Relative proteolytic action of milk-clotting enzyme preparations on bovine alpha- beta and kappa-casein
1996
Ustunol, Z. | Zeckzer, T.
Concentrations of seven milk-clotting enzyme preparations were standardized to equal clot times. Portions of bovine alpha(s)-, beta- and kappa-casein were treated with enzymes. Proteolytic activity of the coagulants on each casein fraction was determined using the TNBS (2,4,6-trinitrobenzene-sulfonic acid) procedure. Recombinant chymosin showed the lowest degree of proteolysis on alpha(s)- and beta-caseins. Excessive proteolysis of calf rennet appeared to be due to the pepsin fraction. M. miehei and M. pusillus var Lindt proteases showed similar degradation of caseins, but M. pusillus var Lindt was more proteolytic when beta-casein was the substrate. C. parasitica protease showed the highest degree of proteolysis on alpha(s)- and beta-caseins but was the least proteolytic on kappa-casein.
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