Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media
While optical methods are not efficient enough for the easy, fast, and efficient detection of enzymatic activity in turbid media, the properties of the electron paramagnetic resonance (EPR) technique make it suitable for use in such media. Nitroxides which exhibit a change in their EPR hyperfine cou...
Published in: | Analytical Chemistry |
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American Chemical Society
2019
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Online Access: | https://oskar-bordeaux.fr/handle/20.500.12278/112620 https://doi.org/10.1021/acs.analchem.9b00561 |
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ftoskarbordeaux:oai:oskar-bordeaux.fr:20.500.12278/112620 2023-05-15T14:15:41+02:00 Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media AUDRAN, Gérard JACOUTOT, Samuel JUGNIOT, Natacha MARQUE, Sylvain MELLET, Philippe 2019 https://oskar-bordeaux.fr/handle/20.500.12278/112620 https://doi.org/10.1021/acs.analchem.9b00561 en eng American Chemical Society 0003-2700 https://oskar-bordeaux.fr/handle/20.500.12278/112620 doi:10.1021/acs.analchem.9b00561 Sciences du Vivant [q-bio] Article de revue 2019 ftoskarbordeaux https://doi.org/10.1021/acs.analchem.9b00561 2021-10-12T22:29:12Z While optical methods are not efficient enough for the easy, fast, and efficient detection of enzymatic activity in turbid media, the properties of the electron paramagnetic resonance (EPR) technique make it suitable for use in such media. Nitroxides which exhibit a change in their EPR hyperfine coupling constants upon enzymatic activity and are selective to lipases were developed under the name of shifting-nitroxides. Several fatty acids, exhibiting saturated and unsaturated chains of various lengths, were coupled with the shifting-nitroxide via an enol ester link and tested against several lipases. As the solubility of fatty acids is low in HEPES buffer, experiments were performed in turbid aqueous solution. Almost all labeled fatty acids were hydrolyzed by Candida rugosa lipase, and more selectivity is observed with Porcine Pancreas lipase type II. No activity was observed for lipase AK Amano 20, Candida antartica lipase B, and Mucor miehei lipase. Other/Unknown Material antartic* OSKAR Bordeaux (Open Science Knowledge ARchive) Rugosa ENVELOPE(-61.250,-61.250,-62.633,-62.633) Analytical Chemistry 91 9 5504 5507 |
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OSKAR Bordeaux (Open Science Knowledge ARchive) |
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ftoskarbordeaux |
language |
English |
topic |
Sciences du Vivant [q-bio] |
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Sciences du Vivant [q-bio] AUDRAN, Gérard JACOUTOT, Samuel JUGNIOT, Natacha MARQUE, Sylvain MELLET, Philippe Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media |
topic_facet |
Sciences du Vivant [q-bio] |
description |
While optical methods are not efficient enough for the easy, fast, and efficient detection of enzymatic activity in turbid media, the properties of the electron paramagnetic resonance (EPR) technique make it suitable for use in such media. Nitroxides which exhibit a change in their EPR hyperfine coupling constants upon enzymatic activity and are selective to lipases were developed under the name of shifting-nitroxides. Several fatty acids, exhibiting saturated and unsaturated chains of various lengths, were coupled with the shifting-nitroxide via an enol ester link and tested against several lipases. As the solubility of fatty acids is low in HEPES buffer, experiments were performed in turbid aqueous solution. Almost all labeled fatty acids were hydrolyzed by Candida rugosa lipase, and more selectivity is observed with Porcine Pancreas lipase type II. No activity was observed for lipase AK Amano 20, Candida antartica lipase B, and Mucor miehei lipase. |
format |
Other/Unknown Material |
author |
AUDRAN, Gérard JACOUTOT, Samuel JUGNIOT, Natacha MARQUE, Sylvain MELLET, Philippe |
author_facet |
AUDRAN, Gérard JACOUTOT, Samuel JUGNIOT, Natacha MARQUE, Sylvain MELLET, Philippe |
author_sort |
AUDRAN, Gérard |
title |
Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media |
title_short |
Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media |
title_full |
Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media |
title_fullStr |
Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media |
title_full_unstemmed |
Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media |
title_sort |
shifting-nitroxides to investigate enzymatic hydrolysis of fatty acids by lipases using electron paramagnetic resonance in turbid media |
publisher |
American Chemical Society |
publishDate |
2019 |
url |
https://oskar-bordeaux.fr/handle/20.500.12278/112620 https://doi.org/10.1021/acs.analchem.9b00561 |
long_lat |
ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
geographic |
Rugosa |
geographic_facet |
Rugosa |
genre |
antartic* |
genre_facet |
antartic* |
op_relation |
0003-2700 https://oskar-bordeaux.fr/handle/20.500.12278/112620 doi:10.1021/acs.analchem.9b00561 |
op_doi |
https://doi.org/10.1021/acs.analchem.9b00561 |
container_title |
Analytical Chemistry |
container_volume |
91 |
container_issue |
9 |
container_start_page |
5504 |
op_container_end_page |
5507 |
_version_ |
1766287995632091136 |