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1. Crop diversity used in branded products with focus on legume species worldwide

Author: Tristan Salord, Marie-Benoît Magrini, Valérie Lullien-Pellerin, Guillaume Cabanac, Marie-Joseph Amiot, Cécile Barron, Adeline Boire, Valérie Micard, and Magalie Weber
Subjects: Nutrition. Foods and food supply, TX341-641, Food processing and manufacture, TP368-456
Abstract: Abstract Food diversity is a challenging issue for sustainable agrifood systems. Diets are increasingly dependent on branded packaged foods. Therefore, the crop diversity offered in the food market through these products is of particular importance. We scrutinize this diversity for some crops under great societal challenge: pulses. Based on the product launches referenced in the Mintel database over the last decade, we compare the food products containing pulse crops with those containing another legume—soy. From the 350,000 products analyzed, our results show that soy is mainly used but reveal some progress in the use of pulse species, particularly in Europe. The position of the examined species in the list of ingredients and in the product description allows us to assess its importance. The text-mining methods used usefully enable the monitoring of crop usage in the food market. We discuss several perspectives, notably how to deepen these results regarding consumer choices.
Published: 2024
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2. Sorghum protein ingredients: Production, compositional variability and enhancement of aqueous dispersibility through homogenization

Author: Thais Cristina Benatti Gallo, Valérie Beaumal, Bérénice Houinsou-Houssou, Michèle Viau, Lucie Ribourg-Birault, Hélène Sotin, Joëlle Bonicel, Adeline Boire, Valéria Aparecida Vieira Queiroz, Hamza Mameri, Sylvain Guyot, Alain Riaublanc, Vânia Regina Nicoletti, and Claire Berton-Carabin
Subjects: Kafirin, Tannins, Composition, Sorghum lipids, Particle size, Solubility, Nutrition. Foods and food supply, TX341-641, Food processing and manufacture, TP368-456
Abstract: Sorghum protein ingredients show promising applications, given that sorghum is a resilient grain with high protein content and bioactive components, such as tannins, in certain genotypes. This study aimed to investigate the production and characterization of sorghum protein ingredients extracted from both tannin-free and tannin-rich cultivars, along with an examination of their behavior in aqueous suspensions. The use of high-pressure homogenization to improve ingredient dispersibility was also assessed. Protein extracts exhibited protein contents ranging from 50 to 67 g/100 g (wet basis), with the highest values obtained in tannin-free samples. Total lipid contents were between 18 and 26 g/100 g (wet basis), with a high contribution of free fatty acids (68–76 g/100 g lipids), and tocopherol contents ranged from 1080 to 2039 µg/g total lipids. This is substantially higher than the lipid content in flours, implying an accumulation of lipids during the protein extraction process. While the dispersibility of the protein extracts in aqueous media was initially limited, high-pressure homogenization proved effective in reducing the average size of the particles in suspension, from 9–66 µm to 1.8–2.5 µm. This processing step significantly enhanced protein dispersibility by up to 288 %, especially for the tannin-rich samples.
Published: 2024
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3. Droplet Microfluidics for Food and Nutrition Applications

Author: Karin Schroen, Claire Berton-Carabin, Denis Renard, Mélanie Marquis, Adeline Boire, Rémy Cochereau, Chloé Amine, and Sébastien Marze
Subjects: emulsions, microgels, microparticles, microcapsules, biopolymers, nutrients, Mechanical engineering and machinery, TJ1-1570
Abstract: Droplet microfluidics revolutionizes the way experiments and analyses are conducted in many fields of science, based on decades of basic research. Applied sciences are also impacted, opening new perspectives on how we look at complex matter. In particular, food and nutritional sciences still have many research questions unsolved, and conventional laboratory methods are not always suitable to answer them. In this review, we present how microfluidics have been used in these fields to produce and investigate various droplet-based systems, namely simple and double emulsions, microgels, microparticles, and microcapsules with food-grade compositions. We show that droplet microfluidic devices enable unprecedented control over their production and properties, and can be integrated in lab-on-chip platforms for in situ and time-resolved analyses. This approach is illustrated for on-chip measurements of droplet interfacial properties, droplet–droplet coalescence, phase behavior of biopolymer mixtures, and reaction kinetics related to food digestion and nutrient absorption. As a perspective, we present promising developments in the adjacent fields of biochemistry and microbiology, as well as advanced microfluidics–analytical instrument coupling, all of which could be applied to solve research questions at the interface of food and nutritional sciences.
Published: 2021
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4. Optimization of a Droplet-Based Millifluidic Device to Investigate the Phase Behavior of Biopolymers, Including Viscous Conditions

Author: Adeline Boire, Anne-Laure Reguerre, Patrice Papineau, Chloé Amine, Joëlle Davy, Denis Renard, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), French National Research Institute for Agriculture, Food and Environment (INRAE), and Region Pays de la Loire.
Subjects: Materials science, Biophysics, Bioengineering, 02 engineering and technology, 010402 general chemistry, 01 natural sciences, Applied Microbiology and Biotechnology, Analytical Chemistry, Millifluidics, Colloid, chemistry.chemical_compound, [SDV.IDA]Life Sciences [q-bio]/Food engineering, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, Turbidity, Phase diagram, Drop (liquid), 021001 nanoscience & nanotechnology, 0104 chemical sciences, Volumetric flow rate, Biopolymers phase separation, [CHIM.POLY]Chemical Sciences/Polymers, chemistry, Chemical engineering, Homogeneous, Titanium dioxide, Grey level, 0210 nano-technology, Food Science
Abstract: International audience; Phase diagrams are widely used to map and control the assembly states of biopolymers. However, these studies are highly time and material consuming. Here, we present the optimization of a simple tool based on millifluidics to screen phase diagram of biopolymers, pure or in mixtures with other biopolymers. It is used (i) to generate a homogeneous mixture of biopolymers/buffer and/or biopolymers 1/ biopolymers 2 in a short time (similar to s), (ii) to vary the composition of the mixtures by adjusting the flow rates, and (iii) to determine the turbidity of the drop by grey level analysis. The mixing efficiency and the calibration turbidity vs. grey level were performed using colloidal titanium dioxide dispersions. The use of millifluidics reduced the amount of material of ten-fold and the experimentation time by a factor five compared to a conventional bulk approach. This set-up was used to explore functional synergies between proteins and polysaccharides as an example of application.
Published: 2020
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5. Monitoring food structure in plant protein gels during digestion: Rheometry and Small Angle Neutron Scattering studies

