Characterization of the autolytic enzymes of Clostridium perfringens.

Summary: Clostridium perfringens and isolated walls of this organism autolysed rapidly when incubated in buffer at pH 7.0 with the release of free-reducing groups but no N-terminal amino acids. The predominant autolytic enzyme was an endo-β-N-acetylglucosaminidase, and an endo-β-N-acetylmuramidase was also present. The autolytic enzymes could be solubilized by extraction of the organisms with 5 M-LiC1 and would then subsequently bind to and rapidly lyse walls of Micrococcus luteus and, more slowly, formamide-extracted walls of C. perfringens and walls of Bacillus subtilis. Lysis of C. perfringens walls by these extracted enzymes could not be demonstrated.