The DAEase gene sequence derived from Clostridium bolteae ATCCBAA-613 was synthesized by codon optimization. Using pCold TF as the expression vector, the cold-shock promoter CspA induced the expression of the DAEase gene in Escherichia coli BL21(DE3) at low temperature. Then, the highly soluble recombinant Cb-DAEase was obtained and purified by Ni-chelating affinity chromatography. Results showed that, the Cb-DAEase exhibited maximum activity at pH7.0 and 55 ℃. Additionally, the Cb-DAEase showed different sensitivities to the various metal ions when Co2+ was able to significantly (P