Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions
Lipase-catalyzed reactions offer many advantages among which a high degree of selectivity combined with the possibility to convert even non-natural substrates are of particular interest. A major drawback in the applicability of lipases in the conversion of synthetically interesting, non-natural subs...
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ftpubmed:oai:pubmedcentral.nih.gov:7814304 2023-05-15T13:41:38+02:00 Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions Engelskirchen, Sandra Wellert, Stefan Holderer, Olaf Frielinghaus, Henrich Laupheimer, Michaela Richter, Sven Nestl, Bettina Nebel, Bernd Hauer, Bernhard 2021-01-05 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7814304/ http://www.ncbi.nlm.nih.gov/pubmed/33469526 https://doi.org/10.3389/fchem.2020.613388 en eng Frontiers Media S.A. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7814304/ http://www.ncbi.nlm.nih.gov/pubmed/33469526 http://dx.doi.org/10.3389/fchem.2020.613388 Copyright © 2021 Engelskirchen, Wellert, Holderer, Frielinghaus, Laupheimer, Richter, Nestl, Nebel and Hauer. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. CC-BY Front Chem Chemistry Text 2021 ftpubmed https://doi.org/10.3389/fchem.2020.613388 2021-01-24T01:32:24Z Lipase-catalyzed reactions offer many advantages among which a high degree of selectivity combined with the possibility to convert even non-natural substrates are of particular interest. A major drawback in the applicability of lipases in the conversion of synthetically interesting, non-natural substrates is the substantial insolubility of such substrates in water. The conversion of substrates, natural or non-natural, by lipases generally involves the presence of a water–oil interface. In the present paper, we exploit the fact that the presence of lipases, in particular the lipase from Candida antarctica B (CalB), changes the bending elastic properties of a surfactant monolayer in a bicontinuous microemulsion consisting of D(2)O/NaCl -n-(d)-octane-pentaethylene glycol monodecyl ether (C(10)E(5)) in a similar manner as previously observed for amphiphilic block-copolymers. To determine the bending elastic constant, we have used two approaches, small angle neutron scattering (SANS) and neutron spin echo (NSE) spectroscopy. The time-averaged structure from SANS showed a slight decrease in bending elasticity, while on nanosecond time scales as probed with NSE, a stiffening has been observed, which was attributed to adsorption/desorption mechanisms of CalB at the surfactant monolayer. The results allow to derive further information on the influence of CalB on the composition and bending elasticity of the surfactant monolayer itself as well as the underlying adsorption/desorption mechanism. Text Antarc* Antarctica PubMed Central (PMC) Frontiers in Chemistry 8 |
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Chemistry Engelskirchen, Sandra Wellert, Stefan Holderer, Olaf Frielinghaus, Henrich Laupheimer, Michaela Richter, Sven Nestl, Bettina Nebel, Bernd Hauer, Bernhard Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions |
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Chemistry |
description |
Lipase-catalyzed reactions offer many advantages among which a high degree of selectivity combined with the possibility to convert even non-natural substrates are of particular interest. A major drawback in the applicability of lipases in the conversion of synthetically interesting, non-natural substrates is the substantial insolubility of such substrates in water. The conversion of substrates, natural or non-natural, by lipases generally involves the presence of a water–oil interface. In the present paper, we exploit the fact that the presence of lipases, in particular the lipase from Candida antarctica B (CalB), changes the bending elastic properties of a surfactant monolayer in a bicontinuous microemulsion consisting of D(2)O/NaCl -n-(d)-octane-pentaethylene glycol monodecyl ether (C(10)E(5)) in a similar manner as previously observed for amphiphilic block-copolymers. To determine the bending elastic constant, we have used two approaches, small angle neutron scattering (SANS) and neutron spin echo (NSE) spectroscopy. The time-averaged structure from SANS showed a slight decrease in bending elasticity, while on nanosecond time scales as probed with NSE, a stiffening has been observed, which was attributed to adsorption/desorption mechanisms of CalB at the surfactant monolayer. The results allow to derive further information on the influence of CalB on the composition and bending elasticity of the surfactant monolayer itself as well as the underlying adsorption/desorption mechanism. |
format |
Text |
author |
Engelskirchen, Sandra Wellert, Stefan Holderer, Olaf Frielinghaus, Henrich Laupheimer, Michaela Richter, Sven Nestl, Bettina Nebel, Bernd Hauer, Bernhard |
author_facet |
Engelskirchen, Sandra Wellert, Stefan Holderer, Olaf Frielinghaus, Henrich Laupheimer, Michaela Richter, Sven Nestl, Bettina Nebel, Bernd Hauer, Bernhard |
author_sort |
Engelskirchen, Sandra |
title |
Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions |
title_short |
Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions |
title_full |
Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions |
title_fullStr |
Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions |
title_full_unstemmed |
Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions |
title_sort |
surfactant monolayer bending elasticity in lipase containing bicontinuous microemulsions |
publisher |
Frontiers Media S.A. |
publishDate |
2021 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7814304/ http://www.ncbi.nlm.nih.gov/pubmed/33469526 https://doi.org/10.3389/fchem.2020.613388 |
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Antarc* Antarctica |
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Antarc* Antarctica |
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Front Chem |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7814304/ http://www.ncbi.nlm.nih.gov/pubmed/33469526 http://dx.doi.org/10.3389/fchem.2020.613388 |
op_rights |
Copyright © 2021 Engelskirchen, Wellert, Holderer, Frielinghaus, Laupheimer, Richter, Nestl, Nebel and Hauer. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
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CC-BY |
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https://doi.org/10.3389/fchem.2020.613388 |
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