Engineered Pichia pastoris strain secreting and expressing β-glucosidase gene of Bacillus pumilus was constructed and enzymatic properties of recombinant enzyme were investigated. Based on the codon usage of Pichia pastoris, the codon of the β-glucosidase gene of Bacillus pumilus was optimized, the whole gene sequence was designed and synthesized, and the expression vector was constructed and transferred into Pichia pastoris. The results showed that the β-glucosidase gene of Bacillus pumilus had been successfully transferred into the yeast and secreted and expressed. The activity of the fermentation broth after 72 h induction could reach 25.39 U/mL. The optimum temperature and pH for the recombinant β-glucosidase were 45 ℃ and 9.0, and the K_m and V_max of recombinant enzyme were 1.26 mmol/L and 32.15 μmol/(min·mg), respectively. The relative activity of recombinant β-glucosidase to soybean glycoside hydrolysis was 248% of that of pNPG, and the transglycosylation activity catalyzed the enzymatic synthesis of gentiobiose yield of 34.25 g/L using 50% glucose as the substrate.