Author: Maja Napieraj, Annie Brûlet, Evelyne Lutton, Urielle Randrianarisoa, Adeline Boire, François Boué, LLB - Matière molle et biophysique (MMB), Laboratoire Léon Brillouin (LLB - UMR 12), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Paris-Saclay Food and Bioproduct Engineering (SayFood), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Mathématiques et Informatique Appliquées (MIA Paris-Saclay), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), and Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
Subjects: Protein, Bioengineering, Gastrointestinal digestion, Rheological properties, Small Angle Neutron Scattering, Applied Microbiology and Biotechnology, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, Canola proteins, Protein gels, Food Science
Abstract: International audience; We studied rheology and nanostructures (by Small Angle Neutron Scattering) of heat-set canola seed protein gels, containing cruciferin and napin, prepared at pH 8 and pH 11. We focused on gastric and intestinal digestion of 10 mm pieces, mimicking human gastro-intestinal tract. Stronger gels, prepared at pH 11 (above the isoelectric points (IEP), of both proteins), retained local folded and compact conformations, close to native ones. Preparation at pH 8 (below napin's IEP but above cruciferin's one), could destabilize conformations due to charge differences of the proteins. For preparation pH 8, proteins were almost unfolded, and the gel softer. In gastric digestion, modulus decreased for pH 8 gels, but surprisingly, increased for pH 11. We propose a competition between unfolding, increasing local interactions (hence the modulus), and enzymatic scission. Scission could be less efficient for pH 11 gels, with less unfolded proteins and higher crosslink density, hindering enzymatic diffusion. Additional interactions could result from crossing one or two IEPs, towards gastric pH 2. For intestinal digestion, the two gels behave similar (proteins re-compaction and modulus decrease). Beyond loss of submicronic connectivity, external erosion of the gel for largest times is observed, but less on SANS, which involves the center of the piece.
Published: 2022
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6. Contrasting Assemblies of Oppositely Charged Proteins

Author: William Nicholas Ainis, Adeline Boire, Véronique Solé-Jamault, Aurélie Nicolas, Richard Ipsen, Saïd Bouhallab, Section of Ingredient and Dairy Technology, Department of Food Science [Copenhagen] (UCPH FOOD), Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU)-Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, and 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)
Subjects: complexing, Models, Molecular, calorimétrie, complexation, interaction, Lactoglobulins, 02 engineering and technology, 010402 general chemistry, 01 natural sciences, ²-lactoglobulin, hétéroprotéine, Protein structure, Dynamic light scattering, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Electrochemistry, Animals, General Materials Science, Surface charge, Protein Structure, Quaternary, lysozyme, Spectroscopy, beta lactoglobuline, Range (particle radiation), Coacervate, assemblage de protéine, Chemistry, temperature, Isothermal titration calorimetry, Surfaces and Interfaces, 021001 nanoscience & nanotechnology, Condensed Matter Physics, turbidity, 0104 chemical sciences, Nap, protéine, Chemical physics, Brownian dynamics, Thermodynamics, Cattle, Muramidase, Protein Multimerization, protein, coacervation, 0210 nano-technology, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, turbidité
Abstract: Oppositely charged proteins can form soluble assemblies that under specific physical chemical conditions lead to liquid-liquid phase separation, also called heteroprotein coacervation. Increasing evidence suggests that surface charge anisotropy plays a key role in heteroprotein complexation, and coacervation. Here, we investigated complexation of an acidic protein, β-lactoglobulin (BLG), with two basic proteins, rapeseed napin (NAP) and lysozyme (LYS), of similar net charge and size but differing in surface charge distribution. Using turbidity measurements and isothermal titration calorimetry, we confirmed that LYS binds BLG as expected from previous studies. This interaction leads to two types of phase separation phenomena, depending on pH: liquid-solid phase separation in the case of strong electrostatic attraction and liquid-liquid phase separation for weaker attraction. More interestingly, we showed using dynamic light scattering that NAP interacts with BLG, resulting in formation of assemblies in the nanometer size range. The formation of assemblies was also evident when modeling the interactions using Brownian dynamics for both BLG + NAP and BLG + LYS. Similarly, to DLS, BLG and NAP formed smaller assemblies than BLG with LYS. The molecular details rather than the net charge of BLG and NAP may therefore play a role in their assembly. Furthermore, simulated BLG + NAP assemblies were larger than those experimentally detected by DLS. We discuss the discrepancy between experiments and simulations in relation to the limitations of modelling precisely the molecular characteristics of proteins.
Published: 2019
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7. Combining plant and dairy proteins in food colloid design

Author: Leonard M.C. Sagis, Claire C. Berton-Carabin, Fanny Guyomarc'H, Karin Schroën, Alain Riaublanc, Marie Hélène Famelart, Adeline Boire, Emma B.A. Hinderink, Valérie Gagnaire, Denis Renard, Saïd Bouhallab, Top Institute Food and Nutrition (TIFN), Wageningen University, Laboratory of Food Process Engineering, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Wageningen University, Laboratory of Physics and Physical Chemistry of Foods, Science et Technologie du Lait et de l'Oeuf (STLO), AGROCAMPUS OUEST, 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)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and Fromageries Bel S.A.,France, Nantes Me ́tropole and Re ́gion Pays de la Loire,France, the Netherlands Organisation for ScientificResearch and the Top-sector Agri&Food NWO projectnumber: ALWTF. 2016.001.
Subjects: Hierarchical structures, Protein aggregates, Physics and Physical Chemistry of Foods, WPI, Polymers and Plastics, LF, SPI, a-lactalbumin, Aqueous dispersion, Protein aggregation, Fluid interfaces, Colloid, 0302 clinical medicine, Colloid and Surface Chemistry, [SDV.IDA]Life Sciences [q-bio]/Food engineering, liquidliquid phase separation, lysozyme, Animal proteins, 0303 health sciences, Chemistry, LSPS, food and beverages, Multiphase systems, Surfaces and Interfaces, lactoferrin, b-lg, Protein solubility, Food systems, soy protein isolate, PPI, Context (language use), Hierarchical structures. Abbreviations NAP, b-lactoglobulin, 03 medical and health sciences, pea protein isolate, LYS, liquid-solid phase separation, Physical and Theoretical Chemistry, Food Process Engineering, Napin, 030304 developmental biology, VLAG, a-lac, Legume proteins, Food structuring, whey protein isolate, 030221 ophthalmology & optometry, LLPS, Non-protein components, Biochemical engineering, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
Abstract: International audience; The use of plant proteins to design colloidal food systems is a hot topic in the current context of the protein transition. However, replacing animal-derived proteins (in particular, dairy proteins) that have been traditionally used for this purpose by plant proteins is a challenge from various perspectives, and in particular, because of drastically different solubility and functionality. A possible route to mitigate these issues is to combine plant and dairy proteins, providing that their interactions can be understood from the molecular to the macroscopic scale. This review addresses the major advances that have occurred in the field of such blend-based systems, all the way from their behaviour in aqueous dispersions to their potential applications in gels, foams and emulsions.
Published: 2021
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8. Droplet microfluidics for food and nutrition applications

Author: Chloé Amine, Adeline Boire, Claire C. Berton-Carabin, Mélanie Marquis, Sébastien Marze, Rémy Cochereau, Denis Renard, Karin Schroën, Wageningen University and Research [Wageningen] (WUR), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Physiopathologie Animale et bioThérapie du muscle et du système nerveux (PAnTher), and Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
Subjects: Computer science, Microfluidics, biopolymers, Nanotechnology, Review, 02 engineering and technology, emulsions, Microparticles, 010402 general chemistry, 01 natural sciences, microgels, Biopolymers, nutrients, Basic research, [SDV.IDA]Life Sciences [q-bio]/Food engineering, TJ1-1570, interfacial properties, Mechanical engineering and machinery, Droplet microfluidics, Electrical and Electronic Engineering, Food Process Engineering, Reaction kinetics, VLAG, microparticles, 2. Zero hunger, Coalescence (physics), Interfacial properties, Microgels, Mechanical Engineering, Nutrients, 021001 nanoscience & nanotechnology, 0104 chemical sciences, microcapsules, Microcapsules, [CHIM.POLY]Chemical Sciences/Polymers, Control and Systems Engineering, Nutrient absorption, encapsulation, reaction kinetics, Research questions, Emulsions, Encapsulation, Applied science, 0210 nano-technology, Nutritional science
Abstract: International audience; Droplet microfluidics revolutionizes the way experiments and analyses are conducted in many fields of science, based on decades of basic research. Applied sciences are also impacted, opening new perspectives on how we look at complex matter. In particular, food and nutritional sciences still have many research questions unsolved, and conventional laboratory methods are not always suitable to answer them. In this review, we present how microfluidics have been used in these fields to produce and investigate various droplet-based systems, namely simple and double emulsions, microgels, microparticles, and microcapsules with food-grade compositions. We show that droplet microfluidic devices enable unprecedented control over their production and properties, and can be integrated in lab-on-chip platforms for in situ and time-resolved analyses. This approach is illustrated for on-chip measurements of droplet interfacial properties, droplet–droplet coalescence, phase behavior of biopolymer mixtures, and reaction kinetics related to food digestion and nutrient absorption. As a perspective, we present promising developments in the adjacent fields of biochemistry and microbiology, as well as advanced microfluidics–analytical instrument coupling, all of which could be applied to solve research questions at the interface of food and nutritional sciences.
Published: 2021
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9. Conformational Changes of Whey and Pea Proteins upon Emulsification Approached by Front-Surface Fluorescence

