Shifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media
International audience 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...
Published in: | Analytical Chemistry |
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Online Access: | https://cnrs.hal.science/hal-02472334 https://doi.org/10.1021/acs.analchem.9b00561 |
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ftuniparissaclay:oai:HAL:hal-02472334v1 2024-05-12T07:56:52+00:00 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 Institut de Chimie Radicalaire (ICR) Aix Marseille Université (AMU)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) Centre de résonance magnétique des systèmes biologiques (CRMSB) Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS) Institut Lavoisier de Versailles (ILV) Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) 2019 https://cnrs.hal.science/hal-02472334 https://doi.org/10.1021/acs.analchem.9b00561 en eng HAL CCSD American Chemical Society info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.analchem.9b00561 hal-02472334 https://cnrs.hal.science/hal-02472334 doi:10.1021/acs.analchem.9b00561 ISSN: 0003-2700 EISSN: 1520-6882 Analytical Chemistry https://cnrs.hal.science/hal-02472334 Analytical Chemistry, 2019, 91 (9), pp.5504-5507. ⟨10.1021/acs.analchem.9b00561⟩ [SDV]Life Sciences [q-bio] info:eu-repo/semantics/article Journal articles 2019 ftuniparissaclay https://doi.org/10.1021/acs.analchem.9b00561 2024-04-15T17:44:26Z International audience 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. Article in Journal/Newspaper antartic* Archives ouvertes de Paris-Saclay Rugosa ENVELOPE(-61.250,-61.250,-62.633,-62.633) Analytical Chemistry 91 9 5504 5507 |
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[SDV]Life Sciences [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 |
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[SDV]Life Sciences [q-bio] |
description |
International audience 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. |
author2 |
Institut de Chimie Radicalaire (ICR) Aix Marseille Université (AMU)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) Centre de résonance magnétique des systèmes biologiques (CRMSB) Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS) Institut Lavoisier de Versailles (ILV) Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
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 |
HAL CCSD |
publishDate |
2019 |
url |
https://cnrs.hal.science/hal-02472334 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_source |
ISSN: 0003-2700 EISSN: 1520-6882 Analytical Chemistry https://cnrs.hal.science/hal-02472334 Analytical Chemistry, 2019, 91 (9), pp.5504-5507. ⟨10.1021/acs.analchem.9b00561⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.analchem.9b00561 hal-02472334 https://cnrs.hal.science/hal-02472334 doi:10.1021/acs.analchem.9b00561 |
op_doi |
https://doi.org/10.1021/acs.analchem.9b00561 |
container_title |
Analytical Chemistry |
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91 |
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9 |
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5504 |
op_container_end_page |
5507 |
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1798837219331407872 |