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Sheehan, JJ,Oliveira, JC,Kelly, AL,Mc Sweeney, PLH;
2007
July
International Dairy Journal
Effect of cook temperature on primary proteolysis and predicted residual chymosin activity of a semi-hard cheese manufactured using thermophilic cultures
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semi-hard cheese cook temperature primary proteolysis predicted residual chymosin activity MILK-CLOTTING ENZYMES SWISS-TYPE CHEESE CHEDDAR CHEESE BOVINE-MILK THERMAL INACTIVATION CATHEPSIN-D ALKALINE PROTEINASE ACID PROTEASE CASEIN PLASMIN
17
826
834
Novel semi-hard cheeses were manufactured using Streptococcus thermophilus and Lactobacillus helveticus as starter cultures and with cook temperatures of 47, 50 or 53 degrees C. There was a progressive and significant degradation of both alpha(s1)- and beta-caseins during ripening of all cheeses. Increasing cook temperature significantly reduced degradation of alpha(s1)-casein during ripening, in the order 53<50<47 degrees C, as measured by densitometric analysis of urea-polyacrylamide gel electrophoresis (urea-PAGE) electrophoretograms. Mean levels of primary proteolysis, as measured by amounts of pH 4.6-soluble N, were also significantly reduced. A mathematical model, incorporating changes in pH and temperature during manufacture of the cheeses, predicted near to total inactivation of residual chymosin as a result of the cooking profiles used in cheesemaking. Increasing cook temperature did not completely inhibit primary proteolysis or hydrolysis of alpha(s1)-casein to alpha(s1)-casein (f24-199) during ripening, although these reactions were slowed. (c) 2006 Elsevier Ltd. All rights reserved.
DOI 10.1016/j.idairyj.2006.08.012
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