized skim milk. New Zealand Journal of Dairy Science and Technology 15 37–49Google Scholar
Creamer, L. K., Zoerb, H. F., Olson, N. F. & Richardson, T. 1982 Surface hydrophobicity of αs1-I, αs1-casein A and B and its implication in cheese structure. Journal of Dairy Science 65 902–906CrossRefGoogle Scholar
Davies, D. T. & Law, A. J. R. 1977 The composition of whole casein from the milk of Ayrshire cows. Journal of Dairy Research 44 447–454CrossRefGoogle Scholar
Davies, D. T. & Law, A. J. R. 1983 Variation in the protein composition of bovine casein micelles and serum casein in relation to micellar size and milk temperature. Journal of Dairy Research 50 67–75CrossRefGoogle Scholar
Dewan, R. K., Chudgar, A., Bloomfield, V. A. & Morr, C. V. 1974 Size distribution and solvation of casein micelles in milk containing αs1-casein A. Journal of Dairy Science 57 394–398CrossRefGoogle Scholar
Farrell, H. M., Kumosinski, T. F., Pulaski, P. & Thompson, M. P. 1988 Calcium-induced associations of the caseins: a thermodynamic linkage approach to precipitation and resolubilization. Archives of Biochemistry and Biophysics 265 146–158CrossRefGoogle ScholarPubMed
Farrell, H. M., Thompson, M. P. & Larsen, B. 1971 Verification of the occurrence of the αs1-casein A allele in Red Danish cattle. Journal of Dairy Science 54 423–425CrossRefGoogle Scholar
Gordon, W. G., Basch, J. J. & Thompson, M. P. 1965 Genetic polymorphism in caseins of cow's milk. VI. Amino acid composition of αs1-caseins A, B, and C. Journal of Dairy Science 48 1010–1013CrossRefGoogle Scholar
Grosclaude, F., Mahé, M.-F., Brignon, G., Di Stasio, L. & Jeunet, R. 1987 A Mendelian polymorphism underlying quantitative variations of goat αs1-casein. Génétique, Sélection, Évolution 19 399–411 [Dairy Science Abstracts 50 596]Google Scholar
Grosclaude, F., Mahé, M.-F., Mercier, J.-C. & Ribadeau-Dumas, B. 1970 [Position, in the NH2-terminal part of bovine αs1-casein, of a deletion of 13 amino acids differentiating the variant A from the variants B and C.] FEBS Letters 11 109–112CrossRefGoogle Scholar
Holt, C. & Sawyer, L. 1988 Primary and predicted secondary structures of the caseins in relation to their biological functions. Protein Engineering 2 251–259CrossRefGoogle ScholarPubMed
Kalan, E. B., Greenberg, R. & Thompson, M. P. 1966 Analysis of proteolytic digests of genetic variants of αs1-casein. Archives of Biochemistry and Biophysics 115 468–477CrossRefGoogle Scholar
Kiddy, C. A., Johnston, J. O. & Thompson, M. P. 1964 Genetic polymorphism in caseins of cow's milk. I. Genetic control of αs-casein variation. Journal of Dairy Science 47 147–151CrossRefGoogle Scholar
Koczan, D., Hobom, G. & Seyfert, H.-M. 1991 Genomic organization of the bovine alpha-S1 casein gene. Nucleic Acids Research 19 5591–5596CrossRefGoogle ScholarPubMed
Kruk, A. 1979 [Effect of casein hydration on heat stability of milk.] Zeszyty Naukowe Akademii Rolniczo-Technicznej w Olsztynie, Technologia Żymności no. 14 185–221 [Dairy Science Abstracts 42 699]Google Scholar
Kumosinski, T. F., Brown, E. M. & Farrell, H. M. 1991 a Three-dimensional molecular modeling of bovine caseins: αs1-casein. Journal of Dairy Science 74 2889–2895CrossRefGoogle Scholar
Kumosinski, T. F., Pessen, H., Brown, E. M., Kakalis, L. T. & Farhell, H. M. 1991 b Quaternary structural changes of bovine casein by small-angle X-ray scattering: effect of genetic variation. In Interactions of Food Proteins, p. 182–194 (Eds Parris, N. and Barford, R.). Washington, DC: American Chemical Society (ACS Symposium Series 454)CrossRefGoogle Scholar
Lee, J. 1983 Calcium matrix effects in multi-element analysis of animal bone by inductively-coupled plasma emission spectrometry. Analytica Chimica Acta 152 141–147CrossRefGoogle Scholar
