Hostname: page-component-586b7cd67f-l7hp2 Total loading time: 0 Render date: 2024-11-27T07:15:20.079Z Has data issue: false hasContentIssue false

Effects of β-lactoglobulin and κ-casein genetic variants and concentrations on syneresis of gels from renneted heated milk

Published online by Cambridge University Press:  01 June 2009

Douglas M. McLean
Affiliation:
Northfield Research Centre, Department of Agriculture, Adelaide, SA 5000, Australia
Johan Schaar
Affiliation:
Department of Animal Breeding and Genetics, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden

Extract

Milk protein genetic polymorphism has a major influence on the composition of milk, and on its processing properties, including yield of cheese (see Schaar et al. 1985; McLean et al. 1984, 1987; McLean, 1987). However, there appears to be little information on the effects of milk protein genetic variants on syneresis of cheese curd. The effect of casein composition on syneresis was studied by Pearse et al. (1986), who found that syneresis was affected only by the level of β-casein. Syneresis is an essential requirement in cheese making from renneted or acidified milk, but is undesirable during the storage of products such as yogurt. Milk for yogurt manufacture is preheated to minimize syneresis and to give maximal firmness of the yogurt coagulum (Tamime & Deeth, 1980). Pearse et al. (1985) showed that the reduction of one-third in the extent of syneresis caused by heating artificial micelle milk (AMM) containing βlactoglobulin (β-lg) in natural concentrations was due to sulphydryl-mediated complex formation between β-lg and micellar κ-casein which appeared to interfere with the micelle–micelle interactions responsible for syneresis. The results presented here were part of a study which investigated the effects of κcasein and κ-lg genetic variants and concentrations on syneresis of curd formed from renneted heated AMM.

Type
Short Communication
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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

Armstrong, J. McD., McKenzie, H. A. & Sawyer, W. H. 1967 On the fractionation of β-lactoglobulin and α-lactalbumin. Biochimica et Biophysica Acta 147 6072CrossRefGoogle ScholarPubMed
Ford, G. D. & Grandison, A. S. 1986. Effect of size of casein micelles on coagulation properties of skim milk. Journal of Dairy Research 53 129133CrossRefGoogle Scholar
Gough, P. & Jenness, R. 1962 Heat denaturation of β-lactoglobulins A and B. Journal of Dairy Science 45 10331039CrossRefGoogle Scholar
McKenzie, G. H., Norton, R. S. & Sawyer, W. H. 1971 Heat-induced interaction of β-lactoglobulin and κ-casein. Journal of Dairy Research 38 343351CrossRefGoogle Scholar
McLean, D. M. 1987 Influence of milk protein genetic variants on milk composition, yield and cheesemaking properties. Animal Genetics 18 Supplement 1, 100102Google Scholar
McLean, D. M., Graham, E. R. B., Ponzoni, R. W. & McKenzie, H. A. 1984 Effects of milk protein genetic variants on milk yield and composition. Journal of Dairy Research 51 531546CrossRefGoogle ScholarPubMed
McLean, D. M., Graham, E. R. B., Ponzoni, R. W. & McKenzie, H. A. 1987 Effects of milk protein genetic variants and composition on heat stability of milk. Journal of Dairy Research 54 219235CrossRefGoogle Scholar
Mariani, P., Losi, G., Russo, V., Castagnetti, G. B., Grazia, L., Morini, D. & Fossa, E. 1976 [Caseification tests made with milk characterized by variants A and B of κ-casein in the production of Parmigiano-Reggiano cheese.] Scienza e Tecnica Lattiero-Casearia 27, 208227Google Scholar
Okigbo, L. M., Richardson, G. H., Brown, R. J. & Ernstrom, C. A. 1985 Casein composition of cow's milk of different chymosin coagulation properties. Journal of Dairy Science 68 18871892CrossRefGoogle Scholar
Pearse, M. J., Linklater, P. M., Hall, R. J. & Mackinlay, A. G. 1985 Effect of heat induced interaction between β-lactoglobulin and κ-casein on syneresis. Journal of Dairy Research 52 159165CrossRefGoogle Scholar
Pearse, M. J., Linklater, P. M., Hall, R. J. & Mackinlay, A. G. 1986 Effect of casein micelle composition and casein dephosphorylation on coagulation and syneresis. Journal of Dairy Research 53 381390CrossRefGoogle Scholar
Pearse, M. J., Mackinlay, A. G., Hall, R. J. & Linklater, P. M. 1984 A microassay for the syneresis of cheese curd. Journal of Dairy Research 51 131139CrossRefGoogle Scholar
Schaar, J. 1984 Effects of κ-casein genetic variants and lactation number on the renneting properties of individual milks. Journal of Dairy Research 51 397406CrossRefGoogle Scholar
Schaar, J., Hansson, B. & Pettersson, H.-E. 1985 Effects of genetic variants of κ-casein and β-lactoglobulin on cheesemaking. Journal of Dairy Research 52 429437CrossRefGoogle Scholar
Schmidt, D. G., Koops, J. & Westerbeek, D. 1977 Properties of artificial casein micelles. 1. Preparation, size distribution and composition. Netherlands Milk and Dairy Journal 31, 328341Google Scholar
Storry, J. E., Grandison, A. S., Millard, D., Owen, A. J. & Ford, G. D. 1983 Chemical composition and coagulating properties of renneted milks from different breeds and species of ruminant. Journal of Dairy Research 50 215229CrossRefGoogle Scholar
Tamime, A. Y. & Deeth, H. C. 1980 Yogurt: technology and biochemistry. Journal of Food Protection 43 939977CrossRefGoogle ScholarPubMed
Wheelock, J. V. & Kirk, A. 1974 The role of β-lactoglobulin in the primary phase of rennin action on heated casein micelles and heated milk. Journal of Dairy Research 41 367372CrossRefGoogle ScholarPubMed