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Action of milk-clotting enzymes on β-caseins from buffalo's and cow's milk
Published online by Cambridge University Press: 01 June 2009
Summary
β-Caseins isolated from buffalo's and cow's milk were hydrolysed either with rennet or with microbial proteases from Mucor miehei, M. pusillus Lindt or Endothia parasitica. The degradation products were separated by polyacrylamide-gel electrophoresis and the residual β-casein was determined quantitatively after various times. The electrophoretic patterns of the degradation products of buffalo and bovine β-casein produced by the different enzymes were not identical. β-Casein of buffalo's milk was hydrolysed by rennet and M. miehei protease at a slower rate than that of cow's milk. The reverse was found with E. parasitica and M. pusillus Lindt proteases. Carbamylation of buffalo β-casein was found to retard its proteolysis by all the enzymes but particularly by rennet and M. miehei protease.
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- Copyright © Proprietors of Journal of Dairy Research 1976
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