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

被引:73
|
作者
Ma, Weichao [1 ,2 ]
Cao, Weijia [1 ]
Zhang, Hong [1 ]
Chen, Kequan [1 ]
Li, Yan [1 ]
Ouyang, Pingkai [1 ]
机构
[1] Nanjing Tech Univ, State Key Lab Mat Oriented Chem Engn, Coll Biotechnol & Pharmaceut Engn, Nanjing 211816, Jiangsu, Peoples R China
[2] Tianshui Normal Univ, Sch Bioengn & Biotechnol, Tianshui 741001, Peoples R China
关键词
Cadaverine; Co-expression; Lysine/cadaverine antiporter; PelB; Whole-cell bioconversion; CORYNEBACTERIUM-GLUTAMICUM; E; COLI; PERMEABILITY; ANTIPORTER; SECRETION; PROTEINS; STRESS; AMINES; OPERON; LEADS;
D O I
10.1007/s10529-014-1753-5
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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.
引用
收藏
页码:799 / 806
页数:8
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