We report the cloning of a novel ${eta}$-glucosidase-like gene by function-based screening of a metagenomic library from uncultured soil microorganisms. The gene was named bgl1C and has an open reading frame of 1,443 base pairs. It encodes a 481 amino acid polypeptide with a predicted molecular mass of about 57.8 kDa. The deduced amino acid sequence did not show any homology with known ${eta}$-glucosidases. The putative ${eta}$-glucosidase gene was subcloned into the pETBlue-2 vector and overexpressed in E. coli Tuner (DE3) pLacI; the recombinant protein was purified to homogeneity. Functional characterization with a high performance liquid chromatography method demonstrated that the recombinant Bgl1C protein hydrolyzed D-glucosyl-${eta}$-(1-4)-D-glucose to glucose. The maximum activity for Bgl1C protein occurred at pH 8.0 and $42^{circ}C$ using p-nitrophenyl-${eta}$-D-glucoside as the substrate. A $CaCl_2$ concentration of 1 mM was required for optimal activity. The putative ${eta}$-glucosidase had an apparent $K_m$ value of 0.19 mM, a $V_max$ value of 4.75 U/mg and a $k_cat$ value of 316.7/min under the optimal reaction conditions. The biochemical characterization of Bgl1C has enlarged our understanding of the novel enzymes that can be isolated from the soil metagenome.