Abstract
Intracellular proteolytic activity was detected in cell-free extracts ofClostridium perfringens NCTC 10239 and NCTC 8798. The kinetics of protease, enterotoxin, and spore formation as well as growth of the wild type at elevated temperature and the use of sporulation mutants indicated that most protease activity was related to sporulation. Intracellular protease activity was inhibited by a mixture of tetrasodium ethylenediaminetetraacetic acid and phenylmethylsulfonyl fluoride; this indicated the presence of an alkaline serine protease and a neutral metallo-protease. Stage 0 sporulation mutants produced only metallo-sensitive proteases; this indicated that only the serine protease was sporulation-specific.
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