Author: Alain Riaublanc, Adeline Boire, Bérénice Houinsou-Houssou, Claude Genot, Emma B.A. Hinderink, Karin Schroën, Claire C. Berton-Carabin, Agrotechnology and Food Sciences, Food Process Engineering, Wageningen University and Research [Wageningen] (WUR), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and Fromageries Bel S.A.. Danone Nutricia. Pepsico Inc.. Unilever. Netherlands Organization for Scientific Research (NWO)
Subjects: 0106 biological sciences, absorption, 01 natural sciences, UV-visible, Fluorescence spectroscopy, Article, Protein structure, Adsorption, [CHIM.GENI]Chemical Sciences/Chemical engineering, plant protein, Whey, [SDV.IDA]Life Sciences [q-bio]/Food engineering, oil-water interface, right-angle fluorescence, UV−visible absorption, Food Process Engineering, VLAG, 2. Zero hunger, tryptophanyl, Chemistry, 010401 analytical chemistry, Tryptophan, Water, food and beverages, General Chemistry, Fluorescence, 0104 chemical sciences, Whey Proteins, Plant protein, UV-visible absorption, Vicilin, oil−water interface, Biophysics, Local environment, Emulsions, General Agricultural and Biological Sciences, 010606 plant biology & botany, Pea Proteins
Abstract: International audience; Proteins are widely used to stabilize emulsions, and plant proteins have raised increasing interest for this purpose. The interfacial and emulsifying properties of proteins depend largely on their molecular properties. We used fluorescence spectroscopy to characterize the conformation of food proteins from different biological origins (dairy or pea) and transformation processes (commercial or lab-made isolates) in solution and at the oil-water interface. The fourth derivative of fluorescence spectra provided insights in the local environment of tryptophan (Trp) residues and thus in the protein structure. In emulsions, whey proteins adsorbed with their Trp-rich region at the oil-water interface. Proteins in the commercial pea isolate were present as soluble aggregates, and no changes in the local environment of the Trp residues were detected upon emulsification, suggesting that these structures adsorb without conformational changes. The lab-purified pea proteins were less aggregated and a Trp-free region of the vicilin adsorbed at the oil-water interface.
Published: 2021
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10. New exploration of the γ-gliadin structure through its partial hydrolysis

Author: Hélène Rogniaux, Adeline Boire, Alexandre Giuliani, Denis Renard, Line Sahli, Véronique Solé-Jamault, Pierre Roblin, Centre National de la Recherche Scientifique - CNRS (FRANCE), Institut National Polytechnique de Toulouse - Toulouse INP (FRANCE), Institut national de recherche pour l'agriculture, l'alimentation et l'environnement - INRAE (FRANCE), Université Toulouse III - Paul Sabatier - UT3 (FRANCE), Laboratoire de Génie Chimique - LGC (Toulouse, France), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Département Caractérisation et Elaboration des Produits Issus de l'Agriculture (CEPIA), Fédération de Recherche Fluides, Energie, Réacteurs, Matériaux et Transferts (FERMAT), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées, Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), and Université de Toulouse (UT)
Subjects: Partial hydrolysis, Peptide, 02 engineering and technology, Intrinsically disordered proteins, Biochemistry, Gliadin, Domain (software engineering), 03 medical and health sciences, Protein Domains, Structural Biology, Enzymatic hydrolysis, Wheat storage proteins, Chymotrypsin, Génie chimique, Génie des procédés, Molecular Biology, Triticum, 030304 developmental biology, 2. Zero hunger, chemistry.chemical_classification, 0303 health sciences, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, Small-angle X-ray scattering, Hydrolysis, food and beverages, General Medicine, 021001 nanoscience & nanotechnology, 3D structure modelling, Template, chemistry, Biophysics, biology.protein, 0210 nano-technology
Abstract: International audience; The partial enzymatic hydrolysis of wheat gliadins constitutes an interesting tool to unravel their structural specificity. In this work, the structure and conformation of γ-gliadin were investigated through its limited chymotrypsic digestion. Using a combination of computational, biochemical and biophysical tools, we studied each of its N and C terminal domains. Our results reveal that γ-gliadin is a partially disordered protein with an unfolded N-terminal domain surprisingly resistant to chymotrypsin and a folded C-terminal domain. Using spectroscopic tools, we showed that structural transitions occured over the disordered N-terminal domain for decreasing ethanol/water ratios. Using SAXS measurements, low-resolution 3D structures of γ-gliadin were proposed. To relate the repeated motifs of the N-terminal domain of γ-gliadin to its structure, engineered peptide models PQQPY/F were also studied. Overall results demonstrated similarities between the N-terminal domain and its derived model peptides. Our findings support the use of these peptides as general templates for understanding the wheat protein assembly and dynamics.
Published: 2020
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11. Rubisco: A promising plant protein to enrich wheat-based food without impairing dough viscoelasticity and protein polymerisation

Author: Marie-Hélène Morel, Maude Ducrocq, Valérie Micard, Adeline Boire, Marc Anton, Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-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), 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)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut national de la recherche agronomique (National Institute of Agricultural Research), European Project: 2300176401(2013), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), European Project: 0720728(2007), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Université de Montpellier (UM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro - Montpellier SupAgro, and 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)
Subjects: Rubisco, Starch, Protein-protein interactions, General Chemical Engineering, Lysine, 01 natural sciences, chemistry.chemical_compound, 0404 agricultural biotechnology, Protein network, 0103 physical sciences, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Essential amino acid, 2. Zero hunger, chemistry.chemical_classification, Dynamic mechanical thermal analysis (DMTA), 010304 chemical physics, biology, Pea protein, RuBisCO, fungi, food and beverages, 04 agricultural and veterinary sciences, General Chemistry, 040401 food science, Gluten, Amino acid, [CHIM.POLY]Chemical Sciences/Polymers, chemistry, Biochemistry, Plant protein, Pea proteins, biology.protein, Food Science
Abstract: International audience; Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), a leaf protein, has an interesting amino acid profile and promising functional properties. Incorporated in wheat-based products, it would increase their protein content and improve their essential amino acid profile, particularly lysine. The impact of rubisco enrichment on wheat dough mechanical properties and protein-protein interactions was investigated using Dynamic Mechanical Thermal Analysis and Size-Exclusion chromatography, respectively. Experiments were also performed on gluten and pea protein enriched doughs as a comparison. Wheat doughs with increasing concentrations of rubisco, gluten or pea proteins (from 0 to 33% of total proteins) were prepared using a 2 g-mixograph at constant hydration. In contrast to pea proteins and gluten, rubisco does not reduce dough stiffening during heating, probably due to its own reactivity to temperature and to low competition with starch for water. Detailed analysis of protein interactions showed that rubisco is part of the gluten network formed during dough mixing through the establishment of weak and disulphide bonds. In addition, rubisco subunits form new covalent bonds during the heat treatment thereby increasing the concentration of SDS insoluble high molecular weight aggregates. These results suggest that rubisco actively participates in the formation of the dough protein network. The colocation of gluten and rubisco proteins on micrographs supports the hypothesis that they form a co-protein network.
Published: 2020
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12. Semi-permeable vesicles produced by microfluidics to tune the phase behaviour of encapsulated macromolecules

