Hostname: page-component-cd9895bd7-fscjk Total loading time: 0 Render date: 2024-12-26T08:35:45.243Z Has data issue: false hasContentIssue false
  • English
  • Français

Heat-induced association of β-lactoglobulin and casein micelles

Published online by Cambridge University Press:  01 June 2009

Petrus Smits  and
Johan H. Van Brouwershaven
Petrus Smits
Affiliation:
Unilever Research, Vlaardingen, The Netherlands
Johan H. Van Brouwershaven
Affiliation:
Unilever Research, Vlaardingen, The Netherlands
Get access Rights & Permissions [Opens in a new window]

Summary

Heat-induced association of β-lactoglobulin (β-lg) and casein micelles, mainly at 85–90 °C, was studied by means of preparative ultracentrifugation, using [3H]-labelled β-lg. Qualitative aspects were studied by gel electrophoresis and electron microscopy. In this association, the formation of intermolecular S–S bonds between β-lg and κ-casein plays a role, but hydrophobic bonds are also involved.

After heating mixtures containing 25 g/kg casein and 4 g/kg β-lg at 90 °C for 20 min, the amount of β-lg sedimented with the casein micelles by ultracentrifugation decreased by approximately 30% when the milk salt buffer system was reduced to 0·25 of its normal concentration; it decreased by about 20% when the pH was increased from 6·8 to 7·3 and increased by 15% when the pH was reduced from 6·8 to 5·8. When the β-lg concentration was decreased from 4 to 2 g/kg, the amount of sedimented β-lg decreased by 25% after heating at 90 °C for 6 min. After heating in milk salt buffer, the amount of sedimented β-lg was 15% higher than after heating in a salt solution which contained neither Ca nor citrate ions.

Although α-lactalbumin (α-la) is involved in the heat-association of β-lg and casein micelles, no influence of α-la on the amount of associated β-lg was found. In addition to the heat-association product of β-lg and whole casein micelles, an association product consisting mainly of β-lg and κ-casein was also formed. This product was observed by electron microscopy as noodle-like particles. The size of these particles depended on the β-lg/κ-casein ratio.

Type
Original Articles
Information
Journal of Dairy Research , Volume 47 , Issue 3 , October 1980 , pp. 313 - 325
Copyright
Copyright © Proprietors of Journal of Dairy Research 1980

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

Argyle, P. J., Jones, N., Chandan, R. C. & Gordon, J. F. (1976). Journal of Dairy Research 43, 45–51.CrossRefGoogle Scholar
BaerA., A.,Oroz, M. & Blanc, B. (1976). Journal of Dairy Research 43, 419–432.CrossRefGoogle Scholar
Beeby, R., Hill, R. D. & Snow, N. S. (1971). In: Milk Proteins, vol. 2, pp. 421–465. (Ed. McKenzie., H. A.) New York: Academic Press.CrossRefGoogle Scholar
Bigelow, C. C. (1967). Journal of Theoretical Biology 16, 187–211.CrossRefGoogle Scholar
Creamer, L. K., Berry, G. P. & Matheson, A. R. (1978). New Zealand Journal of Dairy Science and Technology 13, 9–15.Google Scholar
Davies, F. L., Shankar, P. A., Brooker, B. E. & Hobbs, D. G. (1978). Journal of Dairy Research 45, 53–58.CrossRefGoogle Scholar
Elfagm, A. A. & Wheelock, J. V. (1977). Journal of Dairy Research 44, 367–371.CrossRefGoogle Scholar
Elfagm, A. A. & Wheelock, J. V. (1978). Journal of Dairy Science 61, 159–163.CrossRefGoogle Scholar
Fox, K. K., Harper, M. K., Holsinger, V. H. & Pallansch, M. J. (1967). Journal of Dairy Science 50,443–450.CrossRefGoogle Scholar
Gordon, W. G. & Ziegler, J. (1955). Biochemical Preparations 4, 16–23.Google Scholar
Hostettler, H., Imhof, K. & Stein, J. (1965). Milchwissenschaft 20, 189–198.Google Scholar
Jenness, R. & Koops, J. (1962). Netherlands Milk and Dairy Journal 16, 153–164.Google Scholar
Kalab, M., Emmons, D. B. & Sargant, A. G. (1976). Milchwissenschaft 31, 402–408.Google Scholar
Klostermeyer, H. & Reimerdes, E. H. (1977). Advances in Experimental Medicine and Biology 86B, 263–275.CrossRefGoogle Scholar
Koch, G. K., Heertje, I. & Van Stun, F. (1978). Radiochimica Acta 24, 215–219.CrossRefGoogle Scholar
Kolar, C. W. Jr & Brunner, J. R. (1967). Journal of Dairy Science 50, 941.Google Scholar
Lin, S. H. C.Leong, S. L., Dewan, R. K., Bloomfield, V. A. & Morr, C. V. (1972). Biochemistry 11, 1818–1821.CrossRefGoogle Scholar
Long, J. E., Van Winkle, Q. & Gould, I. A. (1963). Journal of Dairy Science 46, 1329–1334.CrossRefGoogle Scholar
McKenzie, H. A. & Wake, R. G. (1961). Biochimica et Biophysica Acta 47, 240–242.CrossRefGoogle Scholar
Morr, C. V. (1973). Journal of Dairy Science 56, 1258–1266.CrossRefGoogle Scholar
Morr, C. V. (1975). Journal of Dairy Science 58, 977–984.Google Scholar
Morr, C. V. & Josephson, R. V. (1968). Journal of Dairy Science 51, 1349–1355.CrossRefGoogle Scholar
Morrissey, P. A. & O'Mahony, F. (1976). Journal of Dairy Research 43, 267–274.CrossRefGoogle Scholar
Robbins, F. M. & Kronman, M. J. (1964). Biochimica et Biophysica Acta 82, 186–188.CrossRefGoogle Scholar
Rose, D. (1968). Journal of Dairy Science 51, 1897–1902.CrossRefGoogle Scholar
Sawyer, W. H. (1969). Journal of Dairy Science 52, 1347–1355.CrossRefGoogle Scholar
Snoeren, T. H. M. & Van Der Spek, C. A. (1977). Netherlands Milk and Dairy Journal 31, 352–355.Google Scholar
Tessier, H., Yaguchi, M. & Rose, D. (1969). Journal of Dairy Science 52, 139–145.CrossRefGoogle Scholar
Wake, R. G. & Baldwin, R. L. (1961). Biochimica et Biophysica Acta 47, 225–239.CrossRefGoogle Scholar
Waugh, D. F. (1971). In Milk Proteins, vol. 2, pp. 3–85. (Ed. McKenzie., H. A.) New York: Academic Press.CrossRefGoogle Scholar
Wheelock, J. V. & Kirk, A. (1974). Journal of Dairy Research 41, 367–372.CrossRefGoogle Scholar
Wiechen, A. & Knoop, A. M. (1974). Milchwissenschaft 29, 65–70.Google Scholar
Zittle, C. A., Dellamonica, E. S., Rudd, R. K. & Custer, J. H. (1957). Journal of the American Chemical Society 79, 4661–4666.CrossRefGoogle Scholar