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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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Autores principales: Engelskirchen, Sandra, Wellert, Stefan, Holderer, Olaf, Frielinghaus, Henrich, Laupheimer, Michaela, Richter, Sven, Nestl, Bettina, Nebel, Bernd, Hauer, Bernhard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7814304/
https://www.ncbi.nlm.nih.gov/pubmed/33469526
http://dx.doi.org/10.3389/fchem.2020.613388
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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
collection PubMed
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.
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spelling pubmed-78143042021-01-18 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 Front Chem Chemistry 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. Frontiers Media S.A. 2021-01-05 /pmc/articles/PMC7814304/ /pubmed/33469526 http://dx.doi.org/10.3389/fchem.2020.613388 Text en 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.
spellingShingle 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
title 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_short Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions
title_sort surfactant monolayer bending elasticity in lipase containing bicontinuous microemulsions
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7814304/
https://www.ncbi.nlm.nih.gov/pubmed/33469526
http://dx.doi.org/10.3389/fchem.2020.613388
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