Author: Camille Noûs, Denis Renard, Rémy Cochereau, Adeline Boire, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Cogitamus Laboratory, INRAE, and Région Pays de la Loire.
Subjects: Materials science, Dispersity, Microfluidics, 02 engineering and technology, 010402 general chemistry, 01 natural sciences, Biomaterials, Colloid and Surface Chemistry, Phase (matter), [SDV.IDA]Life Sciences [q-bio]/Food engineering, Semipermeable membrane, Giant unilamellar vesicle, Vesicle, 021001 nanoscience & nanotechnology, Macromolecular assembly, 0104 chemical sciences, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Double emulsion, Liquid-liquid phase separation, Membrane, [CHIM.POLY]Chemical Sciences/Polymers, Chemical engineering, 0210 nano-technology, Macromolecule
Abstract: International audience; Understanding the dynamics of macromolecular assemblies in solution, such as Liquid-Liquid Phase Separation (LLPS), represents technologic and fundamental challenges in many fields. In cell biology, such dynamics are of great interest, because of their involvement in subcellular processes. In our study, we aimed to control the assembly of macromolecules in aqueous semi-permeable vesicles, that we named osmosomes, using microfluidics. We developed a microfluidic chip that allows for producting and trapping Giant Unilamellar Vesicles (GUVs) encapsulating macromolecules. This device also allows for modification of the composition of the inner phase and of the membranes of the trapped GUVs. The vesicles are produced from water-in-oil-in-water (w/o/w) double emulsions in less than 20 min after discarding the oil phase. They are highly monodisperse and their diameter can be modulated between 20 and 110 mu m by tuning the flow rates of fluid phases. Their unilamellarity is proofed by two techniques: (1) fluorescence quenching experiments and (2) the insertion of the alpha-hemolysin membrane protein pore. We demonstrate that the internal pH of osmosomes can be tuned in less than 1 min by controlling solvent exchanges through the alpha-hemolysin pores. The detailed analysis of the exchange kinetics suggests that the microfluidic chip provides an efficient pore formation due to the physical trapping of vesicles and the constant flow rate. Finally, we show a proof of concept for macromolecular assembly within osmosomes by pH-triggered LLPS of wheat proteins within a few minutes. (C) 2020 Elsevier Inc. All rights reserved.
Published: 2020
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13. Cartographie des sciences de l'alimentation au travers des publications académiques(1980-2018): vers quelles innovations les connaissances scientifiques orientent les légumineuses à graines en Europe ?

Author: Tristan Salord, Marie-Benoît Magrini, Guillaume Cabanac, Marie-Josephe Amiot-Carlin, Marc Anton, Adeline Boire, Jean-Michel Chardigny, Matteo Lascialfari, Valérie Micard, Christophe Nguyen-the, Stéphane Walrand, AGroécologie, Innovations, teRritoires (AGIR), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Recherche d’Information et Synthèse d’Information (IRIT-IRIS), Institut de recherche en informatique de Toulouse (IRIT), Université Toulouse 1 Capitole (UT1), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse 1 Capitole (UT1), Université Fédérale Toulouse Midi-Pyrénées, Université Toulouse III - Paul Sabatier (UT3), Marchés, Organisations, Institutions et Stratégies d'Acteurs (UMR MOISA), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre International de Hautes Etudes Agronomiques Méditerranéennes - Institut Agronomique Méditerranéen de Montpellier (CIHEAM-IAMM), Centre International de Hautes Études Agronomiques Méditerranéennes (CIHEAM)-Centre International de Hautes Études Agronomiques Méditerranéennes (CIHEAM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Direction Partenariat et Transfert pour l'Innovation (DPTI), Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Sécurité et Qualité des Produits d'Origine Végétale (SQPOV), Avignon Université (AU)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de Nutrition Humaine (UNH), Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Valérie Bonnet (Université de Toulouse 3 - Paul Sabatier), Annette Burguet (Université de Toulouse 3 - Paul Sabatier), Guillaume Cabanac (Université de Toulouse 3 - Paul Sabatier), Lucie Loubère (Université de Toulouse 3 - Paul Sabatier), Pascal Marchand (Université de Toulouse 3 - Paul Sabatier), Daniel Pélissier (Université de Toulouse 1 - Capitole), Gaël Plumecoq (Institut National de la Recherche Agronomique), Pierre Ratinaud (Université de Toulouse 2 - Jean Jaurès), Julie Renard (Université de Toulouse 2 - Jean Jaurès), Natacha Souillard (Université de Toulouse 3 - Paul Sabatier), Centre International de Hautes Études Agronomiques Méditerranéennes (CIHEAM)-Centre International de Hautes Études Agronomiques Méditerranéennes (CIHEAM)-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)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université Toulouse Capitole (UT Capitole), Université de Toulouse (UT)-Université de Toulouse (UT)-Université Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Toulouse Mind & Brain Institut (TMBI), Université Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Université de Toulouse (UT)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université Toulouse Capitole (UT Capitole), Université de Toulouse (UT), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Université de Montpellier (UM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro - Montpellier SupAgro, and 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)
Subjects: [INFO.INFO-TT]Computer Science [cs]/Document and Text Processing, scientometry, [SHS.SOCIO]Humanities and Social Sciences/Sociology, Grain legumes, agrifood research, bibliographic data, [SHS.ECO]Humanities and Social Sciences/Economics and Finance, scientometrics, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, Innovation Studies
Abstract: International audience; Pulses are essential for the sustainability transition of agrifood system. Their nutritional values allow animalbased protein intake reduction and contribute to healthy diets. Moreover, increasing their cultivation reduces fertilizers' uses and so, greenhouse gases emissions. But in high-income countries, and particularly in Europe, pulses consumption is very low. Previous works explained the mechanisms that led to a strong lock-in on pulses compared to the development of major crops, calling for stronger research and innovation to develop alternative food based on pulses. Food innovation remains strongly linked to the scientific knowledge and understanding how research output could sustain food innovation dynamics for sustainability is challenging. Mobilising scientometrics, STS Science and Technology Studies(STS) and Food Sciences and Technology(FST) scholars, the aim of this interdisciplinary study is to conduct a first map of the pulses FST. Describing what are the main issues tackled by FST on pulses will give to stakeholders a better understanding of the opportunities and expectations that could emerge in the development of a new food industry sector on pulses, as it will help academic research to identify specific field of interest to invest into. We considered 16 main pulses to build a dataset of more than 2,000 scholarly publications including at least one European author(articles, book, book chapters, and reviews) between 1980 and 2018, retrieved from the Web of Knowledge(Clarivate Analytics). Based on "natural language processing" clusterisation method we defined the main research themes structuring of the FST on pulses. We show that pulses have become a specific subfield of interest for FST in Europe, organized around of a great variety of subjects, and we focus on identifying the current gaps and opportunities to question science and innovation policies for pulses.
Published: 2020

