In order to study the trehalase (EC 3. 2. 1. 28) from mushroom, Agaricus bisporus Lange Sing., the crude trehalase preparation was separated by fractionation of mushroom extracts with ammonium sulfate between 0.4 and 1.0 saturation, and its properties were examined. Mushroom trehalase showed optimum pH 6.0, and optimum temperature $40^{circ}C$. The enzyme was stable at pH range between 5.0 and 7.0, and at temperature below $50^{circ}C$. The activities of crude trehalase had proportional relations with enzyme concentrations below 490.2 mg % of protein and with substrate concentration below $2.6{ imes}10^{-3}M$, showing a Km value of 0.760 mM. The enzyme was inhibited by some metal ions such as $Sn^{2+}$, $Ca^{2+}$, $Hg^{2+}$, $Cd^{2+}$, $Cu^{2+}$, $Mn^{2+}$, $Zn^{2+}$, $Al^{3+}$, and $Fe^{3+}$, while $Ag^{+}$, $Ba^{2+}$, and $Mg^{2+}$ demonstrated remarkable increasing effects on the enzyme activity.