Abstract
Durum wheat gluten proteins are essential for pasta quality. Glutenin polymers undergo solubilization mechanisms during pasta processing. This study aims to investigate gluten proteins insolubilisation kinetics during a resting period applied to extruded. The goal is to investigate the contribution of time related recovery of large glutenin polymers and temperature related formation of glutenin cross-linked aggregates in the pasta quality. Extruded pasta were rested for 120 min at 20, 30 or 40 °C prior drying at high temperature (90 °C). Glutenins insolubilisation induced by resting and drying was assessed from the SE-HPLC elution profiles of the SDS-soluble proteins from fresh, rested and dried pasta. Final pasta were characterized for their organoleptic (color, surface roughness) and physical (diameter, cooking time, viscoelasticity index) properties, before and after cooking. Pasta quality is discussed in relation with the gluten network structure and the impact of resting time. Resting of freshly extruded pasta extrusion leads to spontaneous insolubilisations of glutenins by creation of weak interactions. High temperature drying induces a strong drop of solubility of all gluten protein fractions by creation of covalent bonds, impacting equally rested and not rested pasta. Dry and cooked pasta organoleptic and physical properties are not significantly impacted by a resting time.
Highlights
33 34 Durum wheat pasta is a traditional and world-wide consumed cereal food
The objective of the present study is to investigate the impact of time during a resting period after extrusion and during drying stage, on protein insolubilisation kinetics in extruded pasta
Pasta resting after extrusion leads to gluten protein insolubilisation reactions by creation of weak interactions
Summary
33 34 Durum wheat pasta is a traditional and world-wide consumed cereal food. Pasta structure relies on physical and chemical interactions that are established in between starch and proteins during pasta making. Pasta processing consists in a succession of several unit operations: hydration, mixing, extrusion, and drying. The agglomerates are structured into pasta by single screw extrusion at low temperature. During the first mixing step, the wet agglomerates of semolina undergo shear deformation, that induces protein hydration and unfolding allowing for the formation of a continuous gluten network enclosing the starch granules (Guerrero et al, 2014). Wheat gluten proteins (12 to 15% of pasta dry weight) are constituted of monomeric gliadins and polymeric glutenins (Shewry & Halford, 2002). Both are soluble in sodium dodecyl sulfate (SDS) buffer, fully for the former and partly for the latter. The gluten protein network allows pasta to resist to starch swelling mechanisms that are promoted by the final cooking stage and promote a firmer texture and a better surface aspect of cooked pasta
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