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Lipases in bovine milk and the relationship between the lipoprotein lipase and tributyrate hydrolysing activities in cream and skim-milk

Published online by Cambridge University Press:  01 June 2009

H. B. Castberg ,
T. Egelrud ,
P. Solberg  and
T. Olivecrona
H. B. Castberg
Affiliation:
Dairy Research Institute, Chemistry and Bacteriology Branch, Agricultural University of Norway
T. Egelrud
Affiliation:
Department of Chemistry, Section on Physiological Chemistry, University of Umeå, Sweden
P. Solberg
Affiliation:
Dairy Research Institute, Chemistry and Bacteriology Branch, Agricultural University of Norway
T. Olivecrona
Affiliation:
Department of Chemistry, Section on Physiological Chemistry, University of Umeå, Sweden
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Summary

The lipoprotein lipase and tributyrate hydrolysing activities were found to be similarly distributed in the fractions obtained when whole milk was separated into skim-milk and cream, and when the cream was washed and freed from lipid. These enzyme activities in skim-milks and in extracts of lipid-free cream could not be separated by affinity chromatography on heparin-Sepharose. The enzymes were inactivated to the same degree when incubated at 37°C in the presence of 1·5 M-NaCl, pH 8·5, and both showed the same marked decrease in stability at 4°C in 1·5 M-NaCl, when the pH was changed from 8·3 to 9·0. Irradiation of skim-milk with UV-light caused the same decrease in both lipoprotein lipase and tributyrate hydrolysing activities. An antiserum against a highly purified skim-milk lipoprotein lipase caused total inhibition of the lipoprotein lipase and tributyrate hydrolysing activities in skim-milk and in extracts of lipid-free cream. It is suggested that in bovine milk there is only one major lipase and that it is identical to lipoprotein lipase.

Type
Research Article
Information
Journal of Dairy Research , Volume 42 , Issue 2 , June 1975 , pp. 255 - 266
Copyright
Copyright © Proprietors of Journal of Dairy Research 1975

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References

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