To characterize the β-glucosidase RpBgl7 from Reticulitermes perilucifugus,it was analyzed by bioinformatics methods to reveal its belonged family and structure.The recombinant vector pCold-TF-RpBgl7 was transferred into E.coli and overexpressed. RpBgl7 was purified to study its optimal conditions and kinetics.The results showed that,RpBgl7 belonged to glycoside hydrolase family 1,and contained 2 conserved catalytic residues Glu187 and Glu394.RpBgl7 overexpressed in BL21(DE3) was purified in one step using nickel chelating affinity chromatography with high purity.The optimal pH value of RpBgl7 was 6.0 and the optimum temperature was 70℃.The K_m and k_cat of RpBgl7 with p-nitrophenyl-β-D-glucopyranoside as substrate were 0.13 mmol/L and 3.15 s-1 ,respectively. RpBgl7 could be tolerant to Na⁺,K⁺,Mg²⁺,Cu²⁺and Ba²⁺,but it was strongly inhibited by Ca²⁺,Hg²⁺and Fe³⁺.