Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography
Abstract The adsorption of water and substrate on immobilized Candida antarctica lipase B was studied by performing adsorption isotherm measurements and using inverse gas chromatography (IGC). Water adsorption isotherm of the immobilized enzyme showed singular profile absorption incompatible with th...
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crwiley:10.1002/biot.201000272 2024-06-02T07:57:03+00:00 Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography Marton, Zsuzsanna Chaput, Ludovic Pierre, Guillaume Graber, Marianne 2010 http://dx.doi.org/10.1002/biot.201000272 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbiot.201000272 https://onlinelibrary.wiley.com/doi/pdf/10.1002/biot.201000272 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology Journal volume 5, issue 11, page 1216-1225 ISSN 1860-6768 1860-7314 journal-article 2010 crwiley https://doi.org/10.1002/biot.201000272 2024-05-03T10:59:38Z Abstract The adsorption of water and substrate on immobilized Candida antarctica lipase B was studied by performing adsorption isotherm measurements and using inverse gas chromatography (IGC). Water adsorption isotherm of the immobilized enzyme showed singular profile absorption incompatible with the Brunauer‐Emmet‐Teller model, probably due to the hydrophobic nature of the support, leading to very low interactions with water. IGC allowed determining the evolution with water thermodynamic activity (a W ) of both dispersive surface energies and acidity and basicity constants of immobilized enzyme. These results showed that water molecules progressively covered immobilized enzyme, when increasing a W , leading to a saturation of polar groups above a W 0.1 and full coverage of the surface above a W 0.25. IGC also enabled relevant experiments to investigate the behavior of substrates under a W that they will experience, in a competitive situation with water. Results indicated that substrates had to displace water molecules in order to adsorb on the enzyme from a W values ranging from 0.1 to 0.2, depending on the substrate. As the conditions used for these adsorption studies resemble the ones of the continuous enzymatic solid/gas reactor, in which activity and selectivity of the lipase were extensively studied, it was possible to link adsorption results with particular effects of water on enzyme properties. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology Journal 5 11 1216 1225 |
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English |
description |
Abstract The adsorption of water and substrate on immobilized Candida antarctica lipase B was studied by performing adsorption isotherm measurements and using inverse gas chromatography (IGC). Water adsorption isotherm of the immobilized enzyme showed singular profile absorption incompatible with the Brunauer‐Emmet‐Teller model, probably due to the hydrophobic nature of the support, leading to very low interactions with water. IGC allowed determining the evolution with water thermodynamic activity (a W ) of both dispersive surface energies and acidity and basicity constants of immobilized enzyme. These results showed that water molecules progressively covered immobilized enzyme, when increasing a W , leading to a saturation of polar groups above a W 0.1 and full coverage of the surface above a W 0.25. IGC also enabled relevant experiments to investigate the behavior of substrates under a W that they will experience, in a competitive situation with water. Results indicated that substrates had to displace water molecules in order to adsorb on the enzyme from a W values ranging from 0.1 to 0.2, depending on the substrate. As the conditions used for these adsorption studies resemble the ones of the continuous enzymatic solid/gas reactor, in which activity and selectivity of the lipase were extensively studied, it was possible to link adsorption results with particular effects of water on enzyme properties. |
format |
Article in Journal/Newspaper |
author |
Marton, Zsuzsanna Chaput, Ludovic Pierre, Guillaume Graber, Marianne |
spellingShingle |
Marton, Zsuzsanna Chaput, Ludovic Pierre, Guillaume Graber, Marianne Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography |
author_facet |
Marton, Zsuzsanna Chaput, Ludovic Pierre, Guillaume Graber, Marianne |
author_sort |
Marton, Zsuzsanna |
title |
Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography |
title_short |
Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography |
title_full |
Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography |
title_fullStr |
Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography |
title_full_unstemmed |
Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography |
title_sort |
lipase hydration state in the gas phase: sorption isotherm measurements and inverse gas chromatography |
publisher |
Wiley |
publishDate |
2010 |
url |
http://dx.doi.org/10.1002/biot.201000272 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbiot.201000272 https://onlinelibrary.wiley.com/doi/pdf/10.1002/biot.201000272 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biotechnology Journal volume 5, issue 11, page 1216-1225 ISSN 1860-6768 1860-7314 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/biot.201000272 |
container_title |
Biotechnology Journal |
container_volume |
5 |
container_issue |
11 |
container_start_page |
1216 |
op_container_end_page |
1225 |
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1800738302888771584 |