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Journal of Dairy Science Vol. 74 No. 3 764-771
© 1991 by American Dairy Science Association ®
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Isolation and Partial Characterization of a Native Serine-Type Protease Inhibitor from Bovine Milk

B. A. Weber 1 and S. S. Nielsen 1

1 Department of Food Science, Purdue University, West Lafayette, IN 47907

Purification of a native serine-type protease inhibitor from raw bovine milk resulted in the isolation of an inhibitor tentatively identified as alphal-antitrypsin. Techniques utilized included ammonium sulfate fractionation followed by metal chelate, hydrophobic interaction, and gel filtration chromatography. Inhibitory activity during the isolation procedure was monitored using benzoyl-DL-arginine-p-nitroanilide. Molecular weight range of the isolated inhibitor (56,000 to 64,000 kDa) was comparable with that of human serum alpha1-antitrypsin (60,000 kDa). The pH optima were 6.0 and 7.5. The isolated inhibitor was active against trypsin and elastase, but activity against plasmin was not detectable. The inhibitor was a glycoprotein and formed an SDS staple complex with elastase.

Key Words: milk • milk protease inhibitor • serine protease inhibitor

Submitted on May 17, 1990
Accepted on October 22, 1990




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Copyright © 1991 by the American Dairy Science Association ®.