Hostname: page-component-586b7cd67f-dlnhk Total loading time: 0 Render date: 2024-11-23T07:03:59.147Z Has data issue: false hasContentIssue false
  • English
  • Français

Effects of κ-casein genetic variants and lactation number on the renneting properties of individual milks

Published online by Cambridge University Press:  01 June 2009

Johan Schaar
Johan Schaar
Affiliation:
Department of Animal Breeding and Genetics, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden
Get access Rights & Permissions [Opens in a new window]

Summary

The effects of κ-casein genetic variants, lactation number, pH and casein content on the renneting properties of individual milks were studied. Rennet coagulation time (RCT) and curd firmness were determined with the aid of a lactodynamograph and the results statistically analysed. Renneting properties were strongly related to κ-casein variants and lactation number, with κ-casein B and higher lactation numbers giving shorter RCT and increased curd firmness, the effects on curd firmness being more pronounced. The effect of κ-casein variant on RCT could be eliminated by reducing pH and adding CaCl2 to the milk samples. The effect on curd firmness was not altered by this treatment, however. The results show that the renneting properties of individual milks are to a considerable degree genetically controlled.

Type
Original Articles
Information
Journal of Dairy Research , Volume 51 , Issue 3 , August 1984 , pp. 397 - 406
Copyright
Copyright © Proprietors of Journal of Dairy Research 1984

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

Andrén, A., Björck, L. & Clabssok, O. 1980 Quantification of chymosin (rennin) and pepsin in bovine abomasa by rocket immunoelectrophoresis. Swedish Journal of Agricultural Research 10 123–130Google Scholar
Aschaffenburg, R. & Drewry, J. 1955 Occurrence of different beta-lactoglobulins in cow's milk. Nature 176 218–219CrossRefGoogle ScholarPubMed
Berglund, B., Brännäng, E., Henningsson, T., Janson, L., Josefsson, G., Lindkvist, G., Magnusson, B.,Philipsson, J. & Swensson, C. 1980 Comprehensive experiments on traits affecting longevity in Swedish dairy cattle breeds. I. Experimental design and general description of the experiment. Swedish Journal of Agricultural Research 10 159–166Google Scholar
Corhadini, C. & Bergamaschi, E. 1974 [Effect of genetic variants on casein behaviour in enzymic process]. Scienza e Tecnica Lattiero-casearia 25 202–213Google Scholar
Dalgleish, D. G. 1983 Coagulation of renneted bovine casein micelles: dependence on temperature, calcium ion concentration and ionic strength. Journal of Dairy Research 50 331–340CrossRefGoogle Scholar
El-Negoumy, A. M. 1971 Effect of αs1-, β- and κ-casein polymorphs on the stability of calcium caseinate micelles in model systems. Journal of Dairy Science 54 1567–1574CrossRefGoogle Scholar
El-Negoumy, A. M. 1972 Effect of polymorphic composition of calcium caseinate sols on their stability to rennin. Journal of Dairy Research 39 373–379CrossRefGoogle Scholar
El-Negoumy, A. M. 1974 Effect of polymorphism on casein stability in salt solutions of varying complexity before and after freezing. Journal of Dairy Science 57 1170–1176CrossRefGoogle Scholar
Falconer, D. S. 1981 Introduction to Quantitative Genetics, 2nd edn, p. 127. London: LongmanGoogle Scholar
Feagan, J. T., Bailey, L. F., Hehir, A. F., Mclean, D. M. & Ellis, N. J. S. 1972 Coagulation of milk proteins. I. Effect of genetic variants of milk proteins on rennet coagulation and heat stability of normal milk. Australian Journal of Dairy Technology 27 129–134Google Scholar
Forar, F. L., Kincaid, R. L., Preston, R. L. & Hillers, J. K. 1982 Variation of inorganic phosphorus in blood plasma and milk of lactating cows. Journal of Dairy Science 65 760–763CrossRefGoogle ScholarPubMed
Gahne, B., Juneja, R. K. & Grolmus, J. 1977 Horizontal polyacrylamide gradient gel electrophoresis for the simultaneous phenotyping of transferrin, post-transferrin, albumin and post-albumin in the blood plasma of cattle. Animal Blood Groups and Biochemical Genetics 8 127–137CrossRefGoogle ScholarPubMed
Helwig, J. T. & Council, K. A. 1979 SAS Users' Guide. Raleigh, NC: SAS Institute Inc.Google Scholar
Hill, R. D. 1970 The effect of the modification of arginine side chains in casein on the coagulation of rennin-altered casein. Journal of Dairy Research 37 187–192CrossRefGoogle Scholar
Kirchmeier, O., Mehana, A., Graml, R. & Buchberger, J. 1982 Influence of casein genotypes on the water binding capacity and the heat stability of casein. 21st International Dairy Congress, Moscow 1 (1) p. 195Google Scholar
Mclean, D. M. 1981 Bovine milk proteins: their determination, and associations between milk protein genotypes and milk yield and composition. Thesis. University of Adelaide, South AustraliaGoogle Scholar
Mclean, D. M., Graham, E. R. B., Ponzoni, R. W. & Mckenzie, H. A. 1982 Heat stability of preheated concentrated skim milk from individual cows: association with milk protein genotype and composition. 2nd Australian Dairy Technology Review Conference, Glenormiston pp. 190–191Google Scholar
Mariani, P., Losi, G., Morini, D. & Castagnetti, G. B. 1979 [Citric acid content in the milk of cows with different genotypes in the κ-casein locus.] Scienza e Tecnica Lattiero-casearia 30 375–384Google 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 27 208–227Google Scholar
Morini, D., Losi, G., Castagnetti, G. B., Benevelli, M., Resmini, P. & Volonterio, G. 1975 [The influence of genetic variants of κ-casein on the size of casein micelles.] Scienza e Tecnica Lattiero-casearia 26 437–444Google Scholar
Morini, D., Losi, G., Castagnetti, G. B. & Mariani, P. 1979 [Properties of ripened cheese in cheesemaking experiments with milk characterized by κ-casein variants A and B.] Scienza e Tecnica Lattiero-casearia 30 243–262Google Scholar
Oltner, R. & Berglund, B. 1983 Leukocytes, packed cell volume, glucose, urea, calcium, inorganic phosphorus and magnesium in the blood of dairy cows. Zentralblatt für Veterinärmedizin 30 530–531CrossRefGoogle ScholarPubMed
Sadler, A. M., Kiddy, C. A., Mccann, R. E. & Mattingly, W. A. 1968 Acid production and curd toughness in milks of different αs1,-casein types. Journal of Dairy Science 51 28–30CrossRefGoogle Scholar
Sjaunja, L. -O. & Schaar, J. 1984 Determination of casein in milk by infrared spectrophotometry. Milchwissenschaft (in press)Google Scholar
Thompson, M. P. & Farrell, H. M. 1974 Genetic variants of the milk proteins. In Lactation, a Comprehensive Treatise vol. III, pp. 109–134 (Eds Larson, B. H. & Smith, V. R.) New York: Academic PressGoogle Scholar