Hostname: page-component-586b7cd67f-l7hp2 Total loading time: 0 Render date: 2024-11-26T14:38:06.393Z Has data issue: false hasContentIssue false
  • English
  • Français

Denaturation, aggregation and heat stability of milk protein during the manufacture of skim milk powder

Published online by Cambridge University Press:  01 June 2009

Harjinder Singh  and
Lawrence K. Creamer
Harjinder Singh
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

The effect of preheat treatment, evaporation and drying in a commercial plant on the denaturation of βlactoglobulin and α-lactalbumin, their incorporation into the casein micelle and the heat stability characteristics of the milks and powders were determined. Preheat treatments between 110 °C for 2 min and 120 °C for 3 min denatured between 80 and 91% of β-lactoglobulin and between 33 and 45% of α-lactalbumin. Evaporation increased the extent of denaturation but spray drying did not increase it further. The incorporation of α-lactalbumin and βlactoglobulin into the micelles was markedly less than the amount that denatured and was not a constant ratio to it. Heat coagulation times at 140 °C of milks, concentrates and powders diluted to the original milk concentration were measured as a function of pH. In general, the greater the collective heat treatment, the shorter the time required to achieve coagulation. Spray drying shifted the peak positions in the pH-heat coagulation time profiles. In contrast, heat coagulation times (measured at 120 °C) of concentrates and powders diluted to 20% total solids content increased with the severity of the preheat treatment. Surprisingly, spray drying markedly increased the heat coagulation times of the diluted concentrates.

Type
Original Articles
Information
Journal of Dairy Research , Volume 58 , Issue 3 , August 1991 , pp. 269 - 283
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

