Abstract

Gliadins were electrospun into ultrafine fibrous membrane-like materials to evaluate their processability and suitability as bio-absorbents. From a wide range of tested protein concentrations and processing conditions, 15 and 20% protein solutions were optimal to produce uniform fibers with sizes <1 μm. The results showed that the 20% gliadin solution produced uniform round fibers, while 15% gliadin solution resulted in formation of diverse morphologies such as round and flat-ribbon shaped fibers. Importantly, post-heat treatment of fibrous materials at 130 °C for 2 h increased crosslinking of gliadin protein and improved functionality of fibers. Heat-treatment induced formation of higher amounts of α-helices and random coils, though no change in β-sheets were observed. With post heat-treatment, the fibrous gliadin materials indicated crosslinking of proteins by inter and intramolecular disulphide, hydrogen bonding and other weaker protein interactions. The newly fabricated gliadin fibrous material demonstrated certain stability and ability to absorb and “lock” defibrinated sheep blood, suggesting a support from submicron sized structural morphology of the material. For further development steps of gliadin-based fibrous materials, new efforts are needed in modification of gliadins to maintain the ultrafine structures and improve their strength in order to explore them as bio-absorbents or even scaffolds.

Keywords

Electrospinning; Gliadin fibers; Protein crosslinking; Protein structure; Absorbents; Blood absorption

Published in

Reactive and Functional Polymers
2022, volume: 181, article number: 105444

Authors' information