Ed. Bastian et al., INHIBITION OF PLASMIN BY BETA-LACTOGLOBULIN USING CASEIN AND A SYNTHETIC SUBSTRATE, Journal of dairy science, 76(11), 1993, pp. 3354-3361
Bovine plasmin (EC 3.4.21.7) activity was measured on H-D-valyl-L-leuc
yl-L-lysyl-4-nitroanilide and acid casein in the presence of native an
d heat-denatured beta-lactoglobulin (denatured at 100 degrees C for 15
min before being mixed with plasmin solutions). Native or denatured b
eta-lactoglobulin was then heated with plasmin at 60 degrees C for 15
min. Enzyme activity again was estimated after this mild heat treatmen
t. Native and denatured beta-lactoglobulin inhibited the action of pla
smin on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide and casein. The mild
heat treatment (60 degrees C for 15 min) caused stronger inhibition o
f the activity of plasmin against casein and the synthetic substrate.
For H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide, inhibition was competit
ive in unheated mixtures, but heating beta-lactoglobulin with plasmin
changed inhibition type to mixed. This change suggests a heat-dependen
t interaction between plasmin and beta-lactoglobulin. Native beta-lact
oglobulin was more inhibitory of plasmin's action against casein than
was denatured beta-lactoglobulin. The converse was observed when plasm
in activity was measured with the synthetic substrate.