Purification and characterization of enzyme property of a cell-wall lytic enzyme against Lactobacillus plantarum were carried out. Final specific activity of purified enzyme was 5.8 units/mg and purity of the enzyme was increased 8.3 fold compared with the enzyme activity in culture broth. The molecular weight of purified enzyme was estimated to be 60,000 kDa by gel filtration and SDS-polyacrylamide gel electrophoresis. Optimal pH and temperature for the activity of this enzyme were 3.0 and 4$0^{circ}C$, respectively. The cell-wall lytic enzyme activity was maintained at 3$0^{circ}C$ when treating the enzyme for 30 mins, whereas the activity was decreased to 80% of the maximum level at 4$0^{circ}C$ The enzyme activity exhibited good stability at the range of pH 4~7.