Durum Wheat Couscous Grains: An Ethnic Mediterranean Food at the Interface of Traditional Domestic Preparation and Industrial Manufacturing.

Couscous is the product prepared from durum wheat semolina that agglomerates by adding water and undergoes physical and thermal treatment. Couscous is a traditional food from Mediterranean countries consumed for many centuries. Between ancestral domestic practices and industrial performance, the diversity of methods for couscous processing meets the needs of different consumers, whether they are concerned about preserving family culinary traditions or discovering innovative foods that respond to changing consumption patterns. In this work, we present the story of durum wheat couscous through several complementary visions and approaches: a "historical and societal" approach to discover the origins of couscous, its migrations and its unifying role in Mediterranean societies; a "physicochemical" approach to describe the role of wheat components at the heart of couscous grains; a "technological" approach to compare domestic and industrial production of couscous; a "food science" approach to understand organoleptic characteristics of couscous grains; and a "consumer" approach to understand the motivations associated with the consumption of couscous.

Emulsifying properties of Acacia senegal gum: Impact of high molar mass protein-rich AGPs.

The impact of high molar mass protein-rich arabinogalactan-proteins (AGPs) on emulsifying properties of Acacia senegal gums were studied using reconstituted gums obtained with two distinct fractions: one containing these specific high molar mass AGPs and the other protein-poor low molar mass AGPs. To produce and stabilize limonene emulsions, the experimental design emphasized not only the role of high molar mass protein-rich AGPs, but also the importance of high total concentration. At low protein contents, reconstituted gums required a slightly higher content in high molar mass protein-rich AGPs than original A. senegal gum, that confirmed the role of low molar mass protein-rich AGPs in the adsorption at interfaces. The comparison of the creaming index between original and reconstituted gums as well as the monitoring of instability phenomena by turbiscan up to 30 days clearly demonstrated the prevalent impact of the bulk apparent viscosity in the long-term stability of emulsions.

Effect of dairy powder rehydration state on gel formation during yogurt process.

Protein fortification and solubilisation into the milk base are important parameters enhancing yogurt texture. In this study, the milk base prepared from reconstituted skim milk powder was fortified with 2% of 'aged' (1 year old) or 'fresh' micellar casein (MC) powder. Micellar casein powders were left to rehydrate at 20°C for different times (5 or 180, 300, 480, 900 or 1440 min) before acidification with glucono-delta-lactone. The rehydration of the MC powders into milk was monitored with a granulo-morphometer equipment, thus, for the first time, allowing the elucidation of MC rehydration process into an opaque environment such as milk. Whereas the gel point was delayed proportionally to the powder rehydration length, the storage modulus appears unaffected. Besides, the gelation onset was not altered by the powder age.

Multiscale characterization of individualized beta-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions.

Aqueous dispersions of demineralized beta-lactoglobulin (beta-lg) were held at 85 degrees C for 15 min at a constant protein concentration of 1 wt % in the pH range of 3.0-7.0. This led to denatured protein content ranging from 20% (pH 3.0) to 90% (pH 5.0). The protein aggregates formed were characterized as to their stability to sedimentation (turbidity), morphology, size, surface charge, ANS surface hydrophobicity, and content in accessible thiol groups. Additionally, the changes in secondary structures of the protein upon heating were followed by Fourier transform infrared spectroscopy (FTIR). Stable dispersions (no sedimentation for 10 min) of individualized beta-lg microgels were obtained at specific pH 4.6 and 5.8, corresponding to an aggregation yield of about 80%. The width of the pH region leading to these microgels was 0.3 pH unit below or above the two specific pH values. Microgels were characterized by a spherical shape and remarkably low polydispersity in size (<0.2). Their z-average hydrodynamic diameter determined by dynamic light scattering (DLS) was between 160 and 220 nm, and their zeta-potential was +30 or -40 mV, depending on the initial pH before heating. Microgels obtained at pH 4.6 displayed a lower binding capacity for ANS and a lower content of accessible thiol groups as compared to those obtained at pH 5.8. Both types of microgels might therefore differ in their internal and interfacial structures. Between pH 4.6 and 5.8, large sedimenting protein particulates were obtained, whereas soluble aggregates were formed at pH <4.6 or >5.8. Interestingly, DLS experiments showed that before heating, beta-lg was mainly present in an oligomeric state at pH 4.6 and 5.8. This result was confirmed by FTIR measurements indicating the stronger contribution of the 1616-1624 cm(-1) spectral band corresponding to intermolecular beta-sheets in the pH range of 4.0-6.0. Upon heating, FTIR spectroscopy revealed that individualized microgels were obtained under pH conditions where a balance between attractive forces arising from protein unfolding leading to the formation of intermolecular beta-sheets (1616-1624 cm(-1 )band) and the repulsive electrostatic forces due to the initial protein net charge was achieved.