Abstract: The ade gene, which was presumed to encode adenine deaminase in Bacillus subtilis, was cloned, then the gene was inserted into expression vector pMal-c2x and transformed into Escherichia coli TB1. The fusion expression of the ade gene product with MBP was induced by IPTG. After purification by MBP affinity chromatography, the fusion protein was detected through SDS-PAGE. The deaminase activity of the fusion protein and related enzyme properties also were analyzed. The results show that the fusion protein had significant deaminase activity and verify that the ade gene was the coding gene of adenine deaminase. The study is very important for us to investigate the metabolism of adenine in Bacillus subtilis.

Key words: adenine deaminase, MBP fusion expression, activity measurement