Hostname: page-component-78c5997874-v9fdk Total loading time: 0 Render date: 2024-11-19T05:33:24.045Z Has data issue: false hasContentIssue false

Influence of concentration of milk solids on the dissociation of micellar κ-casein on heating reconstituted milk at 120°C

Published online by Cambridge University Press:  01 June 2009

Harjinder Singh
Affiliation:
New Zealand Dairy Research Institute, Private Bag, Palmerston North, New Zealand
Lawrence K. Creamer
Affiliation:
New Zealand Dairy Research Institute, Private Bag, Palmerston North, New Zealand

Summary

Skim milks were prepared from skim milk powder at several concentrations between 10 and 25% total solids and portions were pH-adjusted to between pH 6·3 and 7·1 and heated at 120°C. After ultracentrifugation (88000 g for 90 min), the supernatants were analysed using gel electrophoresis to determine the concentrations of β-lactoglobulin, α-lactalbumin and κ-casein. The dissociation of κ-casein from the micelles was dependent on both the pH and the total solids content of milk before heating. Both higher pH (in the range 6·5–7·l) and higher concentration increased the extent of dissociation. A further series of samples were heated for 2–11 min at 120°C at pH 6·55. κ-Casein dissociation increased with concentration and with heating time. It was concluded that as the milk increased in concentration, the pH at which micellar κ-casein dissociated on heating was lowered.

Type
Original articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1991

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

Aoki, T., Suzuki, H. & Imamura, T. 1974 Formation of soluble casein in whey protein-free milk heated at high temperature. Milchwissenschaft 29 589594Google Scholar
Aoki, T., Suzuki, H. & Imamura, T. 1975 Some properties of soluble casein in heated concentrated whey protein-free milk. Milchwissenschaft 30 3035Google 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 3749Google Scholar
Kudo, S. 1980 The heat stability of milk: formation of soluble proteins and protein depleted micelles at elevated temperatures. New Zealand Journal of Dairy Science and Technology 15 255263Google Scholar
Laemmli, U. K. 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 680685CrossRefGoogle ScholarPubMed
Mojonnier, T. & Troy, H. C. 1925 The Technical Control of Dairy Products. 2nd edn pp. 122131Chicago, IL: Mojonnier Bros Co.Google Scholar
Muir, D. D. & Sweetsur, A. W. M. 1978 The effect of concentration on the heat, stability of skim-milk. Journal of Dairy Research 45 3745CrossRefGoogle Scholar
Newstead, D. F., Sanderson, W. B. & Conaghan, E. F. 1977 Effects of whey protein concentrations and heat treatment on the heat stability of concentrated and unconcentrated milk. New Zealand Journal of Dairy Science and Technology 12 2936Google Scholar
Rose, D. 1961 Variations in the heat stability and composition of milk from individual cows during lactation. Journal of Dairy Science 44 430441Google Scholar
Singh, H. & Creamer, L. K. 1990 Aggregation and dissociation of milk protein complexes in heated reconstituted skim milks. Journal of Food Science 55 (In press)Google Scholar
Singh, H., Creamer, L. K. & Newstead, D. F. 1989 Effects of heat on the proteins of concentrated milk systems. International Dairy Federation Bulletin No. 238 94104Google Scholar
Singh, H. & Fox, P. F. 1985 Heat stability of milk: pH-dependent dissociation of micellar κ-casein on heating milk at ultra high temperatures. Journal of Dairy Research 52 529538CrossRefGoogle Scholar
Singh, H. & Fox, P. F. 1986 Heat stability of milk: further studies on the pH-dependent dissociation of micellar κ-casein. Journal of Dairy Research 53 237248Google Scholar
Singh, H. & Fox, P. F. 1987 a Heat stability of milk: role of β-lactoglobulin in the pH-dependent dissociation of micellar κ-casein. Journal of Dairy Research 54 509521Google Scholar
Singh, H. & Fox, P. F. 1987 b Heat stability of milk: influence of colloidal and soluble salts and protein modification on the pH-dependent dissociation of micellar κ-casein. Journal of Dairy Research 54 523534CrossRefGoogle Scholar
Smits, P. & Van Brouwershaven, J. H. 1980 Heat-induced association of β-lactoglobulin and casein micelles. Journal of Dairy Research 47 313325Google Scholar
Sweetsur, A. W. M. & White, J. C. D. 1974 Studies on the heat stability of milk protein. 1. Interconversion of type A and type B milk heat-stability curves. Journal of Dairy Research 41 349358CrossRefGoogle Scholar
White, J. C. D. & Davies, D. T. 1966 The stability of milk protein to heat. III. Objective measurement of heat stability of milk. Journal of Dairy Research 33 93102Google Scholar