Improvement of 2,3-butanediol yield in Klebsiella pneumoniae by deletion of the pyruvate formate-lyase gene

Klebsiella pneumoniae is considered a good host strain for the production of 2,3-butanediol, which is a promising platform chemical with various industrial applications. In this study, three genes, including those encoding glucosyltransferase (wabG), lactate dehydrogenase (ldhA), and pyruvate format...

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Published in:Applied and Environmental Microbiology 2014-10, Vol.80 (19), p.6195-6203
Main Authors: Jung, Moo-Young, Mazumdar, Suman, Shin, Sang Heum, Yang, Kap-Seok, Lee, Jinwon, Oh, Min-Kyu
Format: Article
Language:English
Subjects:
Acetyltransferases - genetics
Acetyltransferases - metabolism
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biochemistry
Biosynthetic Pathways
Biotechnology
Butylene Glycols - metabolism
Comparative analysis
Escherichia coli
Fermentation
Gene expression
Gene Expression Regulation, Bacterial
Gene Expression Regulation, Enzymologic
Gene Knockout Techniques
Genetic engineering
Glucose
Glucose - metabolism
Glucosyltransferases - genetics
Glucosyltransferases - metabolism
Hydrogen
Klebsiella pneumoniae
Klebsiella pneumoniae - enzymology
Klebsiella pneumoniae - genetics
Klebsiella pneumoniae - metabolism
L-Lactate Dehydrogenase - genetics
L-Lactate Dehydrogenase - metabolism
Metabolic Engineering
Pneumonia
Sequence Deletion
Transcriptome
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Summary:Klebsiella pneumoniae is considered a good host strain for the production of 2,3-butanediol, which is a promising platform chemical with various industrial applications. In this study, three genes, including those encoding glucosyltransferase (wabG), lactate dehydrogenase (ldhA), and pyruvate formate-lyase (pflB), were disrupted in K. pneumoniae to reduce both its pathogenic characteristics and the production of several by-products. In flask cultivation with minimal medium, the yield of 2,3-butanediol from rationally engineered K. pneumoniae (ΔwabG ΔldhA ΔpflB) reached 0.461 g/g glucose, which was 92.2% of the theoretical maximum, with a significant reduction in by-product formation. However, the growth rate of the pflB mutant was slightly reduced compared to that of its parental strain. Comparison with similar mutants of Escherichia coli suggested that the growth defect of pflB-deficient K. pneumoniae was caused by redox imbalance rather than reduced level of intracellular acetyl coenzyme A (acetyl-CoA). From an analysis of the transcriptome, it was confirmed that the removal of pflB from K. pneumoniae significantly repressed the expression of genes involved in the formate hydrogen lyase (FHL) system.
ISSN:0099-2240
1098-5336
1098-6596
DOI:10.1128/AEM.02069-14