PROPERTIES OF MILK-CLOTTING ENZYME FROM ASPERGILLUS-VERSICOLOR AND ISOLATION OF RENNIN-LIKE ENZYME

Some properties of the crude milk-clotting enzyme produced by Aspergillus versicolor in surface culture were studied. The enzyme action was optimal at pH 6 and 45 degree C. Addition of increasing amounts of calcium chloride at constant level of skim milk enhanced milk-clotting. The enzyme possessed a high milk-clotting activity/ proteolytic activity ratio and compared well to calf rennin. Electrophoresis in 0. 01 M acetate buffer at pH 3 multiplied by (times) 42 separated the enzyme into three protein components. Two components showed only proteolytic activity while the third component showed high milk-clotting activity and feeble proteolytic action.