Dual-channel glycolysis balances cofactor supply for L-homoserine biosynthesis in Corynebacterium glutamicum.

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ID: 275955
2022
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Abstract
L-Homoserine is an important platform compound that is widely used to produce many valuable bio-based products, but production of L-homoserine in Corynebacterium glutamicum remains low. In this study, an efficient L-homoserine-producing strain was constructed. Native pentose phosphate pathway (PPP) was enhanced and heterologous Entner-Doudoroff (ED) pathway was carefully introduced into L-homoserine-producing strain, which increased the L-homoserine titer. Coexpression of NADH-dependent aspartate-4-semialdehyde dehydrogenase and aspartate dehydrogenase could increase the titer from 11.3 to 13.3 g/L. Next, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (NADP-GPD) was coexpressed with that of NAD-dependent (NAD-GPD) to construct dual-channel glycolysis for balance of intracellular cofactors, which increased the L-homoserine titer by 48.6% to 16.8 g/L. Finally, engineered strain Cg18-1 accumulated 63.5 g/L L-homoserine after 96 h in a 5 L bioreactor, the highest titer reported to date for C. glutamicum. This dual-channel glycolysis strategy provides a reference for automatic cofactor regulation to promote efficient biosynthesis of other target products.
Reference Key
li2022dualchannelbioresource Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Li, Ning;Li, Lihong;Yu, Shiqin;Zhou, Jingwen;
Journal Bioresource technology
Year 2022
DOI
10.1016/j.biortech.2022.128473
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