Effect of overexpression of nicotinic acid phosphoribosyl transferase on succinic acid production in Escherichia coli NZN111.
- Author:
Rongming LIU
1
;
Jiangfeng MA
;
Liya LIANG
;
Bing XU
;
Guangming WANG
;
Min ZHANG
;
Min JIANG
Author Information
1. State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210009, China.
- Publication Type:Journal Article
- MeSH:
Acetyltransferases;
genetics;
metabolism;
Anaerobiosis;
Escherichia coli;
classification;
genetics;
metabolism;
Fermentation;
Genetic Enhancement;
methods;
Glucose;
metabolism;
L-Lactate Dehydrogenase;
genetics;
metabolism;
NAD;
metabolism;
Nicotinamide Phosphoribosyltransferase;
biosynthesis;
genetics;
Succinic Acid;
metabolism
- From:
Chinese Journal of Biotechnology
2011;27(10):1438-1447
- CountryChina
- Language:Chinese
-
Abstract:
Escherichia coli strain NZN111 is a promising candidate for the fermentative production of succinate. However, because lactate dehydrogenase and pyruvate formate lyase were inactivated in NZN111, this strain had an unbalanced NADH/NAD+ ratio and could not use glucose under anaerobic conditions. In this study, a recombinant strain E. coli NZN111/pTrc99a-pncB was constructed to overexpress the nicotinic acid phosphoribosyl transferase gene (pncB). Under anaerobic conditions with the addition of 0.5 mmol/L nicotinic acid and 0.3 mmol/L isopropyl beta-D-thiogalactopyranoside (IPTG), the specific nicotinic acid phosphoribosyl transferase (NAPRTase, EC 2.4.2.11) activity in the recombinant strain was 11-fold higher than that in E. coli NZN111, the concentration of NAD(H) was increased by 3.85-fold, especially the concentration of NAD+ was increased by 5.17-fold and NADH/NAD+ was decreased from 0.640 to 0.125. The recombinant strain regained the capability of growth and glucose utilization under anaerobic conditions.
