Dextranase of Arthrobacter sp. strain B7 (B7DEX enzyme) was characterized in this study. This enzyme hydrolyzed sucrose and dextran, but not other glucans (starch, nigeran, cellulose, -soluble glucan). It also hydrolyzed glucan from dental plaque with the activity of 7.38 + 0.66 U/ml, where the activity toward dextran was 31.88 + 1.24 U/ml. The enzyme exhibited the pH optimum of 7 and the temperature optimum of 50 oC. Its optimum stability was at pH 7 and 50 oC. The enzyme was inhibited by Fe3+, Cu2+, Zn2+, and Ag+, but not by the anionic detergent (SDS) and the nonionic detergent (Triton-X). The enzyme was activated by Ca2+, Na+, Mg2+, and saliva.