Enhanced cadaverine production from L-lysine using recombinant Escherichia coli co-overexpressing CadA and CadB.

The effect of fusing the PelB signal sequence to lysine/cadaverine antiporter (CadB) on the bioconversion of L-lysine to cadaverine was investigated. To construct a whole-cell biocatalyst for cadaverine production, four expression plasmids were constructed for the co-expression of lysine decarboxylase (CadA) and lysine/cadaverine antiporter (CadB) in Escherichia coli. Expressing CadB with the PelB signal sequence increased cadaverine production by 12%, and the optimal expression plasmid, pETDuet-pelB-CadB-CadA, contained two T7 promoter-controlled genes, CadA and the PelB-CadB fusion protein. Based on pETDuet-pelB-CadB-CadA, a whole-cell system for the bioconversion of L-lysine to cadaverine was constructed, and three strategies for L-lysine feeding were evaluated to eliminate the substrate inhibition problem. A cadaverine titer of 221 g l(-1) with a molar yield of 92% from lysine was obtained.