ATP is not essential for cadaverine production by Escherichia coli whole-cell bioconversion

被引：1
作者：
Song, Chenbin [1 ]
Li, Yijing [1 ]
Ma, Weichao [1 ,2 ]
机构：
[1] Tianshui Normal Univ, Coll Bioengn & Biotechnol, Tianshui Engn Res Ctr Agr Prod Deep Proc, Tianshui 741001, Peoples R China
[2] Tianshui Normal Univ, Coll Bioengn & Biotechnol, 105 Xihe South Rd, Tianshui 741001, Peoples R China
来源：
JOURNAL OF BIOTECHNOLOGY | 2022年 / 353卷
关键词：
Cadaverine; Intracellular ATP; Methionine adenosyltransferase; Whole-cell bioconversion; Proton motive force; DECARBOXYLATION; FORCE; NYLON; CADA;
D O I：
10.1016/j.jbiotec.2022.05.014
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：
ATP plays an essential role in the substrate/product transmembrane transportation during whole-cell biocon-version. This study aimed to address the impact of ATP upon cadaverine synthesis by whole-cell biocatalysts. The results showed no significant change in the ATP content (P = 0.625), and the specific cadaverine yield (P = 0.374) was observed in enzyme-catalyzed cadaverine synthesis with exogenous addition of ATP, indicating that the enzyme-catalyzed process does not require the participation of ATP. Furthermore, a whole-cell biocatalyst co-overexpressed methionine adenosyltransferase (MetK), lysine decarboxylase (CadA), and lysine/cadaverine antiporter (CadB) was constructed and used to investigate the effect of ATP deficiency on the cadaverine pro-duction by conversion of L-methionine and L-lysine, simultaneously. The results showed no significant difference (P = 0.585) in the specific cadaverine content between high and low levels of intracellular ATP. In addition, the intra-and extracellular cadaverine concentration and the ratio of ATP/ADP of whole-cell biocatalyst were determined. Results showed that the extracellular cadaverine concentration was much higher than the intra-cellular concentration, and no significant changes in ATP/ADP ratio during cadaverine synthesis. In contrast, an inhibition effect of the proton motive force (PMF) inhibitor carbonyl cyanide m-chlorophenylhydrazone (CCCP) on cadaverine production was detected. These findings strongly suggest that cadaverine transport in whole-cell biocatalysts was energized by PMF rather than ATP. Finally, a model was proposed to describe cadaverine's PMF-driven transport under different external pHs during whole-cell biocatalysis. This study is the first to experi-mentally confirm that the cadaverine production by Escherichia coli whole-cell bioconversion is independent of intracellular ATP, which helps guide the subsequent construction of biocatalysts and optimize transformation conditions.
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页码：44 / 50
页数：7
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