
doi: 10.1271/bbb.58.440
Screening tests for aspartic proteinases with milk-clotting activity were done on basidiomycetes. Crude enzymes from 6 strains had a high ratio of milk-clotting activity to caseinolytic activity. These enzymes showed acidic pH optimum for proteolytic activity and were inhibited considerably by pepstatin, a specific aspartic proteinase inhibitor. Among them, the crude enzyme from Laetiporus sulphureus was more heat-labile than the other enzymes.
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