Studies on the proteinases of some anaerobic and aerobic micro-organisms

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Abstract
Anaerobic organisms, including Clostridium histolyticum, C. sporogenes, C. welchii, C. putrificum and C. botulinum, secreted proteinases which were activated by cysteine. The combination of cysteine with Fe++ gave the maximum activation. The exocellular proteinase of C. welchii hydrolysed clupein, gelatin, casein and Witte peptone. Proteinases of certain aerobic organisms, Bacillus mycoides, Staphylococcus citreus, Pseudomonas fluorescens, and Serratia marcescens, were partially inhibited by cysteine. Marked activations were effected by cysteine in combination with Fe++. The proteinase of the facultative organism, Proteus vulgaris, resembled the proteinases of the Clostridium spp. in activation behavior. Optimal action at neutrality was observed in all the investigated bacterial proteinases.