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Appl Environ Microbiol. 1973 February; 25(2): 163-168
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

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

Food Research Institute, University of Wisconsin, Madison, Wisconsin 53706
Department of Food Science, University of Wisconsin, Madison, Wisconsin 53706

ABSTRACT

The production of a rennin-like enzyme by Byssochlamys 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)₂SO₄ precipitation, diethylaminoethyl-cellulose chromatography and Sephadex G-100 gel filtration. The partially purified enzyme has a pH optimum at 2.9 and a temperature optimum around 60 C. The enzyme appeared to be relatively stable at 40 C between pH 3.0 and pH 6.85. A name, byssochlamyopeptidase A, was proposed for this new enzyme. The milk-clotting activity of byssochlamyo-peptidase A is dependent on pH and appeared to be minimal at pH 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.