2. Academic Validation
  3. Production of d-glucuronic acid from myo-inositol using Escherichia coli whole-cell biocatalyst overexpressing a novel myo-inositol oxygenase from Thermothelomyces thermophile

Production of d-glucuronic acid from myo-inositol using Escherichia coli whole-cell biocatalyst overexpressing a novel myo-inositol oxygenase from Thermothelomyces thermophile

  • Enzyme Microb Technol. 2019 Aug;127:70-74. doi: 10.1016/j.enzmictec.2019.04.013.
Fei Teng 1,  Ran You 2,  Meirong Hu 3,  Weifeng Liu 3,  Lei Wang 4,  Yong Tao 5
Affiliations

Affiliations

  • 1 Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China; College of Life Science, University of Chinese Academy of Sciences, Beijing, China.
  • 2 Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China; University of Science and Technology of China, Anhui, China.
  • 3 Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China.
  • 4 Institute of Microbiology, Chinese Academy of Sciences, CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Beijing, China. Electronic address: [email protected].
  • 5 College of Life Science, University of Chinese Academy of Sciences, Beijing, China. Electronic address: [email protected].
PMID: 31088620 DOI: 10.1016/j.enzmictec.2019.04.013
Abstract

D-glucuronic acid (GlcUA) is an important intermediate with numerous applications in the food, cosmetics, and pharmaceutical industries. Its biological production routes which employ myo-inositol oxygenase (MIOX) as the key Enzyme are attractive. In this study, five diverse MIOX-encoding genes, from Cryptococcus neoformans, Chaetomium thermophilum, Arabidopsis thaliana, Thermothelomyces thermophila, and Mus musculus were overexpressed in Escherichia coli, respectively. A novel MIOX from Thermothelomyces thermophila (TtMIOX) exhibited high specific activity, and efficiently converted myo-inositol to GlcUA. Meanwhile, the degradation of GlcUA was inhibited by inactivation of uxaC from the Escherichia coli genome. Finally, the BWΔuxaC whole-cell biocatalyst harboring TtMIOX resulted in the production of 106 g/L GlcUA within 12 h in a 1-L bioreactor, corresponding to a conversion of 91% and productivity of 8.83 g/L/h. This study provides a feasible method for the industrial production of GlcUA.

Keywords

D-glucuronic acid; Myo-inositol oxygenase; Thermothelomyces thermophile; Whole-cell biocatalyst.

Figures
Products