AI Article Synopsis

  • 1,5-pentanediol (1,5-PDO) is crucial for making polyurethanes, and while it's usually produced chemically, there's a rising interest in making it more sustainably through biosynthesis.* -
  • This study created a new pathway in E. coli for producing 1,5-PDO from lysine, utilizing specific enzymes and optimizing conditions to enhance production efficiency.* -
  • The innovative approach combines cofactor recycling and transamination reactions, achieving a production level of 4.03 mM of 1,5-PDO, offering a greener alternative to traditional methods.*

Article Abstract

Background: 1,5-pentanediol (1,5-PDO) is a linear diol with an odd number of methylene groups, which is an important raw material for polyurethane production. In recent years, the chemical methods have been predominantly employed for synthesizing 1,5-PDO. However, with the increasing emphasis on environmentally friendly production, it has been a growing interest in the biosynthesis of 1,5-PDO. Due to the limited availability of only three reported feasible biosynthesis pathways, we developed a new biosynthetic pathway to form a cell factory in Escherichia coli to produce 1,5-PDO.

Results: In this study, we reported an artificial pathway for the synthesis of 1,5-PDO from lysine with an integrated cofactor and co-substrate recycling and also evaluated its feasibility in E.coli. To get through the pathway, we first screened aminotransferases originated from different organisms to identify the enzyme that could successfully transfer two amines from cadaverine, and thus GabT from E. coli was characterized. It was then cascaded with lysine decarboxylase and alcohol dehydrogenase from E. coli to achieve the whole-cell production of 1,5-PDO from lysine. To improve the whole-cell activity for 1,5-PDO production, we employed a protein scaffold of EutM for GabT assembly and glutamate dehydrogenase was also validated for the recycling of NADPH and α-ketoglutaric acid (α-KG). After optimizing the cultivation and bioconversion conditions, the titer of 1,5-PDO reached 4.03 mM.

Conclusion: We established a novel pathway for 1,5-PDO production through two consecutive transamination reaction from cadaverine, and also integrated cofactor and co-substrate recycling system, which provided an alternative option for the biosynthesis of 1,5-PDO.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11075332PMC
http://dx.doi.org/10.1186/s12934-024-02408-yDOI Listing

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