Mechanical Properties and Network Structure of Wheat Gluten Foams

Abstract

This Article reports the influence of the protein network structure on the mechanical properties of foams produced from commercial wheat gluten using freeze-drying. Foams were produced from alkaline aqueous solutions at various gluten concentrations with or without glycerol, modified with bacterial cellulose nanosized fibers, or both. The results showed that 20 wt % glycerol was sufficient for plasticization, yielding foams with low modulus and high strain recovery. It was found that when fibers were mixed into the foams, a small but insignificant increase in elastic modulus was achieved, and the foam structure became more homogeneous. SEM indicated that the compatibility between the fibers and the matrix was good, with fibers acting as bridges in the cell walls. IR spectroscopy and SE-HPLC revealed a relatively low degree of aggregation, which was highest in the presence of glycerol. Confocal laser scanning microscopy revealed distinct differences in HMW-glutenin subunits and gliadin distributions for all of the different samples.

Non-celiac gluten hypersensitivity Munish Ashat, Rakesh Kochhar

“…The two main constituents of gluten protein are gliadins and glutenins which are resistant to gastric digestion and increase intestinal permeability causing malabsorption and inhibition of cell growth and apoptosis. 15 These features are consistent with CD, a well know gluten sensitivity disorder. Media and general public interest in this topic is overwhelming.…”

Biobased Materials Production from Biodiesel Residuals of Rapeseed

“…From the different treatments evaluated in the present study, glycerol addition seemed to be the most important for changing the tensile properties of the material, followed by the pressing temperature. Addition of glycerol has been found to increase protein polymerisation in gluten foam materials [21].…”

Structural Changes of Gluten/Glycerol Plastics under Dry and Moist Conditions and during Tensile Tests

“…25 WG is a protein blend consisting of two main components: gliadin (monomeric protein) and glutenin (polymeric protein). Gliadin contributes mainly to the viscous behavior of the material, while glutenin influences mainly the elasticity 18,26 . Typically, the pristine WG has no regular self-assembled structure, but denatured aggregates can develop at an elevated temperature, especially in the presence of glycerol.…”

“…25,27,28 Besides the plasticizers, additives, such as acids, bases and urea, have been used to improve the processability of WG. 26,[29][30][31] Interestingly, new tetragonal-packed and HCP nanostructures were discovered in the WG with NaOH and ammonium hydroxide (AH) 28 . A similar HCP structure was also reported in the presence of urea, which act as a combined protein denaturant and plasticizer.…”