Andrews, A. T. 1983 Proteinases in normal bovine milk and their action on caseins. Journal of Dairy Research 50 45–55Google Scholar
Aoki, T., Suzuki, H. & Imamura, T. 1975 Some properties of soluble caseins in heated concentrated whey proteinfree milk. Milchwissenschaft 30 30–35Google Scholar
Belec, J. & Jenness, R. 1962 Dephosphorization of casein by heat treatment. 2. In skimmilks. Journal of Dairy Science 45 20–26CrossRefGoogle Scholar
Creamer, L. K., Berry, G. P. & Matheson, A. R. 1978 The effect of pH on protein aggregation in heated skim milk. New Zealand Journal of Dairy Science and Technology 13 9–15Google 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
Crosby, E. J. & Marshall, W. R. 1958 Effects of drying conditions on the properties of spray-dried particles. Chemical Engineering Progress 54 56–60Google Scholar
Dannenberg, F. & Kessler, H. G. 1988 Reaction kinetics of the denaturation of whey proteins in milk. Journal of Food Science 53 258–263Google Scholar
Davies, D. T. & White, J. C. D. 1959 Determination of heat-induced changes in the protein stability and chemical composition of milk. 15th International Dairy Congress, London 3 1677–1685Google Scholar
Doi, H., Ideno, S., Ibuki, F. & Kanamori, M. 1983 Participation of the Hydrophobic bond in complex formation between κ-casein and β-lactoglobulin. Agricultural and Biological Chemistry 47 407–409Google Scholar
Fox, P. F. 1982 Heat-induced coagulation of milk. In Developments in Dairy Chemistry 1. Proteins pp. 189–228 (Ed. Fox, P. F.) London: Applied Science PublishersGoogle Scholar
Fox, P. F. & Hoynes, M. C. T. 1975 Heat stability of milk; influence of colloidal calcium phosphate and β-lactoglobulin. Journal of Dairy Research 42 427–435CrossRefGoogle Scholar
Harland, H. A., Coulter, S. T. & Jenness, R. 1952 The effect of the various steps in the manufacture on the extent of serum protein denaturation in nonfat dry milk solids. Journal of Dairy Science 35 363–368Google Scholar
Haque, Z. & Kinsella, J. E. 1988 Interaction between κ-casein and β-lactoglobulin: predominance of Hydrophobic interactions in the initial stages of complex formation. Journal of Dairy Research 55 67–80Google Scholar
Hillier, R. M. 1976 The quantitative measurement of whey proteins using polyacrylamide-gel electro-phoresis. Journal of Dairy Research 43 259–265CrossRefGoogle Scholar
Hunziker, H. G. & Tarassuk, N. P. 1965 Chromatographic evidence for heat-induced interaction of α-lactalbumin and β-lactoglobulin. Journal of Dairy Science 48 733–734CrossRefGoogle ScholarPubMed
Kelly, P. M. 1982 Effect of seasonal variation, urea addition and ultrafiltration on the heat stability of skim-milk powder. Journal of Dairy Research 49 119–126CrossRefGoogle Scholar
Kieseker, F. G. 1976 Milk proteins in the manufacture of milk powders. Milk Protein Workshop, Tanunda, South Australia H1-H14Google Scholar
King, D. W., Sanderson, W. B. & Woodhams, D. J. 1974 Spray drying of dairy products. Dairy Jndustries 39 13–16Google Scholar
Laemmli, U. K. 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 680–685CrossRefGoogle ScholarPubMed
Larson, B. L. & Rolleri, G. D. 1955 Heat denaturation of the specific serum proteins in milk. Journal of Dairy Science 38 351–360CrossRefGoogle Scholar
Mojonnier, T. & Troy, H. C. 1925 Technical Control of Dairy Products, 2nd edn pp. 122–131Chicago, IL: Mojonnier BrosGoogle Scholar
Morr, C. V. 1973 Milk ultracentrifugal opalescent layer. 2. Physico-chemical properties. Journal of Dairy Science 56 1258–1266CrossRefGoogle Scholar
Muir, D. D., Abbot, J. & Sweetsur, A. W. M. 1978 Changes in the heat stability of milk protein during the manufacture of dried skim-milk. Journal of Food Technology 13 45–53CrossRefGoogle Scholar
Muir, D. D., Sweetsur, A. W. M. & Holt, C. 1979 The synergic effect of urea and aldehydes on the heat stability of concentrated skim-milk. Journal of Dairy Research 46 381–384CrossRefGoogle Scholar
Newstead, D. F., Sanderson, W. B. & Baucke, A. G. 1975 The effects of heat treatment and pH on the heat stability of recombined evaporated milk. New Zealand Journal of Dairy Science and Technology 10 113–118Google 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 29–36Google Scholar
Nieuwenhuijse, J. A., Timmermans, W. & Walstra, P. 1988 Calcium and phosphate partitions during the manufacture of sterilized concentrated milk and their relations to the heat stability. Netherlands Milk and Dairy Journal 42 387–421Google Scholar
Noh, B., Richardson, T. & Creamer, L. K. 1989 Radiolabelling study of the heat-induced interactions between α-lactalbumin, β-lactoglobulin and κ-casein in milk and in buffer solution. Journal of Food Science 54 889–893Google Scholar
O'Connor, F., McKenna, B. M. & O'Sullivan, A. C. 1969 Bacteriological and whey protein denaturation aspects of heating processes used in the manufacture of low-heat skim-milk powder. Irish Journal of Agriculture Research 8 417–430Google Scholar
Powell, M. E. & Palmer, L. S. 1935 Behavior of caseinate sols in a study of a hysteresis-like phenomenon in the rennet coagulation of heated milk. Journal of Dairy Science 18 401–414CrossRefGoogle Scholar
Pyne, G. T. 1958 The heat coagulation of milk. 2. Variations in the sensitivity of casein to calcium ions. Journal of Dairy Research 25 467–474CrossRefGoogle Scholar
Rose, D. 1961 Factors affecting the pH-sensitivity of the heat stability of milk from individual cows. Journal of Dairy Science 44 1405–1413CrossRefGoogle Scholar
Rose, D. & Tessier, H. 1959 Composition of ultrafiltrates from milk heated at 80 to 230° F. in relation to heat stability. Journal of Dairy Science 42 969–980Google Scholar
Shalabi, S. I. & Fox, P. F. 1982 Effect of diacetyl on the heat stability of concentrated milk. Journal of Food Technology 17 753–760Google Scholar
Shalabi, S. I. & Wheelock, J. V. 1976 The role of α-lactalbumin in the primary phase of chymosin action on heated casein micelles. Journal of Dairy Research 43 331–335Google 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 94–104Google 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 52 529–538Google Scholar
Singh, H. & Fox, P. F. 1987 Heat stability of milk: role of β-lactoglobulin in the pH-dependent dissociation of micellar κ-casein. Journal of Dairy Research 54 509–521Google Scholar
Smits, P. & Van Brouwershaven, J. H. 1980 Heat-induced association of β-lactoglobulin and casein micelles. Journal of Dairy Research 47 313–325CrossRefGoogle ScholarPubMed
Snoeren, T. H. M. & van der Spek, C. A. 1977 Isolation of a heat-induced complex from UHTST milk. Netherlands Milk and Dairy Journal 31 352–355Google Scholar
Tessier, H. & Rose, D. 1964 Influence of κ-casein and β-lactoglobulin on the heat stability of skimmilk. Journal of Dairy Science 47 1047–1051Google Scholar
Trautman, J. C. & Swanson, A. M. 1959 Protein complex formation in evaporated milk. Journal of Dairy Science 42 895Google Scholar
Walstra, P. & Jenness, R. 1984 Dairy Chemistry and Physics pp 317–320New York: John Wiley & SonsGoogle Scholar
Webb, B. H. & Bell, R. W. 1942 The effect of high-temperature short-time forewarming of milk upon the heat stability of its evaporated product. Journal of Dairy Science 25 301–311Google Scholar
Wright, N. C. 1932 Factors affecting the solubility of milk powders. 1. The effect of heat on the solubility of milk proteins. Journal of Dairy Research 4 123–141CrossRefGoogle Scholar