Hostname: page-component-848d4c4894-2pzkn Total loading time: 0 Render date: 2024-06-03T07:00:17.885Z Has data issue: false hasContentIssue false
  • English
  • Français

Effects of iodate, hydrogen peroxide and dichromate on the denaturation of whey proteins in heated milk

Published online by Cambridge University Press:  01 June 2009

Richard J. Marshall
Richard J. Marshall
Affiliation:
National Institute for Research in Dairying (University of Reading), Shinfield, Reading RG2 9 AT, UK*
Get access Rights & Permissions [Opens in a new window]

Summary

The effect of heating raw milk at 75 °C for 30 min and at 95 °C for 15 s in the presence of varying concentrations of three oxidizing agents on the denaturation of total and individual whey proteins was measured. At 75 °C, ±-lactalbumin could be protected against denaturation by both iodate and H202 and ²-Lactoglobulins A and B by H202 and dichromate. However, at concentrations above ∼ 15 MM, the oxidizing agents tended to increase denaturation. At 95 °C, where the extent of whey protein denaturation was much reduced in the absence of oxidizing agents, little or no protective effect was observed. It is suggested that H202 may prove a suitable alternative to iodate in reducing deposits in ultra high temperature plants.

Type
Original Articles
Information
Journal of Dairy Research , Volume 53 , Issue 1 , February 1986 , pp. 89 - 95
Copyright
Copyright © Proprietors of Journal of Dairy Research 1986

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

Blakesby, R. W. & Boezi, J. A. 1977 A new staining technique for proteins in polyaorylamide gels using Coomassie Brilliant Blue G250. Analytical Biochemistry 82 580–582CrossRefGoogle 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
Fish, N. L. & Mickelsen, R. 1967 Effect of hydrogen peroxide treatment on heat induced interaction of κ-casein and ²-lactoglobulin. Journal of Dairy Science 50 1360–1362CrossRefGoogle Scholar
Gregory, M. E., Henry, K. M., Kon, S. K., Porter, J. W. G., Thompson, S. Y. & Benjamin, M. I. W. 1961 The effect of hydrogen peroxide on the nutritive value of milk. Journal of Dairy Research 28 177–182CrossRefGoogle Scholar
Hillier, R. M. 1976 The quantitative measurement of whey proteins using polyacrylamide-gel electrophoresis. Journal of Dairy Research 43 259–265CrossRefGoogle ScholarPubMed
Hird, F. J. R. & Yates, J. R. 1961 The oxidation of protein thiol groups by iodate, bromate and persulphate. Biochemical Journal 80 612–616CrossRefGoogle ScholarPubMed
Lyster, R. L. J. 1964 The free and masked sulphydryl groups of heated milk and milk powder and a new method for their determination. Journal of Dairy Research 31 41–51CrossRefGoogle Scholar
Lyster, R. L. J. 1970 The denaturation of ±-laetalbumin and ²-lactoglobulin in heated milk. Journal of Dairy Research 37 233–243CrossRefGoogle Scholar
McKenzie, H. A. 1971 Milk Proteins: Chemistry and Molecular Biology Vol.2. New York and London: Academic PressGoogle Scholar
Morris, H. A. & Jezeski, J. J. 1964 Influence of the hydrogen peroxide-catalase milk treatment on Cheddar cheese hardness. Journal of Dairy Science 47 681Google Scholar
Perlmutter, R. M. & Brunner, J. R. 1972 Effect of hydrogen peroxide and heat on some characteristics of ²-lactoglobulin. Journal of Dairy Science 55 1064–1068CrossRefGoogle Scholar
Roundy, Z. D. 1958 Treatment of milk for cheese with hydrogen peroxide. Journal of Dairy Science 41 1460–1465CrossRefGoogle Scholar
Rowland, S. J. 1938 The determination of the nitrogen distribution in milk. Journal of Dairy Research 9 42–46CrossRefGoogle Scholar
Röegg, M., Moor, U. & Blanc, B. 1977 A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate. Journal of Dairy Research 44 509–520CrossRefGoogle Scholar
Sawyer, W. H. 1969 Complex between ²-Lactoglobulin and κ-casein. A review. Journal of Dairy Science 52 1347–1355CrossRefGoogle Scholar
Sawyer, W. H., Coulter, S. T. & Jenness, R. 1963 Role of sulphydryl groups in the interactions of κ-casein and ²-Lactoglobulin. Journal of Dairy Science 46 564–565CrossRefGoogle Scholar
Shudder, P. J., Thomas, E. L., Pavey, J. A. & Perkin, A. G. 1981 Effects of adding potassium iodate to milk before UHT treatment. I. Reduction in the amount of deposit on the heated surfaces. Journal of Dairy Research 48 99–113CrossRefGoogle Scholar
Smits, P. & Van BROUWERSHAVEN, J. H. 1980 Heat-induced association of ²-Lactoglobulin and casein micelles. Journal of Dairy Research 47 313–325CrossRefGoogle Scholar
Sreedhara, N. & Subramanean, M. 1981 Physicochemical properties of hydrogen peroxide treated groundnut protein. Journal of Food Science 46 1260–1264CrossRefGoogle Scholar
Swaisgood, H. E. 1982 Chemistry of milk protein. In Developments in Dairy Chemistry -1. Proteins pp. 1–59 (Ed. Fox, P. F.) London: Applied Science PublishersGoogle Scholar