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-Casein
1 Department of Nutrition and Food Sciences, Utah State University, Logan 84322-8700
Proteolytic activity of some milk-clotting enzymes [calf rennet (chymosin), Mucor miehei rennet, and Cryphonectria parasitica rennet] on
-casein was determined with reverse-phase HPLC. All enzymes were standardized to the same milk-clotting activity and incubated with
-casein at 37°C for 1, 5, 15, 30, and 60 min. Protein hydrolysis was stopped by addition of 105 M pepstatin in 8 M urea. Chromatograms of hydrolysis products revealed that the enzymes hydrolyzed
-casein differently. Chymosin hydrolysis was limited to formation of
-macropeptide and para-
-casein; the microbial rennets, particularly that from M. miehei, effected extensive nonspecific hydrolysis of both
-casein and para-
-casein.
Key Words:
-casein milk-clotting enzymes milk coagulation
Submitted on January 8, 1991
Accepted on January 27, 1992
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