A MALDI-TOF based study of the in-vivo assembly of glutenin polymers of durum wheat
| Autor: | Cécile Mangavel, Hélène Rogniaux, Marie-Francoise Samson, Marie-Hélène Morel, Mariana Simões Larraz Ferreira, Joëlle Bonicel |
|---|---|
| Přispěvatelé: | Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
MALDI-TOF
Redox state Glutenin [SDV]Life Sciences [q-bio] Durum wheat Cysteine Grain development polymers chemistry.chemical_compound Storage protein 2. Zero hunger chemistry.chemical_classification Molecular mass biology Oxidative folding food and beverages Glutathione Polymer Monomer chemistry Biochemistry biology.protein Food Science |
| Zdroj: | Food Research International (63), 89-99. (2014) Food Research International Food Research International, Elsevier, 2014, 63, pp.89-99. ⟨10.1016/j.foodres.2013.12.025⟩ |
| ISSN: | 0963-9969 |
| DOI: | 10.1016/j.foodres.2013.12.025⟩ |
| Popis: | Wheat grain is recognized as the most suitable raw material for bread and pasta making due to the unique viscoelasticity of its storage proteins, and in particular its glutenin polymers. During grain development, low molecular weight (LMW) and high molecular weight (HMW) glutenin subunits (GS) gradually assembled through inter-chain disulfide bonds. Despite the impact of the final glutenin polymer size distribution on wheat technological quality, little is known concerning the oxidative folding of GS. In particular, which of their cysteine (Cys) residues participate to GS inter-chains remains putative. In this study GS from immature Triticum durum wheat grain were separated (10 SDS-PAGE) and digested into peptides, which were analyzed by MALDI-TOF/TOF. Differential alkylation of free and disulfide bonded Cys allowed us to identify the oxidative folding state of five types of LMW-GS and of the 1Bx20 HMW-GS. GS as monomers or as part of small oligomers carried a high number of free cysteine residues. In addition, some Cys residues, hitherto assumed as involved in intra-chain disulfide bonds, appeared simultaneously in free and oxidized forms. The last result could be assigned to their partial-blocking by glutathione. We concluded that the complete oxidative folding of LMW-GS is a late event, subsequent to GS inter-chain pairing. (C) 2014 Elsevier Ltd. All rights reserved. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect