Properties of milk-clotting enzyme from Aspergillus versicolor and isolation of rennin-like enzyme

摘要: Abstract Some properties of the crude milk-clotting enzyme produced by Aspergillus versicolor in surface culture were studied. The action was optimal at pH 6 and 45°C. Addition increasing amounts calcium chloride constant level skim milk enhanced milk-clotting. possessed a high activity/proteolytic activity ratio compared well to calf rennin. Electrophoresis 0·01 m acetate buffer 3·42 separated into three protein components. Two components showed only proteolytic while third component feeble action. That rennin-like fraction, which 2·8-fold purification. fraction activated 5-fold treatment with either maleic or iodoacetic acid. It partially inhibited reduced glutathione parachloromercuribenzoate, completely iodine potassium cyanide.