A basic inducible protein, ICG, containing chitinase and β-1,3-glucanase activity concomittantly was purified from cell suspension culture media of rice after the treatment of chitooligosaccharides. The isolated ICG enzyme gave a single band on native and SDS polyacrylamide gel electrophoresis and its molecular weight was estimated to be 52.53 kd. The optimal temperature and optimal pH of both enzyme activities in ICG were 60C, pH 6.0 for chitinase activity and 37℃, pH 4.0 for β-1,3-glucanase activity. K_M and V_(max) values for chitinase were 0.474 mM. 2.997 nM/min., and those for β-1,3-glucanase were 1.004 mM·0.739 nM/min. respectively. TLC analysis of the chitooligosaccharide hydrolysates with ICG enzyme indicated that ICG acts as endochitinase.