Characterization,modification, and overexpression of 3-phosphoglycerate dehydrogenase in Corynebacterium glutamicum for enhancing l-serine production |
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Authors: | Xu Guoqiang Jin Xuexia Guo Wen Dou Wenfang Zhang Xiaomei Xu Zhenghong |
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Institution: | 1.Laboratory of Pharmaceutical Engineering, School of Pharmaceutics Science, Jiangnan University, Wuxi, 214122, China ;2.National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi, 214122, China ;3.The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology Jiangnan University, Wuxi, 214122, China ; |
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Abstract: | The direct fermentative production of l-serine from renewable biomass using Corynebacterium glutamicum is attracting increasing attention. In this study, wild-type C. glutamicum SYPS-062 produced up to 6.65?±?0.23 g/L l-serine; to further improve l-serine production, the serA gene was cloned, and the C-terminal domain of 3-phosphoglycerate dehydrogenase (PGDH) from this strain was truncated. When expressed in Escherichia coli, the resultant mutein SerAΔ197 showed a specific PGDH activity of 1.092?±?0.05 U/mg protein, representing a decrease of 25.87 % from that encoded by serA, and was no longer sensitive to high concentrations of l-serine. When serA
Δ591 was overexpressed in C. glutamicum SYPS-062, the activity of PGDH in C. glutamicum pJC1-tac-serA
Δ591 increased by 47.72 %, and the resultant strain C. glutamicum pJC1-tac-serA
Δ591 could accumulate 7.69?±?0.22 g/L l-serine. Furthermore, when serA
Δ591 was overexpressed in C. glutamicum SYPS-062ΔsdaA, the resultant strain could accumulate 8.84?±?0.23 g/L l-serine at 102 h, and the yield of l-serine on cells (Y p/x) improved by 60 % when compared with that noted in the control. These results demonstrate that l-serine production in C. glutamicum SYPS-062 could be improved by overexpressing a C-terminal truncation of PGDH in combination with other genetic modifications. |
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