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Journal of Dairy Science Vol. 66 No. 11 2271-2277
© 1983 by American Dairy Science Association ®
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Proteinase Activity in Bovine Raw Milk

G. Humbert1, J. Brun-Bellut2, T. Mora1 and C. Alais1

Laboratoire de Biochimie Appliquée, Université De Nancy 1, B.P. 239, F. 54506 Vandoeuvre-Les-Nancy Cédex and Laboratoire de Zootechnie, E.N.S.A.I.A., 54000 — Nancy

ABSTRACT

We measured proteinase activity and such diverse characteristics as pH, nitrogenous fractions, and total and psychrotrophic microflora in 26 individual bovine milks. Activity can change considerably from one animal to another. Variations are less as a function of time for a given cow. Half (46%) of the variability of the proteinase activity may be explained by milk pH (26%), by the psychrotrophic flora (9%), and by stage of lactation (11%). The other measures and amount of lactation have no significant effect on this enzymic activity. The second half (54%) of this variability in activity could be due only to variations of the native milk proteinase system.

FOOTNOTES

1 Laboratoire de Brochimie Appliquee.

2 Laboratoire de Zootechnie.






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Copyright © 1983 by the American Dairy Science Association ®.