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Mining of aminotransferase genes for efficient bio-production of 1, 3-diaminopropane.

Authors :
Ye, Pan
Wang, Tiantian
Xu, Xue
Lu, Mengqing
Zhang, Xinyu
Li, Naiqiang
Source :
Biochemical Engineering Journal. Sep2024, Vol. 209, pN.PAG-N.PAG. 1p.
Publication Year :
2024

Abstract

With the increasing attention to environmental issues and sustainable development, bio-production of diamines from renewable raw materials is very important for the establishment of a sustainable nylon industry. A three carbon linear chain diamine, 1,3-diaminopropane (1,3-DAP), is an important platform chemical and has the potential for novel types of polyamides preparation. In this study, the C 4 biosynthetic pathway for 1,3-DAP reported before was introduced into Escherichia coli W3110 and homolog mining of 2-ketoglutarate 4-aminotransferase genes was conducted to increase 1,3-DAP production. We demonstrated that aminotransferase RocD from Bacillus subtilis 168 was the most effective one among the candidates. Meanwhile, l -aspartate transporters such as GltP from E. coli, GltP and GltT from B. subtilis 168 were examined to further improve the 1,3-DAP production. Subsequently, the dual-vector systems were introduced to the host to co-express aminotransferases from different sources and the engineered E. coli W3110 could accumulate 302 mg/L of 1,3-DAP with a yield of 0.31 mol/mol (1,3-DAP/ l -aspartate) on the shake flask cultivation. The strategies reported here will be useful for the efficient and sustainable bio-based production of 1,3-DAP. • Aminotransferase RocD was first used for efficient production of 1,3-diaminopropane. • l -aspartate transporter GltTbsu improved 1, 3-diaminopropane production by 23.03 %. • Two-aminotransferase system increased 1, 3-diaminopropane titer to 302 mg/L. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
1369703X
Volume :
209
Database :
Academic Search Index
Journal :
Biochemical Engineering Journal
Publication Type :
Academic Journal
Accession number :
178401424
Full Text :
https://doi.org/10.1016/j.bej.2024.109377