Inactivation of aldehyde dehydrogenase:: A key factor for engineering 1,3-propanediol production by Klebsiella pneumoniae

被引:96
|
作者
Zhang, Yanping
Li, Yin
Du, Chenyu
Liu, Ming
Cao, Zhu'an [1 ]
机构
[1] Tsinghua Univ, Dept Chem Engn, Inst Biochem Engn, Beijing 100084, Peoples R China
[2] Chinese Acad Sci, Inst Microbiol, Beijing 100080, Peoples R China
关键词
aldehyde dehydrogenase; Klebsiella pneumoniae; inactivation; 1,3-propanediol; ethanol;
D O I
10.1016/j.ymben.2006.05.008
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
Production of 1,3-propanediol (1,3-PD) from glycerol by Klebsiella pneumoniae is restrained by ethanol formation. The first step in the formation of ethanol from acetyl-CoA is catalyzed by aldehyde dehydrogenase (ALDH), an enzyme that competes with 1,3-PD oxidoreductase for the cofactor NADH. This study aimed to improve the production of 1,3-PD by engineering the ethanol formation pathway. An inactivation mutation of the aldA gene encoding ALDH in K pneumoniae YMU2 was generated by insertion of a tetracycline resistance marker. Inactivation of ALDH resulted in a nearly abolished ethanol formation but a significantly improved 1,3-PD production. Metabolic flux analysis revealed that a pronounced redistribution of intracellular metabolic flux occurred. The final titer, the productivity of 1,3-PD and the yield of 1,3-PD relative to glycerol of the mutant strain reached 927.6 mmol L-1. 14.05 mmol L-1 h(-1) and 0.699mol mol(-1), respectively, which were much higher than those of the parent strain. In addition, the specific 1,3-PD-producing capability (1,3-PD produced per gram of cells) of the mutant strain was 2-fold that of the parent strain due to a lower growth yield of the mutant. By increasing NADH availability, this study demonstrates an important metabolic engineering approach to improve the efficiency of oxidoreduction-coupled bioprocesses. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:578 / 586
页数:9
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