Abstract: ObjectiveTo express wbbLprotein of Mycobacterium tuberculosis in E.coliBL21 (DE3) underoptinistic conditions, and to obtain and identify the soluble protein expressed.MethodsThe pET16b-Tb wbbL was expressed in E.coliBL21 (DE3) under different induction conditions.The cexpression system for expressing chaperons of pKJE7 plasmid and soluble wbbL protein was through condition inprovement Both supernatant and pellet fractions of wbbL protein expressed were analyzed with SDS-PAGE and western blotting methods after ultrasonic processing.ResultsThe results demonstrated that the wbbL protein was obtained in soluble fraction from co-expression system induced by the optinization concentration of 0.5 g/L-arabinose under 30℃ for 5hr and 0.5mmol/L IPTG under 30℃ for 2hr.The recombinant protein constituted 55.6% of the total protein of the cells.The wbbL gene was expressed into wbbL protein correctly Conclusion The soluble wbbL protein from E.coliBL21 (DE3) carrying pET16b-Tb wbbL and pKJE7 plasmid was acquired.The purified wbbL protein could be utilized to study its kinetics and to develope an enzyme assay for screening drugs.