14. Optimization of large-scale purification of omega gliadins and other wheat gliadins

Author: Rémy Cochereau, Véronique Solé-Jamault, Joëlle Davy, Sandra Denery-Papini, Adeline Boire, and Colette Larré
Subjects: chemistry.chemical_classification, Chromatography, Elution, Hydrophilic interaction chromatography, Size-exclusion chromatography, food and beverages, nutritional and metabolic diseases, Fractionation, Reversed-phase chromatography, digestive system, Biochemistry, Gluten, digestive system diseases, Electrophoresis, chemistry, Storage protein, Food Science
Abstract: Among wheat storage proteins, omega-gliadins display a singular amino acid sequence only composed by repetitive sequences. They have been described as a major wheat allergen and also contain T-cell epitopes implicated in coeliac disease. To study the structural and biophysical properties of omega-gliadins and other gliadins (e.g., gluten network formation, allergic response), highly purified and concentrated fractions are needed. In the present work, we used chromatography media screening to improve their fractionation. A S Ceramic Hyper D (Pall) resin was selected for its ability to concentrate omega-gliadins in the first elution peaks. Gamma- and beta-gliadins were then separated by hydrophobic interaction chromatography and eluted with an ethanol gradient. Alpha-gliadins were purified by gel filtration. Each fraction was characterized by electrophoresis and reverse phase HPLC. The developed preparative protocol enabled the purification of several grams of highly purified gliadins to the detriment of the yield.
Published: 2022
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15. Droplets-based millifluidic for the rapid determination of biopolymers phase diagrams

Author: Denis Renard, Mélanie Marquis, Joëlle Davy, Chloé Amine, Adeline Boire, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), French Agronomic Research National Institute (INRA), and region Pays de la Loire
Subjects: Work (thermodynamics), Materials science, [SDV]Life Sciences [q-bio], General Chemical Engineering, Analytical chemistry, 02 engineering and technology, 010402 general chemistry, 01 natural sciences, Colloid, Phase (matter), Polysaccharide, Phase diagram, chemistry.chemical_classification, Binodal, Coacervate, Protein, General Chemistry, Polymer, 021001 nanoscience & nanotechnology, 0104 chemical sciences, Liquid-liquid phase separation, chemistry, Droplets-based millifluidic, Ionic strength, Complex coacervation, 0210 nano-technology, Food Science
Abstract: Liquid-liquid phase separation is a phenomenon occurring spontaneously upon changing the physicochemical conditions of (bio-)polymers mixtures such as pH, ionic strength, total concentration, mixing ratio or temperature. The establishment of a phase diagram is a useful approach to highlight interactions and phase separation conditions of a mixture. Such approach generally performed in bulk is highly time and raw material consuming. In the present work, we developed a droplets-based millifluidic device for rapid phase diagram determination of liquid-liquid phase separated system. The proof of concept was first performed using a colloidal suspension of titanium dioxide (TiO2). The developed millifluidic device was then applied to a model protein-polysaccharide mixture made of beta-lactoglobulin (BLG) and Gum Arabic (GA) in water and at pH 4.2. In this model, a specific type of liquid-liquid phase separation occurs: complex coacervation. Biopolymers droplets of about 2.5 mu L of various compositions were generated to investigate the impact of total biopolymers concentration (0.1-5 wt %) and protein-polysaccharide mixing ratio (1:8 to 8:1). Initiation and suppression of phase separation were then evidenced through turbidity measurements within the droplets using image analysis. High similarities between cloud points probed using the millifluidic device and the binodal curve determined in bulk were found in the total biopolymers concentration range explored. Droplets-based millifluidic represents an efficient and highly versatile tool to probe liquid-liquid phase separation of various biopolymers mixtures.
Published: 2017
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16. Monitoring food structure during digestion using small-angle scattering and imaging techniques

Author: Evelyne Lutton, Thomas Bizien, Frédéric Jamme, Adeline Boire, Jade Pasquier, François Boué, Annie Brûlet, Javier Pérez, LLB - Matière molle et biophysique (MMB), Laboratoire Léon Brillouin (LLB - UMR 12), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Génie et Microbiologie des Procédés Alimentaires (GMPA), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), INRA (CEPIA Division), SOLEIL, LLB, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, and Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
Subjects: Materials science, Kinetics, Small angle neutron scattering, FOS: Physical sciences, 02 engineering and technology, Neutron scattering, Condensed Matter - Soft Condensed Matter, 010402 general chemistry, 01 natural sciences, law.invention, Plant protein, Colloid and Surface Chemistry, law, Elastic modulus, Gel, Small angle X ray scattering, Scattering, 021001 nanoscience & nanotechnology, Synchrotron, 0104 chemical sciences, Brillouin zone, [CHIM.POLY]Chemical Sciences/Polymers, Chemical physics, Deep UV synchrotron radiation fluorescence microscopy, Soft Condensed Matter (cond-mat.soft), Digestion, Small-angle scattering, 0210 nano-technology, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [PHYS.COND.CM-SCM]Physics [physics]/Condensed Matter [cond-mat]/Soft Condensed Matter [cond-mat.soft]
Abstract: Various studies have shown that food structure has an impact on digestion kinetics. We focus here on the effects of gastric and intestinal enzymes (in-vitro digestion) on two canola seed storage proteins, napin and cruciferin. To monitor structure effect we conducted experiments on gels of these proteins at different pHs, yielding different structures and elastic modulus. What is new is to get information on the mechanisms at the lowest scales, using imaging and radiation scattering at large facilities: Synchrotron fluorescence microscopy, X-Ray scattering, at SOLEIL synchrotron, and Small-Angle Neutron Scattering, at Laboratoire Leon Brillouin reactor. We can identify the mechanisms at each step and in two distinct scale ranges, observed simultaneously, the one of the individual protein scale and the one of the structure connectivity: • during gelation individual canola proteins are not deeply modified in comparison with their state in solution ; larger scale gel heterogeneity appears due to connectivity or aggregation • in the gastric step (up to 40 min): ○ at short scale (large q) we see that the proteins disintegration is much slowed down in gels than in solutions, particularly in the gastric phase; ○ at larger scales (low q), we see that the gel structure is also self-resistant to the action of the enzyme (pepsin). • in the intestinal step, such kinetics differences hold until major disintegration after no more than 15 min.
Published: 2020
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17. Role of protein conformation and weak interactions on γ-gliadin liquid-liquid phase separation

