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We studied the influence of the dose of milk-clotting enzyme on alphas1-CN degradation, soluble nitrogen production, and sensory profile for an Argentinean soft cheese: Cremoso Argentino. Five different types of cheeses were produced: 1) control cheeses with normal technology, 2) cheeses with inactivated milk-clotting enzyme, 3) cheeses with inactivated milk-clotting enzyme, without starter (acidified with glucono delta lactone), 4) cheeses with a half dose of milk-clotting enzyme, and 5) cheeses with a double dose of milk-clotting enzyme. Proteolysis was assessed by isoelectric focusing electrophoresis of the insoluble fraction at pH 4.6, followed by densitometric quantification. Soluble nitrogen at pH 4.6, expressed as a percentage of total nitrogen and defined as ripening index was also performed. A sensorial panel evaluated the cheeses at the end of ripening. The hydrolysis level of alphas1-CN depended on the milk-clotting enzyme dose used in cheese making. Cheeses without active coagulant did not show degradation at the end of ripening, while cheeses with half and whole doses showed proportional degradations to coagulant dose. Cheese with a double dose of coagulant did not show higher alphas1-CN hydrolysis than normal cheese. No difference was found between cheeses with and without microbiological starter, indicating that the selected culture, composed of thermophilic strains, was unable to attack the whole casein. A high linear correlation was found between ripening index and the relation Sensorial characteristics of cheeses agree with objective analysis. Cheeses without active coagulant were hard and crumbly, while cheeses with normal dose were soft and creamy.

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Milk-clotting enzyme is considered largely denatured after the cooking step in hard cheeses. Nevertheless, typical hydrolysis products derived from rennet action on alpha(s1)-casein have been detected during the ripening of hard cheeses. The aim of the present work was to investigate the influence of residual milk-clotting enzyme on alpha(s1)-casein hydrolysis in Reggianito cheeses. For that purpose, we studied the influence of cooking temperature (45, 52, and 60 degrees C) on milk-clotting enzyme residual activity and alpha(s1)-casein hydrolysis during ripening. Milk-clotting enzyme residual activity in cheeses was assessed using a chromatographic method, and the hydrolysis of alpha(s1)-casein was determined by electrophoresis and high performance liquid chromatography. Milk-clotting enzyme activity was very low or undetectable in 60 degrees C- and 52 degrees C-cooked cheeses at the beginning of the ripening, but it increased afterwards, particularly in 52 degrees C-cooked cheeses. Cheese curds that were cooked at 45 degrees C had higher initial milk clotting activity, but also in this case, there was a later increase. Hydrolysis of alpha(s1)-casein was detected early in cheeses made at 45 degrees C, and later in those made at higher temperatures. The peptide alpha(s1)-I was not detected in 60 degrees C-cooked cheeses. The results suggest that residual milk-clotting enzyme can contribute to proteolysis during ripening of hard cheeses, because it probably renatures partially after the cooking step. Consequently, the production of peptides derived from alpha(s1)-casein in hard cheeses may be at least, partially due to this proteolytic agent.