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The production of a rennin-like enzyme byByssochlamys fulva varied considerably with the isolates tested. Among the seven isolates tested, NRRL 2260, IMI 83277, and N.Y. 1 were good enzyme producers. The enzyme produced by isolate IMI 83277 was purified approximately 20-fold after (NH4 )2 SO4 precipitation, diethylaminoethyl-cellulose chromatography and Sephadex G-100 gel filtration. The partially purified enzyme has ap H optimum at 2.9 and a temperature optimum around 60 C. The enzyme appeared to be relatively stable at 40 C betweenp H 3.0 andp H 6.85. A name, byssochlamyopeptidase A, was proposed for this new enzyme. The milk-clotting activity of byssochlamyo-peptidase A is dependent onp H and appeared to be minimal atp H 6.2 or above. No extensive proteolysis has been observed during the milk-clotting process. The non-trichloroacetic acid-precipitable nitrogen titration curve on skim milk was comparable to that catalyzed by animal rennet.

Byssochlamyopeptidase A, a Rennin-like Enzyme Produced by Byssochlamys fulva