Abstract
Gliadin and glutenin proteins with 10, 20, 30 and 40% of glycerol were compression molded into films (130 degrees C) and evaluated for protein polymerization, beta-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 beta-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.
| Original language | English |
|---|---|
| Pages (from-to) | 2998-3007 |
| Number of pages | 10 |
| Journal | ACS Sustainable Chemistry and Engineering |
| Volume | 4 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2016 |
Keywords
- Protein morphology
- Protein film
- Glycerol content
- Polymerization
- SAXS
- WAXS
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