:II Some properties of lytic enzyme from Streptococcus mutans AL 7-1 strain

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Lytic enzyme against the strains of Streptococcus sanguis ATCC10558 and Streptococcus mutans E-49 was obtained from the supernatant of culture of Streptococcus mutans AL7-1 strain isolated from infant oral cavity, forming clear lytic zones around the colonies on an agar plate containing heated cells of Streptococcus sanguis and identified as Streptococcus mutans by its various characteristics. The crude lytic enzyme showed optimal activity at pH 6.5 and at 42°C, pH and heat stability at range 5.2 to 7.0 and up to 45°C respectively. The lytic enzyme activity was accelerated by addition of Ca2+, Mn2+, Mg2+ and Pb2+ ions, but completely inhibited by addition of Cu2+ and Hg2+ ions. The lysozyme and caseinase activities of this lytic enzyme preperation were minor. The maximum yield of lytic enzyme activity was obtained from the 24h-culture of Streptococcus mutans AL7-1 strain grown in TM meium containing 0.1% cells (wet weight) of Streptococcus mutans E-49 strain and 0.2% sucrose, and having initial pH range 7.5 to 8.0.
歯科基礎医学会の論文