Abstract
The quantity of released and cell‐bound hyaluronidase and aminopeptidase was determined in cultures of Streptococcus mitis grown under controlled conditions of pH, anaerobiosis, stirring and temperature. The results indicated that the formation of hyaluronidase was completely repressed during exponential growth in the presence of glucose. Synthesis of hyaluronidase occurred after the exhaustion of glucose during an autolytic phase. Aminopeptidase activity of the cells increased both in the presence of glucose and in the autolytic phase. Both enzymes were released into the medium by an autolytic process. Controlled autolysis is suggested as a physiologically useful release mechanism for intracellular enzymes directed at high molecular weight substrates which are unable to pass through the cytoplasmic membrane. Neither selective release of hyaluronidase from intact cells nor extracellular activity could be demonstrated.

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