Purification and some properties of milk-clotting enzyme from Aspergillus niger
作者： H. G. OSMAN , A. F. ABDEL-FATTAH , S. S. MABROUK
DOI: 10.1099/00221287-59-1-131
关键词: Biochemistry 、 Biology 、 Chromatography 、 Enzyme 、 Milk-clotting enzyme 、 Aspergillus niger 、 Enzyme action 、 Proteolysis
摘要: SUMMARY: The electrophoretic separation of partially purified milk-clotting enzyme from Aspergillus niger no. 58 with 0.02 m-acetate buffer showed four protein components. fraction constituted the major part preparation and exhibited highest activity lowest proteolytic action. course proteolysis in first stage enzymic action was similar to that animal rennin. optimal at 50° pH 5·8.
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