A homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids
Abstract The separation of amino acids from complex mixtures remains an essential yet multi-step, energy-intensive process. Membrane separation technology offers a more energy-efficient alternative, but its effectiveness relies on achieving highly precise molecular recognition. Here, we report a hom...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-63247-y |
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| author | Ting Xu Li Cao Shuhao An Xiaowei Liu Zhen Li Zhiping Lai |
| author_facet | Ting Xu Li Cao Shuhao An Xiaowei Liu Zhen Li Zhiping Lai |
| author_sort | Ting Xu |
| collection | DOAJ |
| description | Abstract The separation of amino acids from complex mixtures remains an essential yet multi-step, energy-intensive process. Membrane separation technology offers a more energy-efficient alternative, but its effectiveness relies on achieving highly precise molecular recognition. Here, we report a homochiral covalent organic framework (COF) membrane with ordered ultra-microporous pore structures for targeted extraction of specific enantiomer from amino acid mixtures. Benefiting from its high crystallinity and ultra-microporous chiral channels, the membrane exhibits both excellent permeability and enantioselectivity. A combination of experimental results, density functional theory calculations, and molecular dynamics simulations reveal a retarded transport mechanism, wherein stronger interactions between L-enantiomers and the homochiral pores hinder their transmembrane diffusion. We further demonstrate a two-stage cascade membrane process to simultaneously fractionate and enantioseparate amino acid mixtures, achieving near pure (99.5%) D-threonine from an eight-component protein hydrolysis complex. This study offers a promising and sustainable membrane-based solution for efficient amino acid purification. |
| format | Article |
| id | doaj-art-ccfd5508b24642329e00748b26cb8c39 |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-ccfd5508b24642329e00748b26cb8c392025-08-24T11:36:33ZengNature PortfolioNature Communications2041-17232025-08-011611810.1038/s41467-025-63247-yA homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acidsTing Xu0Li Cao1Shuhao An2Xiaowei Liu3Zhen Li4Zhiping Lai5Center of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST)Center of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST)Center of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST)Center of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST)Center of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST)Center of Excellence for Renewable Energy and Storage Technologies (CREST), Division of Physical Science and Engineering, 4700 King Abdullah University of Science and Technology (KAUST)Abstract The separation of amino acids from complex mixtures remains an essential yet multi-step, energy-intensive process. Membrane separation technology offers a more energy-efficient alternative, but its effectiveness relies on achieving highly precise molecular recognition. Here, we report a homochiral covalent organic framework (COF) membrane with ordered ultra-microporous pore structures for targeted extraction of specific enantiomer from amino acid mixtures. Benefiting from its high crystallinity and ultra-microporous chiral channels, the membrane exhibits both excellent permeability and enantioselectivity. A combination of experimental results, density functional theory calculations, and molecular dynamics simulations reveal a retarded transport mechanism, wherein stronger interactions between L-enantiomers and the homochiral pores hinder their transmembrane diffusion. We further demonstrate a two-stage cascade membrane process to simultaneously fractionate and enantioseparate amino acid mixtures, achieving near pure (99.5%) D-threonine from an eight-component protein hydrolysis complex. This study offers a promising and sustainable membrane-based solution for efficient amino acid purification.https://doi.org/10.1038/s41467-025-63247-y |
| spellingShingle | Ting Xu Li Cao Shuhao An Xiaowei Liu Zhen Li Zhiping Lai A homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids Nature Communications |
| title | A homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids |
| title_full | A homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids |
| title_fullStr | A homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids |
| title_full_unstemmed | A homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids |
| title_short | A homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids |
| title_sort | homochiral covalent organic framework membrane for the enantioseparation and fractionation of amino acids |
| url | https://doi.org/10.1038/s41467-025-63247-y |
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