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Heat stability of the plasmin system in milk and casein systems



Heat stability of the plasmin system in milk and casein systems



New Zealand Journal of Dairy Science & Technology 23(2): 143-152



The heat stability of the plasmin system was lower in milk than in a serum-protein-free micellar casein dispersion. When .beta.-lactoglobulin was added to the latter before heating, plasmin activity was reduced to values even lower than those found in milk, indicating that the activity of the enzyme system is reduced on heating milk due to heat denaturation and to a heat-induced interaction between the enzyme system and denatured .beta.-lactoglobulin, which inhibits plasmin/plasminogen activity. The heat stability of the plasmin system was lower in a non-micellar casein solution than in a micellar casein dispersion, suggesting that the micelle structure may protect the enzyme against denaturation. Increasing the pH from 6.0 to 9.0 decreased the heat stability of the plasmin system in micellar and non-micellar casein systems. The heat stability of isolated plasmin was increased by making the solution to 0.05 M-lysine or 0.05 M-6-aminohexanoic acid, suggesting that the binding of plasmin/plasminogen to casein micelles via lysine binding sites increases its heat stability in milk and micellar casein dispersions.

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