Publications by authors named "Alain Riaublanc"

(1) Background: Adding white vinegar to the batter of a sponge cake without biological fermentation requires the effects of acidification on the batter to be checked, in particular concerning batter-to-crumb transition. (2) Methods: µDSC analyses were carried out on three batters formulated from flour, colza oil, salt, carrot, and water with or without the addition of white vinegar. (3) Results: Wheat, chickpea, and quinoa starches had gelatinization temperatures (T) of 60.

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This work is part of a study aiming to design a high-throughput foaming microsystem. The main focused field of application is the food industry. With the objective of improving the design of the microdevice, the effects of the geometry and the nature of the liquid base are presently investigated through visualizations of the flow typology of bubbles trains, aiming to expand the knowledge on key parameters that lead to an improved gas breakup.

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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.

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Lutein is a xanthophyll carotenoid provided exclusively by the diet, that has protective functions and beneficial effects on human health. Supplementation in lutein is necessary to reach the recommended daily dietary intake. However, the introduction of lutein into foods and beverages is a real challenge since this lipophilic nutrient has a poor aqueous solubility and a low bioavailability.

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The digestion of plant protein is highly dependent on multiple factors, with two of the most important being the protein source and the food matrix. The present study investigated the effects of these two factors on the digestion of seitan (a wheat-based food), tofu, soya juice, and a homemade emulsion of soy oil and water that was stabilised with pea protein. The four plant matrices and their respective protein isolates/concentrates (wheat gluten, soya protein, pea protein) were subjected to in vitro static digestion following the INFOGEST consensus protocol.

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The biological membrane surrounding fat globules in milk (milk fat globule membrane; MFGM) is an interface involved in many biological functions and interactions with the surrounding proteins or lipolytic enzymes in the gastro-intestinal tract during digestion. The MFGM exhibits lateral heterogeneities resulting from the different phase states and/or head-group charge of the polar lipids, which were both hypothesized to drive interaction with the casein micelles that is the major milk protein assembly. Atomic force microscopy (AFM) imaging was used to track the interactions of casein micelles with hydrated supported lipid bilayers of different composition, phase state and charge.

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Background: Human milk composition analysis seems essential to adapt human milk fortification for preterm neonates. The Miris human milk analyzer (HMA), based on mid-infrared methodology, is convenient for a unique determination of macronutrients. However, HMA measurements are not totally comparable with reference methods (RMs).

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We report on the structure of whey protein aggregates formed by a short heating coupled to shear at high temperatures (80-120) and neutral pH in scale-up processing conditions, using gel filtration chromatography, light scattering, small angle neutron scattering, and cryogenic transmission electron microscopy. The results are interpreted in terms of coexistence of residual non-aggregated proteins and aggregates. The characteristics of aggregates such as the size, the aggregation number and the shape evidence two different morphologies.

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Model systems composed of tristearin in solid state and tricaprin in liquid state with different solid-fat content (SFC) and storage time have been investigated by relaxation NMR and NMR diffusometry. The T(2) relaxation of the tricaprin in the melt exhibited a bimodal distribution as previously observed. The SFC had a major effect on the T(2) relaxation.

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We report on dispersions of fatty acid-lysine salts in aqueous solutions which are further used to produce foams. The alkyl chain length is varied from dodecyl to stearic. In aqueous solutions, the lysine salt of the dodecyl chain yields an isotropic solution, probably micelles, whereas for longer alkyl chains, vesicles formed but crystallized upon resting at room temperature or when kept at 4 degrees C.

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We investigated the structure of heat-induced assemblies of whey globular proteins using small angle neutron scattering (SANS), static and dynamic light scattering (SLS and DLS), and cryogenic transmission electron microscopy (Cryo-TEM). Whey protein molecules self-assemble in fractal aggregates with a structure density depending on the electrostatic interactions. We determined the static and dynamic properties of interfacial layer formed by the protein assemblies, upon adsorption and spreading at the air-water interface using surface film balance and interfacial dilatational rheology.

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Low density lipoproteins (LDL) from egg yolk have a classical structure of lipoprotein with a core of neutral lipids surrounded by a monolayer of apoproteins and phospholipids. This structure collapses during adsorption and all constituents spread at the interface. To understand better the nature of the interactions between apoproteins and lipids at the interface, we have deposited LDL at an air-water interface and analysed the isotherms during their compression on a Langmuir trough.

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The structure of aggregates and gels formed by heat-denatured whey protein isolate (WPI) has been studied at pH 7 and different ionic strengths using light scattering and turbidimetry. The results were compared with those obtained for pure beta-lactoglobulin (beta-Lg). WPI aggregates were found to have the same self-similar structure as pure beta-Lg aggregates.

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We have studied the structure of films made by low density lipoproteins (LDL) from hen egg yolk, which are composed of apoproteins, neutral lipids and phospholipids. These LDL have been deposited on air-water interface to form a monolayer which has been compressed to measure an isotherm using Langmuir balance. This isotherm presented three transitions (neutral lipid (surface pressure, pi=19 mN/m), apoprotein-lipid (pi=41 mN/m) and phospholipid (pi=51 mN/m) transitions).

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The chemical composition and crystallisation properties of milk fat and its primary fractions, obtained by dry fractionation at 21 degrees C, were investigated. The solid fraction (stearin) and the liquid fraction (olein) displayed a different triacylglycerol (TG) composition. Stearin fraction was enriched in long-chain fatty acids, whereas olein fraction was enriched in short-chain and unsaturated fatty acids.

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Hen egg yolk is largely used as an ingredient in food emulsions due to its exceptional emulsifying properties. Low-density lipoproteins (LDL) are the main egg yolk constituents and the most important contributors to yolk emulsifying properties. To better understand the LDL adsorption mechanism and spreading at the interface, we extracted and studied LDL at different interfaces.

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The water self-diffusion coefficients in casein matrixes were measured using a pulsed field gradient spin-echo nuclear magnetic resonance technique (PFG-SE NMR). The dependence of the water self-diffusion coefficient on the casein concentration and the aqueous phase composition is reported in both a rehydrated native phosphocaseinate dispersion and a concentrated casein retentate. A model has been proposed to explain the different behavior of the water self-diffusion coefficient in the two casein systems.

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The structural and quantitative variability of caprine alpha(s1)-casein induced by the extensive polymorphism recorded at the corresponding locus strongly influences the composition (proteins as well as lipids) and the technological behaviour of milk. Immuno-histo-chemistry studies coupled with electron microscopy analysis have shown that a dysfunction exists in the intracellular transport of caseins when alpha(s1)-casein is lacking. Casein accumulation in the endoplasmic reticulum leads to a dilation of the cisternae that could disturb the whole secretion process (including lipids).

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