Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment
| Autor: | Frank Wien, Laetitia Théron, Christophe Chambon, Matthieu Réfrégiers, Thierry Sayd, Christine Ravel, Jacques Rouel, Aline Bonifacie, Jérémy Delabre, Véronique Santé-Lhoutellier, Philippe Gatellier, Laurent Aubry, Thierry Astruc |
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| Přispěvatelé: | Qualité des Produits Animaux (QuaPA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), ROSSI, Sabine |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Health (social science) Plant Science TP1-1185 digestion Protein oxidation 01 natural sciences Health Professions (miscellaneous) Microbiology 03 medical and health sciences Pepsin Denaturation (biochemistry) protein oxidation Protein secondary structure synchrotron radiation circular dichroism pepsin mass spectrometry 2. Zero hunger chemistry.chemical_classification biology 010405 organic chemistry Chemical technology Communication 0104 chemical sciences [SDV.AEN] Life Sciences [q-bio]/Food and Nutrition 030104 developmental biology Enzyme chemistry Digestive enzyme Biophysics biology.protein Protein folding Digestion [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition Food Science |
| Zdroj: | Foods Foods, MDPI, 2021, 10 (5), pp.998. ⟨10.3390/foods10050998⟩ Foods, 2021, 10 (5), pp.998. ⟨10.3390/foods10050998⟩ Foods, Vol 10, Iss 998, p 998 (2021) |
| ISSN: | 2304-8158 |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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