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Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment

Food processing affects the structure and chemical state of proteins. In particular, protein oxidation occurs and may impair protein properties. These chemical reactions initiated during processing can develop during digestion. Indeed, the physicochemical conditions of the stomach (oxygen pressure,...

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Autores principales: Théron, Laetitia, Bonifacie, Aline, Delabre, Jérémy, Sayd, Thierry, Aubry, Laurent, Gatellier, Philippe, Ravel, Christine, Chambon, Christophe, Astruc, Thierry, Rouel, Jacques, Santé-Lhoutellier, Véronique, Réfrégiers, Matthieu, Wien, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8147470/
https://www.ncbi.nlm.nih.gov/pubmed/34063224
http://dx.doi.org/10.3390/foods10050998
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author Théron, Laetitia
Bonifacie, Aline
Delabre, Jérémy
Sayd, Thierry
Aubry, Laurent
Gatellier, Philippe
Ravel, Christine
Chambon, Christophe
Astruc, Thierry
Rouel, Jacques
Santé-Lhoutellier, Véronique
Réfrégiers, Matthieu
Wien, Frank
author_facet Théron, Laetitia
Bonifacie, Aline
Delabre, Jérémy
Sayd, Thierry
Aubry, Laurent
Gatellier, Philippe
Ravel, Christine
Chambon, Christophe
Astruc, Thierry
Rouel, Jacques
Santé-Lhoutellier, Véronique
Réfrégiers, Matthieu
Wien, Frank
author_sort Théron, Laetitia
collection PubMed
description Food processing affects the structure and chemical state of proteins. In particular, protein oxidation occurs and may impair protein properties. These chemical reactions initiated during processing can develop during digestion. Indeed, the physicochemical conditions of the stomach (oxygen pressure, low pH) favor oxidation. In that respect, digestive proteases may be affected as well. Yet, very little is known about the link between endogenous oxidation of digestive enzymes, their potential denaturation, and, therefore, food protein digestibility. Thus, the objective of this study is to understand how oxidative chemical processes will impact the pepsin secondary structure and its hydrolytic activity. The folding and unfolding kinetics of pepsin under oxidative conditions was determined using Synchrotron Radiation Circular Dichroism. SRCD gave us the possibility to monitor the rapid kinetics of protein folding and unfolding in real-time, giving highly resolved spectral data. The proteolytic activity of control and oxidized pepsin was investigated by MALDI-TOF mass spectrometry on a meat protein model, the creatine kinase. MALDI-TOF MS allowed a rapid evaluation of the proteolytic activity through peptide fingerprint. This study opens up new perspectives by shifting the digestion paradigm taking into account the gastric digestive enzyme and its substrate.
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spelling pubmed-81474702021-05-26 Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment Théron, Laetitia Bonifacie, Aline Delabre, Jérémy Sayd, Thierry Aubry, Laurent Gatellier, Philippe Ravel, Christine Chambon, Christophe Astruc, Thierry Rouel, Jacques Santé-Lhoutellier, Véronique Réfrégiers, Matthieu Wien, Frank Foods Communication Food processing affects the structure and chemical state of proteins. In particular, protein oxidation occurs and may impair protein properties. These chemical reactions initiated during processing can develop during digestion. Indeed, the physicochemical conditions of the stomach (oxygen pressure, low pH) favor oxidation. In that respect, digestive proteases may be affected as well. Yet, very little is known about the link between endogenous oxidation of digestive enzymes, their potential denaturation, and, therefore, food protein digestibility. Thus, the objective of this study is to understand how oxidative chemical processes will impact the pepsin secondary structure and its hydrolytic activity. The folding and unfolding kinetics of pepsin under oxidative conditions was determined using Synchrotron Radiation Circular Dichroism. SRCD gave us the possibility to monitor the rapid kinetics of protein folding and unfolding in real-time, giving highly resolved spectral data. The proteolytic activity of control and oxidized pepsin was investigated by MALDI-TOF mass spectrometry on a meat protein model, the creatine kinase. MALDI-TOF MS allowed a rapid evaluation of the proteolytic activity through peptide fingerprint. This study opens up new perspectives by shifting the digestion paradigm taking into account the gastric digestive enzyme and its substrate. MDPI 2021-05-02 /pmc/articles/PMC8147470/ /pubmed/34063224 http://dx.doi.org/10.3390/foods10050998 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Théron, Laetitia
Bonifacie, Aline
Delabre, Jérémy
Sayd, Thierry
Aubry, Laurent
Gatellier, Philippe
Ravel, Christine
Chambon, Christophe
Astruc, Thierry
Rouel, Jacques
Santé-Lhoutellier, Véronique
Réfrégiers, Matthieu
Wien, Frank
Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment
title Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment
title_full Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment
title_fullStr Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment
title_full_unstemmed Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment
title_short Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment
title_sort investigation by synchrotron radiation circular dichroism of the secondary structure evolution of pepsin under oxidative environment
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8147470/
https://www.ncbi.nlm.nih.gov/pubmed/34063224
http://dx.doi.org/10.3390/foods10050998
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