Author: Alexandre Giuliani, Véronique Solé-Jamault, Denis Renard, Adeline Boire, Line Sahli, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Département Caractérisation et Elaboration des Produits Issus de l'Agriculture (CEPIA), DISCO, Partenaires INRAE, regional programme 'Food for Tomorrow/Cap Aliment, Research, Education and Innovation in Pays de la Loire' - French Region Pays de la Loire, European Regional Development Fund (FEDER)European Union (EU), and Sahli, Line
Subjects: Models, Molecular, 0301 basic medicine, Phase transition, Protein Conformation, Liquid-Liquid Extraction, Static Electricity, lcsh:Medicine, Gliadin, Phase Transition, Article, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Protein structure, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Static electricity, Storage protein, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, lcsh:Science, Triticum, 2. Zero hunger, chemistry.chemical_classification, Intrinsically disordered proteins, Multidisciplinary, Aqueous solution, Ethanol, Chemistry, Hydrogen bond, lcsh:R, Proteins, nutritional and metabolic diseases, food and beverages, digestive system diseases, 030104 developmental biology, Ionic strength, Seeds, Biophysics, lcsh:Q, 030217 neurology & neurosurgery
Abstract: Wheat storage proteins, gliadins, were found to form in vitro condensates in 55% ethanol/water mixture by decreasing temperature. The possible role of this liquid-liquid phase separation (LLPS) process on the in vivo gliadins storage is elusive and remains to be explored. Here we use γ-gliadin as a model of wheat proteins to probe gliadins behavior in conditions near physiological conditions. Bioinformatic analyses suggest that γ-gliadin is a hybrid protein with N-terminal domain predicted to be disordered and C-terminal domain predicted to be ordered. Spectroscopic data highlight the disordered nature of γ-gliadin. We developed an in vitro approach consisting to first solubilize γ-gliadin in 55% ethanol (v/v) and to progressively decrease ethanol ratio in favor of increased aqueous solution. Our results show the ability of γ-gliadin to self-assemble into dynamic droplets through LLPS, with saturation concentrations ranging from 25.9 µM ± 0.85 µM (35% ethanol (v/v)) to 3.8 µM ± 0.1 µM (0% ethanol (v/v)). We demonstrate the importance of the predicted ordered C-terminal domain of γ-gliadin in the LLPS by highlighting the protein condensates transition from a liquid to a solid state under reducing conditions. We demonstrate by increasing ionic strength the role displayed by electrostatic interactions in the phase separation. We also show the importance of hydrogen bonds in this process. Finally, we discuss the importance of gliadins condensates in their accumulation and storage in the wheat seed.
Published: 2019
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18. Liquid-Liquid Phase Separation of Wheat Gliadins - Towards Physiological Conditions

Author: Denis Renard, Line Sahli, Véronique Solé-Jamault, Adeline Boire, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), and Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
Subjects: [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, Chromatography, Chemistry, Biophysics, Liquid liquid, ComputingMilieux_MISCELLANEOUS
Abstract: International audience
Published: 2019
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19. Associative properties of rapeseed napin and pectin: Competition between liquid-liquid and liquid-solid phase separation

Author: Alice Kermarrec, Adeline Boire, Chloé Amine, Denis Renard, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), French Agronomic Research National Institute (INRA), and Region Pays de la Loire
Subjects: Phase transition, food.ingredient, Rapeseed, Pectin, General Chemical Engineering, Mixing (process engineering), Polysaccharide, 01 natural sciences, 0404 agricultural biotechnology, food, complex coacervation, 0103 physical sciences, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Liquid liquid, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, chemistry.chemical_classification, pectin, 010304 chemical physics, Chemistry, digestive, oral, and skin physiology, 04 agricultural and veterinary sciences, General Chemistry, 040401 food science, Nap, Chemical engineering, napin, Plant protein, phase transition, droplets millifluidic, Food Science
Abstract: International audience; We investigated the assembly of a plant protein, rapeseed napin (NAP), mixed with a plant polysaccharide, highly methylated pectin (PEC). The optimum pH for NAP/PEC interactions was found at pH 4.0 for which the charge difference between the two biopolymers is the highest. Two types of phase transition were observed depending on pH and mixing ratios: liquid-solid and liquid-liquid phase separation. We showed that liquid-solid transition was favored by strong electrostatic attraction whereas liquid-liquid phase separation was promoted by weaker attraction. In addition, we highlighted a solid-to-liquid phase transition overtime for ratios with excess of proteins. We showed that polysaccharide charge neutralisation was a requisite for the transition as no rearrangement was observed when residual charges remained. The underlying mechanism leading to this transition remains to be explored. To the best of our knowledge, such solid-to-liquid transition has never been reported for protein-polysaccharide mixtures.
Published: 2019
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20. Soft Matter Approaches for Controlling Food Protein Interactions and Assembly

Author: Antoine Bouchoux, Saïd Bouhallab, Paul Menut, Stéphane Pezennec, Valérie Lechevalier, Thomas Croguennec, Denis Renard, Cécile Le Floch-Fouéré, Adeline Boire, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Ingénierie, Procédés, Aliments (GENIAL), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Ecole Nationale Supérieure Agronomique de Montpellier (ENSA M), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), 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), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)
Subjects: assembly, Protein Conformation, innovation alimentaire, interaction, protéine de l'aliment, 02 engineering and technology, 010402 general chemistry, 01 natural sciences, Structuring, food proteins, Phase Transition, Supramolecular assembly, structure de l'aliment, polymère, assemblage, [SDV.IDA]Life Sciences [q-bio]/Food engineering, protéine alimentaire, Soft matter, colloïde, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], colloid, 2. Zero hunger, business.industry, Food protein, assemblage de protéine, assemblage supramoléculaire, digestive, oral, and skin physiology, supramolecular structure, Models, Theoretical, 021001 nanoscience & nanotechnology, structure supramoléculaire, 0104 chemical sciences, texture de l'aliment, Food, Food products, Food processing, Biochemical engineering, Dietary Proteins, 0210 nano-technology, business, Protein concentration, physics, [PHYS.COND.CM-SCM]Physics [physics]/Condensed Matter [cond-mat]/Soft Condensed Matter [cond-mat.soft], [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, matrice alimentaire, Food Science
Abstract: International audience; Animal-and plant-based proteins are present in a wide variety of raw and processed foods. They play an important role in determining the final structure of food matrices. Food proteins are diverse in terms of their biological origin, molecular structure, and supramolecular assembly. This diversity has led to segmented experimental studies that typically focus on one or two proteins but hinder a more general understanding of food protein structuring as a whole. In this review, we propose a unified view of how soft-matter physics can be used to control food protein assembly. We discuss physical models from polymer and colloidal science that best describe and predict the phase behavior of proteins. We explore the occurrence of phase transitions along two axes: increasing protein concentration and increasing molecular attraction. This review provides new perspectives on the link between the interactions, phase transitions, and assembly of proteins that can help in designing new food products and innovative food processing operations.
Published: 2019
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21. Osmotic Compression of Anisotropic Proteins: Interaction Properties and Associated Structures in Wheat Gliadin Dispersions

