Comparing Proteolytic Action of Milk-Clotting Enzymes on Caseins and Cheese

The proteotytie properties of fungal rennets from Endothia parasitica and from Mucor pusillus var. Lindt were compared with those of veal rennet and of pepsin. Enzyme proteolysis of whole, as-, and flcasein, soluble in 12% trichloroacetic acid and soluble nitrogen compounds produced by enzymes on freshly ground mild cheese curd were determined. Residual fractions from the action of the enzymes on the casein substrates and on cheese were determined by polyacrylamide-gel electrophoresis.