In this study, a beta-glucosidase from Paenibacillus sp. M1 was expressed in E. coli BL21(DE3), purified and characterized. The specific activity of purified BglA was 137.64 U.mg(-1) protein with optimal temperature and pH of 50 degrees C and 6.0. Furthermore, BglA shows excellent adaption to various environmental factors such as temperature, pH and metal ions. Engineered E. coli Suc260 was further reconstructed by overexpressing the beta-glucosidase for achieving direct cellobiose utilization, which could efficiently utilize the pretreated sugarcane bagasses hydrolysate (SBH) consisting of 25.30 g.L-1 cellobiose, 9.70 g.L-1 glucose, 5.90 g.L-1 arabinose and 7.10 g.L-1 xylose. As a result, 26.50 g.L-1 and 24.30 g.L-1 succinic acid were produced by strain Suc260(pTbglA) from cellobiose and SBH with corresponding yields of 88.30% and 89.20% using dual-phase fermentation, respectively. This study indicated that incomplete enzymatic hydrolysate of SCB will be a potential feedstock for succinic acid production. (C) 2017 Elsevier Ltd. All rights reserved.