The polysaccharide component of the bacteriolytic enzymatic complex "lysoamidase" (M(r) 1300 kDa) has been found to contain negatively charged ionic groups and can electrostatically interact with some enzymes within the complex. At pH 8.0 optimal for bacterial lysis, such interaction promotes the stabilization of bacteriolytic enzymes, increasing their half-inactivation temperature by 8 degrees and their stability upon storage by 40%. The polysaccharide decreases the thermal stability of phosphatase but has no stabilizing effect on the metalloprotease.