Action of milk-clotting enzymes on beta-caseins from buffalo's and cow's milk.
beta-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 beta-casein was determined quantitatively after various times. The electrophoretic patterns of the degradation products of buffalo and bovine beta-casein produced by the different enzymes were not identical. beta-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 beta-casein was found to retard its proteolysis by all the enzymes but particularly by rennet and M. miehei protease.
D000818:Animals; D002020:Buffaloes; D002364:Caseins / Q000031:analogs & derivatives / Q000378:metabolism*; D002417:Cattle; D012085:Chymosin / Q000378:metabolism*; D005260:Female; D006868:Hydrolysis; D008892:Milk; D009089:Mucor / Q000201:enzymology; D010447:Peptide Hydrolases / Q000378:metabolism*; D013045:Species Specificity; D013098:Xylariales / Q000201:enzymology
D002364:Caseins; D010447:Peptide Hydrolases; D012085:Chymosin