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

Biotechnol Lett. 2015 Apr;37(4):799-806. doi: 10.1007/s10529-014-1753-5. Epub 2014 Dec 17.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Transport Systems / genetics
  • Amino Acid Transport Systems / metabolism*
  • Antiporters / genetics
  • Antiporters / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacteriophage T7 / genetics
  • Cadaverine / metabolism*
  • Carboxy-Lyases / genetics
  • Carboxy-Lyases / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Gene Expression
  • Lysine / metabolism*
  • Metabolic Engineering*
  • Metabolic Networks and Pathways*
  • Plasmids
  • Promoter Regions, Genetic


  • Amino Acid Transport Systems
  • Antiporters
  • Bacterial Proteins
  • CadB protein, Bacteria
  • Carboxy-Lyases
  • lysine decarboxylase
  • Lysine
  • Cadaverine