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Factors affecting the distribution of lipoprotein lipase activity between serum and casein micelles in bovine milk

Published online by Cambridge University Press:  01 June 2009

Malcolm Anderson
Malcolm Anderson
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9 AT, UK
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Summary

The influence of mastitis and early lactation, and the effect of treating milk with heparin, blood serum and trypsin, on the proportion of lipoprotein lipase (LPL) activity in milk serum was investigated. The relative importance of milk serum LPL and LPL bound to micellar casein in promoting lipolysis was also examined. Colostrum contained LPL activity, 45% of which was found in the serum phase in samples obtained from the first milking post partum, but this value fell to 34% in samples taken 24 h later. The proportion of serum LPL was also increased in milks from quarters infected with Staphylococcus aureus, but not after overnight treatment of normal milk at 4 °C with 5% (w/v) blood serum or 2 µg/ml trypsin. The addition of 5 µg/ml heparin resulted in a consistent increase in serum LPL which varied between 14 and 50% of total milk LPL. Heparin did not release all the enzyme bound to casein micelles even after a second heparin treatment of resuspended micelles. Serum LPL was more effective in promoting lipolysis and was more responsive to blood serum activation than LPL bound to casein micelles. Lipolysis increased after heparin treatment but the increase was not related to serum LPL activity.

Type
Original Articles
Information
Journal of Dairy Research , Volume 49 , Issue 1 , February 1982 , pp. 51 - 59
Copyright
Copyright © Proprietors of Journal of Dairy Research 1982

