The epsilon-poly-L-lysine-degrading enzyme of the epsilon-poly-L-lysine-tolerant Chryseobacterium sp. OJ7 was purified and characterized. The bacterium excreted the enzyme into the culture filtrate. The purified enzyme has a molecular mass of approximately 38.4 kDa and consists of two identical subunits with a molecular mass of 19.5 kDa. The enzyme catalyzed the endo-type degradation of epsilon-poly-L-lysine. A correlation between the epsilon-poly-L-lysine tolerance of the bacterium and the high epsilon-poly-L-lysine-degrading activity was suggested.