Influence of residual milk-clotting enzyme in alpha s1 casein hydrolysis during ripening of Reggianito Argentino cheese

ERICA HYNES; LUCIANA APARO; MARIO CANDIOTI

JOURNAL OF DAIRY SCIENCE

ADSA (American Dairy Science Associacion)

Año: 2004 vol. 87 p. 565 - 573

0022-0302

Milk-clotting enzyme is considered largely denatured after the cooking step in hard cheeses. Nevertheless, typical hydrolysis products derived from rennet action on ás1-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 ás1-casein hydrolysis in Reggianito cheeses. For that purpose, we studied the influence of cooking temperature (45, 52, and 60°C) on milk-clotting enzyme residual activity and ás1-casein hydrolysis during ripening. Milk-clotting enzyme residual activity in cheeses was assessed using a chromatographic method, and the hydrolysis of ás1-casein was determined by electrophoresis and high performance liquid chromatography. Milk-clotting enzyme activity was very low or undetectable in 60°C- and 52°C-cooked cheeses at the beginning of the ripening, but it increased afterwards, particularly in 52°C-cooked cheeses. Cheese curds that were cooked at 45°C had higher initial milk clotting activity, but also in this case, there was a later increase. Hydrolysis of ás1-casein was detected early in cheeses made at 45°C, and later in those made at higher temperatures. The peptide ás1-I was not detected in 60°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 ás1-casein in hard cheeses may be at least, partially due to this proteolytic agent. ás1-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 ás1-casein hydrolysis in Reggianito cheeses. For that purpose, we studied the influence of cooking temperature (45, 52, and 60°C) on milk-clotting enzyme residual activity and ás1-casein hydrolysis during ripening. Milk-clotting enzyme residual activity in cheeses was assessed using a chromatographic method, and the hydrolysis of ás1-casein was determined by electrophoresis and high performance liquid chromatography. Milk-clotting enzyme activity was very low or undetectable in 60°C- and 52°C-cooked cheeses at the beginning of the ripening, but it increased afterwards, particularly in 52°C-cooked cheeses. Cheese curds that were cooked at 45°C had higher initial milk clotting activity, but also in this case, there was a later increase. Hydrolysis of ás1-casein was detected early in cheeses made at 45°C, and later in those made at higher temperatures. The peptide ás1-I was not detected in 60°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 ás1-casein in hard cheeses may be at least, partially due to this proteolytic agent.