Author: Adeline Boire, Marie-Hélène Morel, Paul Menut, Christian Sanchez, 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), 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), and 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)
Subjects: Osmosis, Equation of state, 02 engineering and technology, 010402 general chemistry, 01 natural sciences, Gliadin, Protein Structure, Secondary, Colloid, Rheology, Materials Chemistry, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Physical and Theoretical Chemistry, Protein secondary structure, Triticum, Quantitative Biology::Biomolecules, biology, Chemistry, Charge density, 021001 nanoscience & nanotechnology, 0104 chemical sciences, Surfaces, Coatings and Films, Crystallography, Virial coefficient, Chemical physics, Intramolecular force, biology.protein, Anisotropy, Thermodynamics, 0210 nano-technology, Protein Binding
Abstract: In this Article, we investigated the interaction properties of wheat gliadins, properties-that are at the basis of:their functionality in wheat grain and in food matrixes: We established the equation of state of our isolate by osmotic compression and characterized the concentration-induced structural transitions, from the secondary structure of proteins to the rheological properties. We evidenced three thermodynamical regimes corresponding to several structuring regimes. First, for Phi < 0.03, gliadins behave as repulsive colloids, with a positive second virial coefficient, arising presumably from their surface charge density and/or their, steric repulsion: No intermolecular interaction was detected by FT-IR, suggesting that proteins form a stable dispersion. In the second regime, the system becomes more easily compressible, i.e., less repulsive and/or more attractive.,It is associated with beta-the disappearance of beta-sheet intraramolecular structures of the proteins in favor of random coils/alpha-helix and intermolecular beta-sheet interactions. This coincides with the appearance of elasticity and the increase of the apparent viscosity. Finally, in the last regime, for Phi > 0.16, FT-IR spectra show that proteins are strongly interacting via intermolecular interactions. A correlation peak develops in SAXS, revealing a global order in the dispersion. Interestingly, the osmotic pressure applied to extract the solvent is higher than expected from a hard-sphere-like protein and we highlighted a liquid-like state at very high concentration (>450 g L-1) which:is in contrast with most proteins that form gel or glass at such concentration. In the discussion, we questioned the existence of supramolecular assemblies and the role of the solvation that would lead to this specific behavior.
Published: 2015
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22. Dynamics of liquid-liquid phase separation of wheat gliadins

Author: Paul Menut, Adeline Boire, Minne Paul Lettinga, Christian Sanchez, Marie-Hélène Morel, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), 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), Forschungszentrum Jülich GmbH | Centre de recherche de Juliers, Helmholtz-Gemeinschaft = Helmholtz Association, Université Catholique de Louvain = Catholic University of Louvain (UCL), Ingénierie, Procédés, Aliments (GENIAL), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, European Project: 262348,EC:FP7:INFRA,FP7-INFRASTRUCTURES-2010-1,ESMI(2011), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and 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)
Subjects: 0301 basic medicine, Spinodal decomposition, Kinetics, Ingénierie des aliments, Nucleation, lcsh:Medicine, 02 engineering and technology, SEED-STORAGE PROTEINS, Gliadin, Light scattering, Supramolecular assembly, 03 medical and health sciences, STAGE SPINODAL DECOMPOSITION, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Food engineering, Storage protein, grain de blé, Solubility, lcsh:Science, gliadine, TEMPERATURE, Triticum, KINETICS, chemistry.chemical_classification, SOLVENT, Science & Technology, Multidisciplinary, biology, Chemistry, lcsh:R, COLLOID-POLYMER MIXTURES, protéine de blé, GAMMA, 021001 nanoscience & nanotechnology, ANGLE LIGHT-SCATTERING, Multidisciplinary Sciences, Condensed Matter::Soft Condensed Matter, 030104 developmental biology, STATES, Chemical physics, Seeds, biology.protein, Science & Technology - Other Topics, lcsh:Q, 0210 nano-technology, ddc:600, BEHAVIOR
Abstract: During wheat seeds development, storage proteins are synthetized and subsequently form dense protein phases, also called Protein Bodies (PBs). The mechanisms of PBs formation and the supramolecular assembly of storage proteins in PBs remain unclear. In particular, there is an apparent contradiction between the low solubility in water of storage proteins and their high local dynamics in dense PBs. Here, we probe the interplay between short-range attraction and long-range repulsion of a wheat gliadin isolate by investigating the dynamics of liquid-liquid phase separation after temperature quench. We do so using time-resolved small angle light scattering, phase contrast microscopy and rheology. We show that gliadins undergo liquid-liquid phase separation through Nucleation and Growth or Spinodal Decomposition depending on the quench depth. They assemble into dense phases but remain in a liquid-like state over an extended range of temperatures and concentrations. The analysis of phase separation kinetics reveals that the attraction strength of gliadins is in the same order of magnitude as other proteins. We discuss the respective role of competing interactions, protein intrinsic disorder, hydration and polydispersity in promoting local dynamics and providing this liquid-like behavior despite attractive forces. ispartof: SCIENTIFIC REPORTS vol:8 issue:1 ispartof: location:England status: published
Published: 2018
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23. Unravelling the Contrasting Phase Behavior of Wheat Storage Proteins: How to Store Storage Proteins?

Author: Marie Helene Morel, Christian Sanchez, M. Paul Lettinga, Paul Menut, Adeline Boire, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), 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), Forschungszentrum Jülich GmbH, Université Catholique de Louvain (UCL), Ingénierie, Procédés, Aliments (GENIAL), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, 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), Université Catholique de Louvain = Catholic University of Louvain (UCL), Julich Forschungsctr, 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), and 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)
Subjects: chemistry.chemical_classification, 0303 health sciences, [SDV]Life Sciences [q-bio], Biophysics, technology, industry, and agriculture, food and beverages, protéine de blé, GeneralLiterature_MISCELLANEOUS, 03 medical and health sciences, 0302 clinical medicine, ComputingMethodologies_PATTERNRECOGNITION, protéine de stockage, chemistry, blé, Phase (matter), wheat, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Data_FILES, Storage protein, 030217 neurology & neurosurgery, 030304 developmental biology
Abstract: Unravelling the contrasting phase behavior of wheat storage proteins: how to store storage proteins?. 62nd Annual Meeting of the Biophysical-Society
Published: 2018
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24. Proteins for the future: A soft matter approach to link basic knowledge and innovative applications

Author: Alain Riaublanc, Marc Anton, Karima Laleg, Paul Menut, Valérie Lechevalier, Adeline Boire, Thomas Croguennec, Antoine Bouchoux, Vincenza Ferraro, Stéphane Pezennec, Saïd Bouhallab, Valérie Micard, Véronique Santé-Lhoutellier, Anne-Laure Chapeau, Denis Renard, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, 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), Qualité des Produits Animaux (QuaPA), Ingénierie, Procédés, Aliments (GENIAL), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, 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), European Project: 609398,EC:FP7:PEOPLE,FP7-PEOPLE-2013-COFUND,AGREENSKILLSPLUS(2014), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), 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), and 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)
Subjects: Computer science, Ingénierie des aliments, Nanotechnology, 02 engineering and technology, Industrial and Manufacturing Engineering, hétéroprotéine, caséine micellaire, aliment enrichi, 0404 agricultural biotechnology, Basic knowledge, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Food engineering, Soft matter, valorisation des sous produits, propriété de surface, gliadine, lysozyme, interaction intermoléculaire, 04 agricultural and veterinary sciences, General Chemistry, interaction protéine protéine, intermolecular interaction, 021001 nanoscience & nanotechnology, 040401 food science, Data science, innovation, protéine, new technology, encapsulation, surface properties, 0210 nano-technology, protein, Food Science
Abstract: • Protein interactions play a key role in determining the final structure and properties of products.
Published: 2018
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25. Cytoskeletal crosstalk: when three different personalities team up

