@article{mbs:/content/journal/micro/10.1099/00221287-59-1-131, author = "Osman, H. G. and Abdel-Fattah, A. F. and Mabrouk, Souhair S.", title = "Purification and Some Properties of Milk-clotting Enzyme from Aspergillus niger", journal= "Microbiology", year = "1969", volume = "59", number = "1", pages = "131-135", doi = "https://doi.org/10.1099/00221287-59-1-131", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-59-1-131", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "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. The milk-clotting enzyme fraction constituted the major part of the preparation and exhibited the highest milk-clotting activity and the lowest proteolytic action. The course of proteolysis in the first stage of the enzymic action was similar to that of animal rennin. The enzyme action was optimal at 50° and pH 5.8.", }