The $eta$-glucosidase gene from Streptomyces coelicolor A3(2) was cloned and expressed in Escherichia coli. The ORF consisted of 1377 nucleotides encoding 51 kDa in a predicted molecular weight. Effects of pH indicated that the $eta$-glucosidase showed similar activity using $alpha$-pNPG($ ho$-nitrophenyl-$alpha$-D-glucopyranoside), $eta$-pNPG($ ho$-nitrophenyl-$eta$-D-glucopyranoside), and $eta$-pNPF($ ho$-nitrophenyl-$eta$-D-fucopyranoside) at range of pH 3 to 10, and high activity using $eta$-pNPGA ($ ho$-nitrophenyl-$eta$-D-galactopyranoside) from pH 5 to 10, especially, 3.3 times higher activity at pH 9. Effects of temperature indicated that the $eta$-glucosidase showed low activity using $alpha$-pNPG, $eta$-pNPG, and $eta$-pNPF from $20^{circ}C$ to $70^{circ}C$, and increased activity using $eta$-pNPGA from $30^{circ}C$ to $50^{circ}C$, 1.8 times higher activity at $50^{circ}C$ than at $30^{circ}C$. According to activity determination of other substrates, the enzyme was active on daidzin, genistin, and glycitin, inactive on esculin and apigenin-7-glucose. The EDTA and DTT as reducing agents inhibited $eta$-glucosidase activity, but SDS and mercaptoethanol did not inhibit. Monovalent or divalent metal ions such as $MnSO_4$, $CaCl_2$, KCl, and $MgSO_4$ did not inhibited $eta$-glucosidase activity. $CuSO_4$ and NaCl showed low inhibition, and $ZnSO_4$ inhibited 3.3 times higher than control.