Author: Magdalena Preciado López, Adeline Boire, Gijsje H. Koenderink, Florian Huber, and FOM Institute for Atomic and Molecular Physics (AMOLF)
Subjects: Intermediate Filaments, Cell migration, Cell Biology, Biology, Microtubules, Cell biology, Biomechanical Phenomena, Crosstalk (biology), Actin Cytoskeleton, [CHIM.POLY]Chemical Sciences/Polymers, Microtubule, Cell Movement, Animals, Cytoskeleton, Intermediate filament, Cell shape, Cell mechanics, Cell Shape, Actin
Abstract: Stichting voor Fundamenteel Onderzoek der Materie (FOM) - Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO) 110 -143 Marie Curie IEF fellowship; Cell shape and mechanics are determined by the interplay of three distinct cytoskeletal networks, made of actin filaments, microtubules, and intermediate filaments. These three types of cytoskeletal polymers have rather different structural and physical properties, enabling specific cellular functions. However, there is growing evidence that the three cytoskeletal subsystems also exhibit strongly coupled functions necessary for polarization, cell migration, and mechano-responsiveness. Here we summarize this evidence from a biophysical point of view, focusing on physical (direct) interactions between the cytoskeletal elements and their influence on cell mechanics and cell migration.
Published: 2014
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26. Phase behaviour of a wheat protein isolate

Author: Paul Menut, Christian Sanchez, Marie Helene Morel, Adeline Boire, Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), 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), 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), and 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)
Subjects: chemistry.chemical_classification, 010304 chemical physics, Linear polymer, [SDV]Life Sciences [q-bio], Protein isolate, Thermodynamics, food and beverages, 02 engineering and technology, General Chemistry, Composition (combinatorics), 021001 nanoscience & nanotechnology, Condensed Matter Physics, 01 natural sciences, chemistry, Phase (matter), 0103 physical sciences, Storage protein, Partition (number theory), Turbidity, 0210 nano-technology, Phase diagram
Abstract: We investigated the liquid-liquid phase separation of wheat storage proteins with molecular weight (MW) ranging from 25 kg mol(-1) to 300 kg mol(-1). We characterized the onset of the phase separation upon a temperature decrease by turbidity. The protein compositions at equilibrium after temperature quenches were additionally determined by size-exclusion-high performance liquid chromatography. We found that wheat proteins can be classified into two classes according to their phase behaviour. The partition of the proteins between the two phases depends on their MW above a critical size of 45 kg mol(-1). For those high MW proteins, we observed that the behaviour is similar to the one of neutral, linear polymers. Their partition and critical parameters are well described by Flory-Huggins theory. Proteins below 45 kg mol(-1), namely alpha-, beta- and gamma-gliadins, have similar interaction potentials under the physicochemical conditions tested. Their phase diagrams, characterized by a low value of critical volume fraction, are characteristic of long-range interactions. Wheat protein behaviour can resultantly be rationalized in a much simpler way than expected from their complex composition.
Published: 2013
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27. Elastic properties of extruded starchy melts containing wheat bran using on-line rheology and dynamic mechanical thermal analysis

Author: Laurent Forny, Heike P. Schuchmann, Stefan Palzer, Mario Horvat, Steffen Dattinger, Adeline Boire, Frédéric Robin, Department of Food Science and Technology, Nestlé Research Center, Institute of Process Engineering in Life Science, Karlsruhe Institute of Technology (KIT), 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), Nestlé Product Technology Center York, and Nestlé UK Ltd
Subjects: Expansion, Materials science, 030309 nutrition & dietetics, Starch, Wheat flour, Cereals, DMTA, 03 medical and health sciences, chemistry.chemical_compound, 0404 agricultural biotechnology, Rheology, Shear viscosity, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Composite material, Thermal analysis, 0303 health sciences, Bran, Extrusion, digestive, oral, and skin physiology, Elastic properties, food and beverages, 04 agricultural and veterinary sciences, Dynamic mechanical analysis, 040401 food science, Fibers, chemistry, On-line rheometry, Glass transition, Food Science
Abstract: Addition of wheat bran reduces the expansion volumes of extruded cereals. This may be explained by the influence wheat bran has on the elastic properties of the melt. The elastic properties of extruded refined wheat flour supplemented with wheat bran were investigated using a complementary on-line and an off-line rheological technique. The Bagley pressure (end pressure), reflecting extensional properties of the melt, was measured on-line using the orifice die method (dies with different lengths). The storage modulus of the extruded samples was measured using dynamic mechanical thermal analysis (DMTA). Increasing the bran concentration to an intermediate level significantly increased the Bagley pressure likely due to a reduced mobility of starch molecules. Further increasing the bran concentration significantly decreased the Bagley pressure. This might be caused by physical rupture of the melt at the die exit due to the low adhesion properties between starch and bran particles. This change in Bagley pressure indicates that the elastic properties of the composite melt may be reduced by bran particles. The storage modulus measured by DMTA was decreased when increasing the bran concentration, further supporting a potential decrease of the elastic properties of the melt with bran.
Published: 2012
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28. Osmotic Compression of Anisotropic Proteins: InteractionProperties and Associated Structures in Wheat Gliadin Dispersions.

Author: Adeline Boire, Paul Menut, Marie-Hélène Morel, and Christian Sanchez
Published: 2015
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28 results on '"Adeline Boire"'

1. Crop diversity used in branded products with focus on legume species worldwide

2. Sorghum protein ingredients: Production, compositional variability and enhancement of aqueous dispersibility through homogenization

3. Droplet Microfluidics for Food and Nutrition Applications

4. Optimization of a Droplet-Based Millifluidic Device to Investigate the Phase Behavior of Biopolymers, Including Viscous Conditions

5. Monitoring food structure in plant protein gels during digestion: Rheometry and Small Angle Neutron Scattering studies

6. Contrasting Assemblies of Oppositely Charged Proteins

7. Combining plant and dairy proteins in food colloid design

8. Droplet microfluidics for food and nutrition applications

9. Conformational Changes of Whey and Pea Proteins upon Emulsification Approached by Front-Surface Fluorescence

10. New exploration of the γ-gliadin structure through its partial hydrolysis

11. Rubisco: A promising plant protein to enrich wheat-based food without impairing dough viscoelasticity and protein polymerisation

12. Semi-permeable vesicles produced by microfluidics to tune the phase behaviour of encapsulated macromolecules

13. Cartographie des sciences de l'alimentation au travers des publications académiques(1980-2018): vers quelles innovations les connaissances scientifiques orientent les légumineuses à graines en Europe ?

14. Optimization of large-scale purification of omega gliadins and other wheat gliadins

15. Droplets-based millifluidic for the rapid determination of biopolymers phase diagrams

16. Monitoring food structure during digestion using small-angle scattering and imaging techniques

17. Role of protein conformation and weak interactions on γ-gliadin liquid-liquid phase separation

18. Liquid-Liquid Phase Separation of Wheat Gliadins - Towards Physiological Conditions

19. Associative properties of rapeseed napin and pectin: Competition between liquid-liquid and liquid-solid phase separation

20. Soft Matter Approaches for Controlling Food Protein Interactions and Assembly

21. Osmotic Compression of Anisotropic Proteins: Interaction Properties and Associated Structures in Wheat Gliadin Dispersions

22. Dynamics of liquid-liquid phase separation of wheat gliadins

23. Unravelling the Contrasting Phase Behavior of Wheat Storage Proteins: How to Store Storage Proteins?

24. Proteins for the future: A soft matter approach to link basic knowledge and innovative applications

25. Cytoskeletal crosstalk: when three different personalities team up

26. Phase behaviour of a wheat protein isolate

27. Elastic properties of extruded starchy melts containing wheat bran using on-line rheology and dynamic mechanical thermal analysis

28. Osmotic Compression of Anisotropic Proteins: InteractionProperties and Associated Structures in Wheat Gliadin Dispersions.

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28 results on '"Adeline Boire"'

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