Journal
BIOTECHNOLOGY LETTERS
Volume 37, Issue 4, Pages 799-806Publisher
SPRINGER
DOI: 10.1007/s10529-014-1753-5
Keywords
Cadaverine; Co-expression; Lysine/cadaverine antiporter; PelB; Whole-cell bioconversion
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Funding
- National Nature Science Foundation of China [21390200, 21106068]
- National Key Technology Support Program [2012BAI44G00]
- 973 Program of China [2011CBA00807]
- 863 Program of China [2014AA021703]
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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.
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