SUMMARYOf 48 fungal isolates, 28 (including one Penicillium and three Aspergilli) secreted milk-clotting enzymes. This activity was in general related to the mycelial growth of a given isolate, but not with pH change of the culture filtrate during incubation. It was not found when mucilage was formed by isolates capable of doing so. The ratio of general proteolytic activity to milk-clotting activity varied from one organism to another, and with the age of culture of the same fungal strain.
In a previous paper, Abdel-Fattah et al.1) reported on the production of milk-clotting and proteolytic enzymes by fungi. The latter authors found that Penicilliwn expansum was the potent organism for producing the most active milk-clotting rennin-like enzyme. We now report on the purification and the properties of this fungal enzyme.
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