Monitoring of the molecular motions and secondary structures of gliadin (Gli) and glutenin (Glu) in blends with 10, 20, 30, and 40% glycerol was performed by solid-state (SS) and time domain (TD) NMR spectroscopy. Increasing the glycerol content increased the relative amount of β-sheets and disordered structures, while decreasing α-helices in Gli/Glu–glycerol blends studied by 13C CPMAS NMR. For ≥20% glycerol samples, the protein side-chain mobility increased similarly for Gli and Glu. A higher proportion of α-helices versus β-sheets was found in Gli-glycerol blends compared with Glu–glycerol blends. Glycerol acted as “immobilized” in 10–20% glycerol Gli samples and was found mainly “free” in 30 and 40% glycerol Gli/Glu samples. During temperature experiments, 30 and 40% glycerol amounts impacted the dynamic molecular behavior of the Gli and Glu proteins differently than lipids, as observed by TD-NMR. The combination of TD-NMR together with SS-NMR showed details of the dynamic molecular variations in Gli/Glu protein structure and are promising techniques to monitor the molecular dynamics of plasticized proteins.
|Tidskrift||Journal of Polymer Science, Part B: Polymer Physics|
|Status||Published - 2018 maj 1|
- Fysikalisk kemi