Hostname: page-component-586b7cd67f-rdxmf Total loading time: 0 Render date: 2024-11-26T13:46:07.095Z Has data issue: false hasContentIssue false

Heat stability of milk: the mechanism of stabilization by formaldehyde

Published online by Cambridge University Press:  01 June 2009

Harjinder Singh
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic
Patrick F. Fox
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic

Summary

The increase produced by formaldehyde (HCHO) in the heat stability of milk did not occur when milk was treated with HCHO at temperatures up to 60°C followed by dialysis at 5°C. However, the minimum in the heat coagulation time (HCT)–pH curve was irreversibly removed if the milk was preheated at 80–C for 10 min in the presence of 5 mM-HCHO. Although this treatment blocked the ε-amino groups of lysyl residues, the stabilizing mechanism is considered to be due to the cross linking action of HCHO which reduced the level of non-sedimentable, κ-casein-rich protein dissociated from the micelles on heating. The specific crosslinking agent, dimethyl suberimidate, modified the HCT-pH profile of milk in a manner similar to preheating at 80°C for 10 min with 5 mM-HCHO, supporting the crosslinking hypothesis. The results of this study appear to lend some support to the proposal of Kudo (1980) that the minimum in the HCT-pH curve of milk is due to the dissociation of κ-casein from the micelles on heating at high temperatures at pH values greater than 6η7.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1985

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. & Kako, Y. 1983 Relation between micelle size and formation of soluble casein on heating concentrated milk. Journal of Dairy Research 50 207213CrossRefGoogle Scholar
Aoki, T. & Kako, Y. 1984 Effect of formaldehyde on the heat stability of concentrated milk and the formation of soluble casein. Agricultural and Biological Chemistry 48 10171021Google Scholar
Aoki, T., Suzuki, H. & Imamura, T. 1975 Some properties of soluble casein in heated concentrated whey protein-free milk. Milchwissenschaft 30 3035Google Scholar
Association Of Official Analytical Chemists 1970 Official Methods of Analysis of the Association of Official Analytical Chemists 11th edn p. 858Washington, DC: AOACGoogle Scholar
Carpenter, K. J. & Booth, V. H. 1973 Damage to lysine in food processing: its measurement and its significance. Nutrition Abstracts and Reviews 43 423451Google Scholar
Davies, D. T. & White, J. C. D. 1966 The stability of milk protein to heat. I. Subjective measurement of heat stability of milk. Journal of Dairy Research 33 6781CrossRefGoogle Scholar
Davies, G. E. & Stark, G. R. 1970 Use of dimethyl suberimidate, a crosslinking reagent, in studying the subunit structure of oligomeric proteins. Proceedings of National Academy of Sciences of the USA 66 651656CrossRefGoogle ScholarPubMed
Fox, P. F. & Hearn, C. M. 1978 Heat stability of milk: influence of denaturable proteins and detergents on pH sensitivity. Journal of Dairy Research 45 159172CrossRefGoogle 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 427435CrossRefGoogle Scholar
Fraenkel-Conrat, H., Brandon, B. A. & Olcott, H. S. 1947 The reaction of formaldhyde with proteins. IV. Participation of indole groups. Gramicidin. Journal of Biological Chemistry 168 99117CrossRefGoogle Scholar
Fraenkel-Conrat, H. & Olcott, H. S. 1948 a The reaction of formaldehyde with proteins. V. Crosslinking between amino and primary amide or guanidyl groups. Journal of the American Chemical Society 70 26732684CrossRefGoogle ScholarPubMed
Fraenkel-Conrat, H. & Olcott, H. S. 1948 b Reaction of formaldehyde with proteins. VI. Crosslinking of amino groups with phenol, imidazole, or indole groups. Journal of Biological Chemistry 174 827843CrossRefGoogle ScholarPubMed
French, D. & Edsall, J. T. 1945 The reactions of formaldehyde with amino acids and proteins. Advances in Protein Chemistry 2 277335CrossRefGoogle Scholar
Holt, C., Muir, D. D. & Sweetsur, A. W. M. 1978 The heat stability of milk and concentrated milk containing added aldehydes and sugars. Journal of Dairy Research 45 4752CrossRefGoogle Scholar
Hunter, M. J. & Ludwig, M. L. 1962 The reaction of imidoesters with proteins and related small molecules. Journal of the American Chemical Society 84 34913504CrossRefGoogle Scholar
Jenness, R. & Koops, J. 1962 Preparation and properties of a salt solution which simulates milk ultrafiltrate. Netherlands Milk and Dairy Journal 16 153164Google Scholar
Kosikowski, F. V. 1944 The effect of high temperature and various chemical agents upon the heat stability, browning and apparent changes in lactose concentration of whole and evaporated milk. Ph.D. Thesis, Cornell University, Ithaca, NYGoogle 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 & Technology 15 255263Google 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, 381384.CrossRefGoogle Scholar
Nelson, V. 1954 Effects of formaldehyde and copper salts on the heat stability of evaporated milk. Journal of Dairy Science 37 825829CrossRefGoogle Scholar
Pyne, G. T. 1932 The determination of milk-proteins by formaldehyde titration. Biochemical Journal 26 10061014.CrossRefGoogle ScholarPubMed
Shalabi, S. I. & Fox, P. F. 1982 a Heat stability of milk: synergic action of urea and carbonyl compounds. Journal of Dairy Research 49 197207CrossRefGoogle Scholar
Shalabi, S. I. & Fox, P. F. 1982 b Heat stability of milk: influence of modification of lysine and arginine on the heat stability-pH profile. Journal of Dairy Research 49 607617CrossRefGoogle ScholarPubMed
Thompson, M. P., Kiddy, C. A., Johnston, J. O. & Weinberg, R. M. 1964 Genetic polymorphism in caseins of cows' milk. II. Confirmation of the genetic control of β-casein variation. Journal of Dairy Science 47 378381CrossRefGoogle Scholar
Warren, L. 1959 The thiobarbituric acid assay of sialic acids. Journal of Biological Chemistry 234 19711975CrossRefGoogle ScholarPubMed
Zittle, C. A. & Dellamonica, E. S. 1956 Viscosity and flocculation of heated β-lactoglobulin solutions; effect of calcium concentration and pH. Journal of Dairy Science 39 514521CrossRefGoogle Scholar