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Artificially sporulated Escherichia coli cells as a robust cell factory for interfacial biocatalysis

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  • Zhiyong Sun

    (University of Southern Denmark)

  • René Hübner

    (Ion Beam Center, Helmholtz-Zentrum Dresden - Rossendorf)

  • Jian Li

    (ShanghaiTech University)

  • Changzhu Wu

    (University of Southern Denmark
    University of Southern Denmark)

Abstract

The natural bacterial spores have inspired the development of artificial spores, through coating cells with protective materials, for durable whole-cell catalysis. Despite attractiveness, artificial spores developed to date are generally limited to a few microorganisms with their natural endogenous enzymes, and they have never been explored as a generic platform for widespread synthesis. Here, we report a general approach to designing artificial spores based on Escherichia coli cells with recombinant enzymes. The artificial spores are simply prepared by coating cells with polydopamine, which can withstand UV radiation, heating and organic solvents. Additionally, the protective coating enables living cells to stabilize aqueous-organic emulsions for efficient interfacial biocatalysis ranging from single reactions to multienzyme cascades. Furthermore, the interfacial system can be easily expanded to chemoenzymatic synthesis by combining artificial spores with metal catalysts. Therefore, this artificial-spore-based platform technology is envisioned to lay the foundation for next-generation cell factory engineering.

Suggested Citation

  • Zhiyong Sun & René Hübner & Jian Li & Changzhu Wu, 2022. "Artificially sporulated Escherichia coli cells as a robust cell factory for interfacial biocatalysis," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-30915-2
    DOI: 10.1038/s41467-022-30915-2
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    References listed on IDEAS

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    1. Zachary C. Litman & Yajie Wang & Huimin Zhao & John F. Hartwig, 2018. "Cooperative asymmetric reactions combining photocatalysis and enzymatic catalysis," Nature, Nature, vol. 560(7718), pages 355-359, August.
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