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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,...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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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. |
format | Online Article Text |
id | pubmed-8147470 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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