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.
CITATION STYLE
Ma, W., Cao, W., Zhang, H., Chen, K., Li, Y., & Ouyang, P. (2015). Enhanced cadaverine production from l-lysine using recombinant Escherichia coli co-overexpressing CadA and CadB. Biotechnology Letters, 37(4), 799–806. https://doi.org/10.1007/s10529-014-1753-5
Mendeley helps you to discover research relevant for your work.