Electrospinning of Prolamin Proteins in Acetic Acid: The Effects of Protein Conformation and Aggregation in Solution

The electrospinnability of hordein and gliadin from acetic acid solutions is demonstrated and compared to that of zein. The relation between protein conformations in solution and the properties of post‐spun fibers are studied by means of CD, FTIR, TEM, DLS, viscosity measurements, SEM, and mechanical testing. The results show that both electrospinnability of the proteins and mechanical properties of post‐spun fibers are significantly influenced by solution protein conformations. Ultrafine fibers are fabricated at optimized concentrations, while large compact aggregates caused by hydrophobic interactions have a negative effect on the formation of continuous protein fibers. Moreover, hordein fibers show a lower cytotoxicity than gliadin and zein fibers. magnified image