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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

Safinaz El-Shibiny  and
M. H. Abd El-Salam
Safinaz El-Shibiny
Affiliation:
Laboratory of Food Technology and Dairying, National Research Centre, Cairo, Egypt
M. H. Abd El-Salam
Affiliation:
Laboratory of Food Technology and Dairying, National Research Centre, Cairo, Egypt
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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.

Type
Original Articles
Information
Journal of Dairy Research , Volume 43 , Issue 3 , October 1976 , pp. 443 - 448
Copyright
Copyright © Proprietors of Journal of Dairy Research 1976

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