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Bovine milk procathepsin D and cathepsin D: coagulation and milk protein degradation

Published online by Cambridge University Press:  01 June 2009

Lotte B. Larsen ,
Connie Benfeldt ,
Lone K. Rasmussen  and
Torben E. Petersen
Lotte B. Larsen
Affiliation:
Protein Chemistry Laboratory, University of Aarhus, Science Park, DK-8000 Aarhus C, Denmark
Connie Benfeldt
Affiliation:
MD Foods Research and Development Centre, Rørdrumvej 2, DK-8220 Brabrand, Denmark
Lone K. Rasmussen
Affiliation:
Protein Chemistry Laboratory, University of Aarhus, Science Park, DK-8000 Aarhus C, Denmark
Torben E. Petersen
Affiliation:
Protein Chemistry Laboratory, University of Aarhus, Science Park, DK-8000 Aarhus C, Denmark
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Summary

Cathepsin D is an indigenous aspartic proteinase in bovine milk. By competitive enzyme-linked immunosorbent assay the amount of immunoreactive cathepsin D and procathepsin D in bovine skim milk was estimated to be 0·4 μg/ml. Immunoreactive cathepsin D purified from whey consisted of a small fraction of mature cathepsin D, but the major form was the proenzyme procathepsin D. A preparation of bovine milk procathepsin D was, like mature cathepsin D, able to degrade purified αs1-, αs2-, β- and κ-casein and α-lactalbumin, while β-lactoglobulin was resistant to cleavage. The cleavage sites in these proteins were determined and compared with those of chymosin. Cathepsin D was capable of generating the αs1-I, β-I, β-II and β-III fragments originally described from the action of chymosin on the respective caseins, and these fragments were subjected to further proteolysis. Cathepsin D was also able to liberate the caseinomacropeptide from purified κ-casein, and to coagulate bovine skim milk. This demonstrated that milk contains an indigenous coagulation enzyme present mainly in the whey fraction.

Type
Original Articles
Information
Journal of Dairy Research , Volume 63 , Issue 1 , February 1996 , pp. 119 - 130
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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