Abstract
A lytic enzyme was isolated from the lysate of Ps. aeruginosa infected with a new strain of bacteriophage, phage 95. The enzyme, LE95, was purified by chromatography in twice on IRC50 column and by gel filtration in twice on Sephadex G-75 column. The molecular weight was estimated as 21, 000. The optimal condition for the hydrolysis of acetone-dried cells of Ps. aeruginosa was determined to be following: the optimal pH was between 6.5 and 7.0, the temperature about 70°C and the concentration of phosphate buffer about 5mM. The enzyme was strongly inhibited by Ag+, Hg2+, Ni2, Fe2+ and Cu2+ ions. When peptideglycan obtained from Ps. aeruginosa was digested by LE95, free amino groups were liberated without release of reducing sugars. The enzyme was suggested to be amidase or peptidase.
