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pneumoniae were inserted into a co-expression vector pACYCDuet-1 synchronously and the recombinant strain E. coli/pACYCDuet-dhaB-dhaT was obtained. Both enzymes were functionally coexpressed in E. coli at the presence of the selective pressure and the addition of the IPTG. The specific
enzyme activity of DHAB and DHAT were 8.3 and 6.2 U/mg, respectively. When cultivated at 37°C for 30 h, the recombinant microorganisms produced 1,3-PD of 11.3 g with the consumption of 40 g glycerol per liter. The production of 1,3-PD by the strain E. coli/pACYCDuet-dhaB-dhaT was about 13-fold higher than the recombinant E. coli harboring the gene dhaB.