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Journal of Dairy Science Vol. 76 No. 11 3354-3361
© 1993 by American Dairy Science Association ®
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Inhibition of Plasmin by ß-Lactoglobulin Using Casein and a Synthetic Substrate

Eric D. Bastian 1, Karlo G. Hansen 1, and Rodney J. Brown 1

1 Department of Nutrition and Food Sciences, Utah State University, Logan 84322-8700

Bovine plasmin (EC 3.4.21.7) activity was measured on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide and acid casein in the presence of native and heat-denatured ß-lactoglobulin (denatured at 100°C for 15 min before being mixed with plasmin solutions). Native or denatured ß-lactoglobulin was then heated with plasmin at 60°C for 15 min. Enzyme activity again was estimated after this mild heat treatment. Native and denatured ß-lactoglobulin inhibited the action of plasmin on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide and casein. The mild heat treatment (60°C for 15 min) caused stronger inhibition of the activity of plasmin against casein and the synthetic substrate. For H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide, inhibition was competitive in unheated mixtures, but heating ß-lactoglobulin with plasmin changed inhibition type to mixed. This change suggests a heat-dependent interaction between plasmin and ß-lactoglobulin. Native ß-lactoglobulin was more inhibitory of plasmin's action against casein than was denatured ß-lactoglobulin. The converse was observed when plasmin activity was measured with the synthetic substrate.

Key Words: plasmin • ßbeta;lactoglobulin • inhibition

Submitted on August 24, 1992
Accepted on May 19, 1993




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