JDS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Journal of Dairy Science Vol. 65 No. 12 2308-2316
© 1982 by American Dairy Science Association ®
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by DeFeo, A. A.
Right arrow Articles by Kilara, A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by DeFeo, A. A.
Right arrow Articles by Kilara, A.

Purification and Partial Characterization of Caprine Milk Lipoprotein Lipase1

A. A. DeFeo, P. S. Dimick and A. Kilara

Department of Food Science, The Pennsylvania State University, University Park 16802

ABSTRACT

Lipoprotein lipases of caprine and bovine milks were isolated, purified, and partially characterized from raw whole milk. Fractions with enzyme activity were two for caprine and one for bovine lipase. The milk lipoprotein lipase enzyme fractions were purified further by hydroxylapatite and intervent dilution chromatography. Caprine enzyme fractions were purified 142,000 and 87,000-fold from the isolates compared to the bovine enzyme, which was purified 5500-fold. For the two caprine enzyme fractions were three distinct electrophoretic bands of molecular weights 66,100; 58,900; and 55,000. Electrophoretic patterns of the two fractions were similar. Isoelectric focusing of the highly purified caprine fractions also revealed heterogeneity with minor differences in isoelectric points, pH 5.02 and 5.14. Bovine enzyme had two distinct electrophoretic bands with molecular weights of 74,100 and 66,100, but poly aery lamide gel electrophoresis in the absence of sodium dodecylsulfate or ß-mercaptoethanol revealed only one major band indicating a quaternary structure. The pH optimum of the caprine milk lipoprotein lipase was 8.7 compared to bovine enzyme of 8.5. Increase of yield of enzyme from both species during purification was attributed to several factors, the most important being the removal of an inhibitor. If in milk, this inhibitor may play a role in susceptibility of milk to hydrolytic rancidity.

FOOTNOTES

1 Paper No. 6397 in Journal Series of the Pennsylvania Agricultural Experiment Station.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1982 by the American Dairy Science Association ®.