Further studies on an asporogenous mutant of Bacillus subtilis lacking in vivo proteolytic activity.

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Abstract
Various properties such as pH optimum, response to metal ions and inhibitors and heat stability of 2 extracellular and 1 intracellular proteases from both parent and asporogenous strains of B. subtilis were examined, and no significant difference between the 2 strains was observed. The intracellular protease was a serine protease absolutely requiring Ca2+. In vivo degradation of the cellular protein at the stationary phase in both parent and mutant strains was examined and degradation occurred only in the parent strain. Addition of Ca2+ and toluene together to the reaction mixture of the mutant strain, resulted in significant degradation of the cellular protein in the mutant strain, although the addition of either Ca2+ or toluene alone had no stimulating effect on the degradation. Apparently, the mutant strain is defective in its transport system for Ca2+.

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