In order to determine the characteristics of $eta$-glucosidase associated with cellulose degradation, the enzyme produced extracellularly by the mycelia of Tricholoma matsutake DGUM 26001 in culture broth was partially purified. The enzyme activity was maintained in the range of temperatures trom 55 to $70^{circ}C$ and its optimum temperature was $65^{circ}C$. The $eta$-glucosidase enzyme showed relatively high activity in the range of pH 3.0-5.0 and its optimum pH was 4.0. Under the optimal conditions, the specific activity of $eta$-glucosidase for salicin as a substrate was 18.7 unit/mg protein. After thermal treatment of the enzyme at $55^{circ}C$ for 60 min, more than 90% of the enzyme activity was still sustained. Iron($Fe^{++}$) stimulated enzyme activity, whereas mercury($Hg^{++}$) and copper($Cu^{++}$) inhibited. Compared to salicin as a substrate, the relative activity for cellobiose was observed to be 48.6%. The apparent $K_m$ and $V_{max}$ of the enzyme with cellobiose were 0.12 mM and 0.02 umol/min, respectively.