Enhancement of 1,3-propanediol production by expression of pyruvate decarboxylase and aldehyde dehydrogenase from Zymomonas mobilis in the acetolactate-synthase-deficient mutant of Klebsiella pneumoniae
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- Enhancement of 1,3-propanediol production by expression of pyruvate decarboxylase and aldehyde dehydrogenase from Zymomonas mobilis in the acetolactate-synthase-deficient mutant of Klebsiella pneumoniae
- Sung Mok Lee; Won-Kyung Hong; Sun-Yeon Heo; Jang Min Park; You Ree Jung; Baek Rock Oh; M H Joe; Jeong-Woo Seo; Chul Ho Kim
- Bibliographic Citation
- Journal of Industrial Microbiology & Biotechnology, vol. 41, no. 8, pp. 1259-1266
- Publication Year
- The acetolactate synthase (als)-deficient mutant of Klebsiella pneumoniae fails to produce 1,3-propanediol (1,3-PD) or 2,3-butanediol (2,3-BD), and is defective in glycerol metabolism. In an effort to recover production of the industrially valuable 1,3-PD, we introduced the Zymomonas mobilis pyruvate decarboxylase (pdc) and aldehyde dehydrogenase (aldB) genes into the als-deficient mutant to activate the conversion of pyruvate to ethanol. Heterologous expression of pdc and aldB efficiently recovered glycerol metabolism in the 2,3-BD synthesis-defective mutant, enhancing the production of 1,3-PD by preventing the accumulation of pyruvate. Production of 1,3-PD in the pdc- and aldB-expressing als-deficient mutant was further enhanced by increasing the aeration rate. This system uses metabolic engineering to produce 1,3-PD while minimizing the generation of 2,3-BD, offering a breakthrough for the industrial production of 1,3-PD from crude glycerol.
- 1,3-propanediol; Acetolactate synthase; Glycerol; Klebsiella pneumoniae; Metabolic engineering
- Appears in Collections:
- Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
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