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Journal of Dairy Science Vol. 59 No. 3 369-375
© 1976 by American Dairy Science Association ®
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Bovine Pacreatic Lipase1. I. Isolation, Homogeneity, and Characterization

K. M. Shahani, I. M. Khan2 and R. C. Chandan3

Department of Food Science and Technology, University of Nebraska, Lincoln 68503

ABSTRACT

Bovine pancreatic lipase was isolated in a pure form by lyophilization of fresh bovine pancreas, extraction of the enzyme with sucrose solution, fractional precipitation with ammonium sulfate and acetone, followed by chromatography on Sephadex G-100. The specific activity of the purest lipase fraction was 1750 micro-moles fatty acid, liberated in 30 min per milligram of protein, indicating a purification of approximately 473-fold, with an overall yield of about 42%. Homogeneity of the enzyme was confirmed by re-chromatography on Sephadex G-100 as well as with the gel electrophoretic and ultracentrifugal techniques. The purified enzyme gave a typical protein ultraviolet absorption spectrum with maximum absorption at 276 nm and minimum at 252 nm. The purified enzyme exhibited a single pH optimum of 8.8 and an isoelectric point near pH 5.5. Its optimum temperature was 37 C, and its optimum substrate concentration was 10%. These properties resembled those of milk lipase.

FOOTNOTES

1 Published with the approval of the Director as paper No. 3902, Journal Series, Agricultural Experiment Station, Lincoln, NE. Research work was conducted on Project 16-17. This study was supported in part by grants from American Dairy Association and Dairy Research, Inc. (DRINC).

2 The Cary Memorial Hospital, 33 Lyndon Street, Caribou, ME 04736.

3 Purity Cheese Company, Mayville, WI 53050.






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Copyright © 1976 by the American Dairy Science Association ®.