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

  • H. B. Castberg (a1), T. Egelrud (a2), P. Solberg (a1) and T. Olivecrona (a2)

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.

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

  • H. B. Castberg (a1), T. Egelrud (a2), P. Solberg (a1) and T. Olivecrona (a2)

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