An endoglucanase from Bacillus akibai I-1 was successfully overexpressed in Bacillus subtilis 168 and the expression level of the recombinant enzyme was greatly enhanced by using the sucrose-inducible sacB promoter. The endoglucanase activity in the culture supernatant of recombinant B. subtilis by using itself promoter (Hpall) in plasmid pMA5 was 3 U/ml. Interestingly, with the addition of sacB promoter at down-stream from the Hpall promoter or the replacement of Hpall promoter by the sacB promoter, the endoglucanase activities reached 62 and 60 U/ml, respectively, under the optimal culture conditions. These results demonstrated that the sacB promoter might be more efficient for the expression of the endoglucanase than the Hpall promoter. More interestingly, the purified native enzyme had broad pH stability, good thermostability and resistibility to various metal ions and chelating agents examined, while the recombinant enzyme had improved resistibility to SDS, which was stable in 0.2% (w/v) laundry detergent and thus showed great potential in detergents industry. (C) 2012 Elsevier Inc. All rights reserved.