Effects of added plasmin on the formation and rheological properties of rennet-induced skim milk gels.

Elevated plasmin enzyme activity has been suggested as a likely cause of impaired functional properties that occur in milk from cows either in their late-lactational period or that are experiencing mastitis. However, there are conflicting reports on the impact of plasmin on rennet coagulation properties of milk. The effects of added plasmin on the rheological properties, at small and large deformation, of rennet-induced gels were investigated. The microstructure of rennet-induced gels was studied, using confocal scanning laser microscopy. Porcine plasmin was added to reconstituted milk, and samples were incubated at 37 degrees C for between 0.5 to 8 h. The hydrolysis reaction was terminated using soybean trypsin inhibitor. The extent of degradation of caseins was determined with SDS-PAGE. The extent of breakdown of alpha(s)- and beta-caseins increased with incubation time with plasmin. Storage modulus of rennet gels decreased linearly with increasing degradation of caseins. There was an increase in the loss tangent parameter of the gels with increasing casein degradation, indicating a more liquid-like gel character. Gelation time decreased until approximately 3 h of incubation with plasmin (when the amounts of intact alpha(s)- and beta-caseins were approximately 46 and 50%, respectively); thereafter, gelation time increased considerably. Yield stress of rennet-induced gels decreased with increasing casein breakdown. When the level of casein hydrolysis was high (<40% of intact caseins), the microstructure of rennet-induced gels was drastically altered. Even when there were low levels of casein hydrolysis, the rheological properties of rennet gels were altered, which could have negative impacts on cheese yield and texture.