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POLYMER MEMBRANES

Proteins tailor pore geometry

Nature Materials volume 19, pages 257–258 (2020)Cite this article

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Using organic solvent shortens formation time of membrane nanosheets comprising proteins and copolymers, while tuning protein structure tailors the pore geometry, resulting in superior water permeation.

Separation processes account for more than 50% of the total energy consumed in many industries including clean water production1, crude oil fractionation2 and pharmaceutical purification3, which utilize heat for evaporation, distillation and crystallization. Synthetic membranes have been developed and applied in these processes to reduce energy consumption by removing dependence on phase-change-based separations. Pores with a range of diameters from micrometres to sub-nanometres are created in synthetic membranes to fulfil the requirements of different applications. Separation of molecules is achieved by passing small dimension molecules in a fluid through the pores while retaining larger dimension molecules including solutes. Over the past few decades, membrane scientists have strived to maximize the fluid flux and tailor the solute selectivity. Faster permeation rates can reduce membrane area, required pressure or both, and thus the operational cost for processing a given quantity of fluid within a definite timeframe. Tailoring pore geometry and/or microporosity in the separating layer might allow the customization of membranes for dedicated applications requiring sharp and clear cut-offs. Defined and controllable pores are sought after to provide straight through-membrane pathways that should only transport molecules with dimension smaller than the pore diameter. However, enhancement of fluid flux and manipulation of selectivity can compete with each other4, so that optimization of both remains a key challenge.

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Fig. 1: Stable membranes comprising artificial water channels made from proteins and block copolymers.
Fig. 2: Effect of intrinsic membrane permeance on process efficiency using spiral-wound membrane modules.

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Authors and Affiliations

  1. Department of Chemical Engineering, Imperial College London, London, UK

    Andrew G. Livingston & Zhiwei Jiang

  2. School of Engineering and Materials Science, Queen Mary University of London, London, UK

    Andrew G. Livingston

Authors
  1. Andrew G. Livingston
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  2. Zhiwei Jiang
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Correspondence to Andrew G. Livingston.

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Livingston, A.G., Jiang, Z. Proteins tailor pore geometry. Nat. Mater. 19, 257–258 (2020). https://doi.org/10.1038/s41563-019-0596-9

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  • DOI: https://doi.org/10.1038/s41563-019-0596-9

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