文摘
Gliadin and glutenin proteins with 10, 20, 30 and 40% of glycerol were compression molded into films (130 °C) and evaluated for protein polymerization, β-sheet structure and nano-structural morphology. Here, for the first time we show how different amounts of glycerol impact the nano-structure and functional properties of the gliadin and glutenin films. Most polymerized protein was found in the gliadin films with 20 and 30% glycerol, and in all the glutenin films (except 10%), by RP-HPLC. A β-sheet-rich protein structure was found to be high in the 10 and 20% glycerol gliadin films, and in the 20 and 30% glycerol glutenin films by FT-IR. Glycerol content of 20, 30 and 40% impacted the nano-structural morphology of the gliadin glycerol films observed by SAXS, and to a limited extent for 10 and 20% glycerol gliadin films revealed by WAXS. No ordered nano-structure was found for the glutenin glycerol films. The 20%, 30% and 40% glycerol films were the most tunable for specific mechanical properties. For the highest stiffness and strength, the 10% glycerol protein films were the best choice.