Beta 1,3-1,4 glucanase was purified 12.3-fold to homogeneity with a yield of 20.3% in two steps which comprised, ammonium sulfate precipitation and size exclusion chromatography. The molecular mass was determined to be 39 kDa. The isoelectric point and optimum pH were 4.5 and 5.0 and beta-glucanase at low pH was more stable than that at high pHs. The optimum temperature of beta-glucanase was 50°C and it was relatively stable at below 40°C for 60 min. The half-lives of the enzyme at 50°C and 70°C were 120 min and 29.5 min, respectively. The Km of the enzyme on beta-glucan was 5.1 mg/ml, and the Vm on beta-glucan was 52.1 µmol of glucose equivalents per mg of the protein per min. The purified enzyme was highly sensitive to Mn+2, but showed less sensitivity to other divalent ions. Results indicated that produced beta 1,3-1,4 glucanase with relatively good thermal stability and stability at low pH, might be used in industrial applications particularly in animal feed industry.