Your browser doesn't support javascript.
loading
Engineering Corynebacterium glutamicum for the efficient production of 3-hydroxypropionic acid from glucose via the ß-alanine pathway.
Wang, Xiaodi; Hou, Junyuan; Cui, Jieyao; Wang, Zhiwen; Chen, Tao.
Affiliation
  • Wang X; Frontier Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering of the Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, China.
  • Hou J; School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, China.
  • Cui J; Frontier Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering of the Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, China.
  • Wang Z; School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, China.
  • Chen T; Frontier Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering of the Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, China.
Synth Syst Biotechnol ; 9(4): 752-758, 2024 Dec.
Article in En | MEDLINE | ID: mdl-39007091
ABSTRACT
3-Hydroxypropionic Acid (3-HP) is recognized as a high value-added chemical with a broad range of applications. Among the various biosynthetic pathways for 3-HP production, the ß-alanine pathway is particularly noteworthy due to its capacity to generate 3-HP from glucose at a high theoretical titer. In this study, the ß-alanine biosynthesis pathway was introduced and optimized in Corynebacterium glutamicum. By strategically regulating the supply of precursors, we successfully engineered a strain capable of efficiently synthesizing 3-HP through the ß-alanine pathway, utilizing glucose as the substrate. The engineered strain CgP36 produced 47.54 g/L 3-HP at a yield of 0.295 g/g glucose during the fed-batch fermentation in a 5 L fermenter, thereby attaining the highest 3-HP titer obtained from glucose via the ß-alanine pathway.
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Synth Syst Biotechnol Year: 2024 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Synth Syst Biotechnol Year: 2024 Document type: Article Affiliation country: Country of publication: