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Casein compositional studies. III. Changes in Irish milk for manufacturing and role of milk proteinase

Published online by Cambridge University Press:  01 June 2009

William J. Donnelly
Affiliation:
The Agricultural Institute, Moorepark Research Centre, Fermoy, Co. Cork, Irish Republic
J. Gerard Barry
Affiliation:
The Agricultural Institute, Moorepark Research Centre, Fermoy, Co. Cork, Irish Republic

Summary

The composition of casein in Irish milk for manufacturing was examined throughout the year. Large changes in composition were observed in the final quarter of the year as a result of the influence of late lactation when the proportion of αs- and β-caseins declined and the proportion of κ- and γ-caseins and of minor casein components increased. Similar changes in casein composition were induced by treatment of milk with porcine plasmin. The activity of plasmin-like milk proteinase in milk was quantified from the rate of conversion of added [14C]β-casein to [14C]γ-caseins. This activity was considerably higher in a late lactation milk than in a mid lactation milk and was ∼ 20 times higher at 37 °C than at 4 °C. It was concluded that casein compositional changes in late lactation were largely the result of proteolysis of individual caseins by plasmin-like milk proteinase.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1983

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References

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