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Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme
During the processing of biomolecules by ultrafiltration, the lysozyme enzyme undergoes conformational changes, which can affect its antibacterial activity. Operational conditions are considered to be one of the main parameters responsible for such changes, especially when using the same membrane an...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8187345/ https://www.ncbi.nlm.nih.gov/pubmed/34103632 http://dx.doi.org/10.1038/s41598-021-91564-x |
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author | Miron, Simona M. de Espindola, Ariane Dutournié, Patrick Ponche, Arnaud |
author_facet | Miron, Simona M. de Espindola, Ariane Dutournié, Patrick Ponche, Arnaud |
author_sort | Miron, Simona M. |
collection | PubMed |
description | During the processing of biomolecules by ultrafiltration, the lysozyme enzyme undergoes conformational changes, which can affect its antibacterial activity. Operational conditions are considered to be one of the main parameters responsible for such changes, especially when using the same membrane and molecule. The present study demonstrates that, the same cut-off membrane (commercial data) can result in different properties of the protein after filtration, due to their different pore network. The filtration of lysozyme, regardless of the membrane, produces a decrease in the membrane hydraulic permeability (between 10 and 30%) and an increase in its selectivity in terms of observed rejection rate (30%). For the filtrated lysozyme, it appears that the HPLC retention time increases depending on the membrane used. The antibacterial activity of the filtrated samples is lower than the native protein and decreases with the increase of the applied pressure reaching 55–60% loss for 12 bar which has not been reported in the literature before. The observed results by SEC-HPLC and bacteriological tests, suggest that the conformation of the filtrated molecules are indeed modified. These results highlight the relationship between protein conformation or activity and the imposed shear stress. |
format | Online Article Text |
id | pubmed-8187345 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-81873452021-06-09 Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme Miron, Simona M. de Espindola, Ariane Dutournié, Patrick Ponche, Arnaud Sci Rep Article During the processing of biomolecules by ultrafiltration, the lysozyme enzyme undergoes conformational changes, which can affect its antibacterial activity. Operational conditions are considered to be one of the main parameters responsible for such changes, especially when using the same membrane and molecule. The present study demonstrates that, the same cut-off membrane (commercial data) can result in different properties of the protein after filtration, due to their different pore network. The filtration of lysozyme, regardless of the membrane, produces a decrease in the membrane hydraulic permeability (between 10 and 30%) and an increase in its selectivity in terms of observed rejection rate (30%). For the filtrated lysozyme, it appears that the HPLC retention time increases depending on the membrane used. The antibacterial activity of the filtrated samples is lower than the native protein and decreases with the increase of the applied pressure reaching 55–60% loss for 12 bar which has not been reported in the literature before. The observed results by SEC-HPLC and bacteriological tests, suggest that the conformation of the filtrated molecules are indeed modified. These results highlight the relationship between protein conformation or activity and the imposed shear stress. Nature Publishing Group UK 2021-06-08 /pmc/articles/PMC8187345/ /pubmed/34103632 http://dx.doi.org/10.1038/s41598-021-91564-x Text en © The Author(s) 2021 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 Miron, Simona M. de Espindola, Ariane Dutournié, Patrick Ponche, Arnaud Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme |
title | Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme |
title_full | Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme |
title_fullStr | Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme |
title_full_unstemmed | Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme |
title_short | Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme |
title_sort | study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8187345/ https://www.ncbi.nlm.nih.gov/pubmed/34103632 http://dx.doi.org/10.1038/s41598-021-91564-x |
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