Lysosubtilin G10x, a lytic enzyme from Bacillus subtilis SK-52 was studied with respect to its physico-chemical properties such as effect of optimal conditions and stability. The maximum activity of the enzyme was observed in phosphate buffer at a concentration of the buffer mixture equal to 0.004 M, pH 7.2 and the temperature of 37-50 degrees C. Aqueous solutions of lysosubtilin G10x were stable at pH 5-9. The lytic activity of the enzyme aqueous solutions rapidly lowered at a temperature above 50 degrees C. The ions of some metals, especially those of mercury, copper and ferrous iron inhibited the enzyme. Lysis activation was recorded in the presence of surface active substances such as sodium dodecylsuphate, tritone X-100 and certain twins. Comparison of the findings with the results of our previous studies on the lytic properties of enzymes from other strains of B. subtilis showed that irrespective of the strain lysosubtilins were sensitive to changes in the medium ionic strength, they were mostly active in neutral solutions of low ionic strength, their activity was inhibited by heavy metal ions and they were stable within wide ranges of pH. This should be taken into account in practical use of lysosubtilin G10x.
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