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Unlocking the access to oxidized coenzyme A via a single-step green membrane-based purification
A new membrane-based strategy to purify oxidized coenzyme A ((CoAS)(2)) from adenosine triphosphate (ATP), adenosine diphosphate (ADP) and adenosine monophosphate (AMP) has been developed. Commercially available membranes were screened and studied (permeate flux and overall compounds retention) whic...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9338019/ https://www.ncbi.nlm.nih.gov/pubmed/35906370 http://dx.doi.org/10.1038/s41598-022-17250-8 |
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author | Mouterde, Louis M. M. Willig, Gaëlle Langlait, Maxime M. J. Brunois, Fanny Chadni, Morad Allais, Florent |
author_facet | Mouterde, Louis M. M. Willig, Gaëlle Langlait, Maxime M. J. Brunois, Fanny Chadni, Morad Allais, Florent |
author_sort | Mouterde, Louis M. M. |
collection | PubMed |
description | A new membrane-based strategy to purify oxidized coenzyme A ((CoAS)(2)) from adenosine triphosphate (ATP), adenosine diphosphate (ADP) and adenosine monophosphate (AMP) has been developed. Commercially available membranes were screened and studied (permeate flux and overall compounds retention) which allowed the identification of one efficient membrane (GK from Suez Water Technologies & Solutions). Different total compounds concentrations solutions were used in the system in order to find the following working conditions: 4 bars with a total compounds solution of 5.19 g L(−1). Applying these conditions to a dia-filtration set-up allowed us to reach 68% pure (CoAS)(2) in 4.8 diafiltration volumes (DV) and a 95% (CoAS)(2) purity can be predicted in 8.5 DV. A comparative study of green metrics—i.e. process mass index (PMI)—of the classic chromatography vs the membrane-based one demonstrated the great advantages of the latter in terms of sustainability. This strategy unlocks the access to the essential and central cofactor that is coenzyme A. |
format | Online Article Text |
id | pubmed-9338019 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-93380192022-07-31 Unlocking the access to oxidized coenzyme A via a single-step green membrane-based purification Mouterde, Louis M. M. Willig, Gaëlle Langlait, Maxime M. J. Brunois, Fanny Chadni, Morad Allais, Florent Sci Rep Article A new membrane-based strategy to purify oxidized coenzyme A ((CoAS)(2)) from adenosine triphosphate (ATP), adenosine diphosphate (ADP) and adenosine monophosphate (AMP) has been developed. Commercially available membranes were screened and studied (permeate flux and overall compounds retention) which allowed the identification of one efficient membrane (GK from Suez Water Technologies & Solutions). Different total compounds concentrations solutions were used in the system in order to find the following working conditions: 4 bars with a total compounds solution of 5.19 g L(−1). Applying these conditions to a dia-filtration set-up allowed us to reach 68% pure (CoAS)(2) in 4.8 diafiltration volumes (DV) and a 95% (CoAS)(2) purity can be predicted in 8.5 DV. A comparative study of green metrics—i.e. process mass index (PMI)—of the classic chromatography vs the membrane-based one demonstrated the great advantages of the latter in terms of sustainability. This strategy unlocks the access to the essential and central cofactor that is coenzyme A. Nature Publishing Group UK 2022-07-29 /pmc/articles/PMC9338019/ /pubmed/35906370 http://dx.doi.org/10.1038/s41598-022-17250-8 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Mouterde, Louis M. M. Willig, Gaëlle Langlait, Maxime M. J. Brunois, Fanny Chadni, Morad Allais, Florent Unlocking the access to oxidized coenzyme A via a single-step green membrane-based purification |
title | Unlocking the access to oxidized coenzyme A via a single-step green membrane-based purification |
title_full | Unlocking the access to oxidized coenzyme A via a single-step green membrane-based purification |
title_fullStr | Unlocking the access to oxidized coenzyme A via a single-step green membrane-based purification |
title_full_unstemmed | Unlocking the access to oxidized coenzyme A via a single-step green membrane-based purification |
title_short | Unlocking the access to oxidized coenzyme A via a single-step green membrane-based purification |
title_sort | unlocking the access to oxidized coenzyme a via a single-step green membrane-based purification |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9338019/ https://www.ncbi.nlm.nih.gov/pubmed/35906370 http://dx.doi.org/10.1038/s41598-022-17250-8 |
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