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Immobilization protects enzymes from plasma-mediated inactivation
Non-thermal plasmas are used in various applications to inactivate biological agents or biomolecules. A complex cocktail of reactive species, (vacuum) UV radiation and in some cases exposure to an electric field together cause the detrimental effects. In contrast to this disruptive property of techn...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10598437/ https://www.ncbi.nlm.nih.gov/pubmed/37876274 http://dx.doi.org/10.1098/rsif.2023.0299 |
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author | Dirks, Tim Yayci, Abdulkadir Klopsch, Sabrina Krewing, Marco Zhang, Wuyuan Hollmann, Frank Bandow, Julia E. |
author_facet | Dirks, Tim Yayci, Abdulkadir Klopsch, Sabrina Krewing, Marco Zhang, Wuyuan Hollmann, Frank Bandow, Julia E. |
author_sort | Dirks, Tim |
collection | PubMed |
description | Non-thermal plasmas are used in various applications to inactivate biological agents or biomolecules. A complex cocktail of reactive species, (vacuum) UV radiation and in some cases exposure to an electric field together cause the detrimental effects. In contrast to this disruptive property of technical plasmas, we have shown previously that it is possible to use non-thermal plasma-generated species such as H(2)O(2) as cosubstrates in biocatalytic reactions. One of the main limitations in plasma-driven biocatalysis is the relatively short enzyme lifetime under plasma-operating conditions. This challenge could be overcome by immobilizing the enzymes on inert carrier materials. Here, we tested whether immobilization is suited to protect proteins from inactivation by plasma. To this end, using a dielectric barrier discharge device (PlasmaDerm), plasma stability was tested for five enzymes immobilized on ten different carrier materials. A comparative analysis of the treatment times needed to reduce enzyme activity of immobilized and free enzyme by 30% showed a maximum increase by a factor of 44. Covalent immobilization on a partly hydrophobic carrier surface proved most effective. We conclude from the study, that immobilization universally protects enzymes under plasma-operating conditions, paving the way for new emerging applications. |
format | Online Article Text |
id | pubmed-10598437 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-105984372023-10-26 Immobilization protects enzymes from plasma-mediated inactivation Dirks, Tim Yayci, Abdulkadir Klopsch, Sabrina Krewing, Marco Zhang, Wuyuan Hollmann, Frank Bandow, Julia E. J R Soc Interface Life Sciences–Physics interface Non-thermal plasmas are used in various applications to inactivate biological agents or biomolecules. A complex cocktail of reactive species, (vacuum) UV radiation and in some cases exposure to an electric field together cause the detrimental effects. In contrast to this disruptive property of technical plasmas, we have shown previously that it is possible to use non-thermal plasma-generated species such as H(2)O(2) as cosubstrates in biocatalytic reactions. One of the main limitations in plasma-driven biocatalysis is the relatively short enzyme lifetime under plasma-operating conditions. This challenge could be overcome by immobilizing the enzymes on inert carrier materials. Here, we tested whether immobilization is suited to protect proteins from inactivation by plasma. To this end, using a dielectric barrier discharge device (PlasmaDerm), plasma stability was tested for five enzymes immobilized on ten different carrier materials. A comparative analysis of the treatment times needed to reduce enzyme activity of immobilized and free enzyme by 30% showed a maximum increase by a factor of 44. Covalent immobilization on a partly hydrophobic carrier surface proved most effective. We conclude from the study, that immobilization universally protects enzymes under plasma-operating conditions, paving the way for new emerging applications. The Royal Society 2023-10-25 /pmc/articles/PMC10598437/ /pubmed/37876274 http://dx.doi.org/10.1098/rsif.2023.0299 Text en © 2023 The Authors. https://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Life Sciences–Physics interface Dirks, Tim Yayci, Abdulkadir Klopsch, Sabrina Krewing, Marco Zhang, Wuyuan Hollmann, Frank Bandow, Julia E. Immobilization protects enzymes from plasma-mediated inactivation |
title | Immobilization protects enzymes from plasma-mediated inactivation |
title_full | Immobilization protects enzymes from plasma-mediated inactivation |
title_fullStr | Immobilization protects enzymes from plasma-mediated inactivation |
title_full_unstemmed | Immobilization protects enzymes from plasma-mediated inactivation |
title_short | Immobilization protects enzymes from plasma-mediated inactivation |
title_sort | immobilization protects enzymes from plasma-mediated inactivation |
topic | Life Sciences–Physics interface |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10598437/ https://www.ncbi.nlm.nih.gov/pubmed/37876274 http://dx.doi.org/10.1098/rsif.2023.0299 |
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