Lin, S. H. C., Leong, S. L., Dewan, R. K., Bloomfield, V. A. & Morr, C. V. 1972 Effect of calcium ion on the structure of native bovine casein micelles. Biochemistry 11 1818–1821CrossRefGoogle ScholarPubMed
McLean, D. M., Graham, E. R. B., Ponzoni, R. W. & McKenzie, H. A. 1984 Effects of milk protein genetic variants on milk yield and composition. Journal of Dairy Research 51 531–546CrossRefGoogle ScholarPubMed
Pessen, H., Kumosinski, T. F., Farrell, H. M. & Brumberger, H. 1991 Tertiary and quaternary structural differences between two genetic variants of bovine casein by small-angle X-ray scattering. Archives of Biochemistry and Biophysics 284 133–142CrossRefGoogle ScholarPubMed
Richardson, B. C., Creamer, L. K., Pearce, K. N. & Munford, R. E. 1974 Comparative micelle structure. II. Structure and composition of casein micelles in ovine and caprine milk as compared with those in bovine milk. Journal of Dairy Research 41 239–247CrossRefGoogle Scholar
Sadler, A. M., Kiddy, C. A., McCann, R. E. & Mattingly, W. A. 1968 Acid production and curd toughness in milks of different αs1-casein types. Journal of Dairy Science 51 28–30CrossRefGoogle Scholar
Snoeren, T. H. M., Klok, H. J., Van Hooydonk, A. C. M. & Damman, A. J. 1984 The voluminosity of casein micelles. Milchwissenschaft 39 461–463Google Scholar
Southward, C. R. & Dolby, R. M. 1968 Seasonal variation in the viscosity index and adhesive strength of casein from the milk of individual cows. Journal of Dairy Research 35 25–30CrossRefGoogle Scholar
Sullivan, R. A., Fitzpatrick, M. M. & Stanton, E. K. 1959 Distribution of kappa-casein in skim-milk. Nature 183 616–617CrossRefGoogle ScholarPubMed
Sullivan, R. A., Fitzpatrick, M. M., Stanton, E. K., Annino, R., Kissel, G. & Palermiti, F. 1955 The influence of temperature and electrolytes upon the apparent size and shape of α- and β-casein. Archives of Biochemistry and Biophysics 55 455–468CrossRefGoogle Scholar
Tarodo De La Fuente, B. & Alais, C. 1975 Solvation of casein in bovine milk. Journal of Dairy Science 58 293–300CrossRefGoogle Scholar
Thompson, M. P., Farrell, H. M. & Greenberg, R. 1969 a αs1-Casein A (Bos taurus): a probable sequential deletion of eight amino acid residues and its effects on physical properties. Comparative Biochemistry and Physiology 28 471–475CrossRefGoogle Scholar
Thompson, M. P., Gordon, W. G., Boswell, R. T. & Farrell, H. M. 1969 b Solubility, solvation, and stabilization of αs1- and β-caseins. Journal of Dairy Science 52 1166–1173CrossRefGoogle Scholar
Thompson, M. P., Kiddy, C. A., Pepper, L. & Zittle, C. A. 1962 Variations in the αs-casein fraction of individual cow's milk. Nature 195 1001–1002CrossRefGoogle Scholar
Threadgill, D. W. & Womack, J. E. 1990 Genomic analysis of the major bovine milk protein genes. Nucleic Acids Research 18 6935–6942CrossRefGoogle ScholarPubMed
Walstra, P. 1979 The voluminosity of bovine casein micelles and some of its implications. Journal of Dairy Research 46 317–323CrossRefGoogle ScholarPubMed
Walstra, P. 1990 On the stability of casein micelles. Journal of Dairy Science 73 1965–1979CrossRefGoogle Scholar
Waugh, D. F. 1971 Formation and structure of casein micelles. In Milk Proteins: Chemistry and Molecular Biology, vol. II, pp. 3–85 (Ed. McKenzie, H. A.). New York: Academic PressCrossRefGoogle Scholar
Waugh, D. F., Creamer, L. K., Slattery, C. W. & Dresdner, G. W. 1970 Core polymers of casein micelles. Biochemistry 9 786–795CrossRefGoogle ScholarPubMed
Waugh, D. F. & Noble, R. W. 1965 Casein micelles. Formation and structure. II. Journal of the American Chemical Society 87 2246–2257CrossRefGoogle ScholarPubMed