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References

REFERENCES

Anderson, M. 1977 Source and significance of lysosomal enzymes in bovine milk fat globule membrane. Journal of Dairy Science 60 1217–1222CrossRefGoogle Scholar
Anderson, M. 1981 Inhibition of lipolysis in bovine milk by proteose peptone. Journal of Dairy Research 48 247–252CrossRefGoogle ScholarPubMed
Anderson, M. & Andrews, A. T. 1977 Progressive changes in individual milk protein concentrations associated with high somatic cell counts. Journal of Dairy Research 44 223–235CrossRefGoogle ScholarPubMed
Brumby, P. E., Anderson, M., Storry, J. E., Cheeseman, G. C. & Hall, A. J. 1970 National Institute for Research in Dairying Report 1969–70 p. 119Google Scholar
Castberg, H. B., Egelrud, T., Solberg, P. & Olivecrona, T. 1975 Lipases in bovine milk and the relationship between the lipoprotein lipase and tributyrate hydrolysing activities in cream and skim-milk. Journal of Dairy Research 42 255–266CrossRefGoogle ScholarPubMed
Castberg, H. B. & Solberg, P. 1974 The lipoprotein lipase and the lipolysis in bovine milk. Meieriposten 63 961–975Google Scholar
Clegg, R. A. 1978 Bovine serum apo-lipoprotein effectors of milk lipoprotein lipase. Biochemical Society Transactions 6 1207–1210CrossRefGoogle ScholarPubMed
Deeth, H. C. & Fitz-GERALD, C. H. 1975 Factors governing the susceptibility of milk to spontaneous lipolysis. International Dairy Federation Annual Bulletin (Document 86) 24–34 (Proceedings of the Lipolysis Symposium Cork (Ireland) 5–7 March 1975)Google Scholar
Downey, W. K. 1974 Enzymic aspects of hydrolytic rancidity. 19th International Dairy Congress, New Delhi 1 E 351–352Google Scholar
Downey, W. K. & Andrews, P. 1966 Studies on the properties of cow's-milk tributyrinases and their interaction with milk proteins. Biochemical Journal 101 651–660CrossRefGoogle ScholarPubMed
Downey, W. K. & Murphy, R. F. 1975 Partitioning of the lipolytic enzymes in bovine milk. International Dairy Federation Annual Bulletin (Document 86) 19–23 (Proceedings of the Lipolysis Symposium Cork (Ireland) 5–7 March 1975)Google Scholar
Driessen, F. M. 1976 A comparative study of the lipase in bovine colostrum and in bovine milk. Netherlands Milk and Dairy Journal 30 186–196Google Scholar
Driessen, F. M. & Stadhouders, J. 1974 A study of spontaneous rancidity. Netherlands Milk and Dairy Journal 28 130–145Google Scholar
Egelrud, T. & Olivecrona, T. 1972 The purification of a lipoprotein lipase from bovine skim milk. Journal of Biological Chemistry 247, 6212–6217CrossRefGoogle ScholarPubMed
Fielding, C. J. & Fielding, P. E. 1976 Mechanism of salt-mediated inhibition of lipoprotein lipase. Journal of Lipid Research 17 248–256CrossRefGoogle ScholarPubMed
Hoynes, M. C. T. & Downey, W. K. 1973 Relationship of the lipase and lipoprotein lipase activities of bovine milk. Biochemical Society Transactions 1 256–259CrossRefGoogle Scholar
Tverius, P. H., Lindahl, U., Eoblrud, T. & Olivbckona, T. 1972 Effects of heparin on lipoprotein lipase from bovine milk. Journal of Biological Chemistry 247 6610–6616Google Scholar
Jellema, A. 1975 Note on susceptibility of bovine milk to lipolysis. Netherlands Milk and Dairy Journal 29 145–152Google Scholar
Jenness, R. & Koops, J. 1962 Preparation and properties of a salt solution which simulates milk ultrafiltrate. Netherlands Milk and Dairy Journal 16 153–164Google Scholar
Koops, J. & Klomp, H. 1977 Rapid colorimetric determination of free fatty acids (lipolysis) in milk by the copper soap method. Netherlands Milk and Dairy Journal 31 56–74Google Scholar
Lowry, O. H., Rosebrouoh, N. J., Farr, A. L. & Randall, R. J. 1951 Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193 265–275CrossRefGoogle ScholarPubMed
Mather, I. H. & Keenan, T. W. 1975 Studies on the structure of the milk fat globule membrane. Journal of Membrane Biology 21 65–85CrossRefGoogle ScholarPubMed
Nilsson-EHLE, P. & Schotz, M. C. 1976 A stable, radioactive substrate emulsion for assay of lipoprotein lipase. Journal of Lipid Research 17 536–541CrossRefGoogle ScholarPubMed
Olivecrona, T. 1980 Biochemical aspects of lipolysis in bovine milk. International Dairy Federation Bulletin (Document 118) 19–25Google Scholar
Pettipher, G. L., Mansell, R., Mckinnon, C. H. & Cousins, C. M. 1980 Rapid membrane filtrationepifluorescent microscopy technique for direct enumeration of bacteria in raw milk. Applied and Environmental Microbiology 39 423–429CrossRefGoogle ScholarPubMed
Salih, A. M. A. 1978 Factors affecting lipolytic activity in cow's milk. Thesis, University of Reading.Google Scholar
Salih, A. M. A. & Anderson, M. 1979 a Observations on the influence of high cell count on lipolysis in bovine milk. Journal of Dairy Research 46 453–462CrossRefGoogle ScholarPubMed
Salih, A. M. A. & Anderson, M. 1979 b Effect of diet and stage of lactation on bovine milk lipolysis. Journal of Dairy Research 46 623–631CrossRefGoogle Scholar
Sharma, K. K. & Randolph, H. E. 1974 Influence of mastitis on properties of milk. VIII. Distribution of soluble and micellar casein. Journal of Dairy Science 57 19–23CrossRefGoogle Scholar
Shipe, W. F., Senyk, G. F. & Fountain, K. B. 1980 Modified copper soap solvent extraction method for measuring free fatty acids in milk. Journal of Dairy Science 63 193–198CrossRefGoogle Scholar
Tallamy, P. T. & Randolph, H. E. 1970 Influence of mastitis on properties of milk. V. Total and free concentrations of major minerals in skimmilk. Journal of Dairy Science 53 1386–1388CrossRefGoogle ScholarPubMed