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Research on the electrospinning of nanofibers has increased in recent years because of the number of potential applications in different areas, ranging from technical textiles (e.g., filters, composite reinforcements, and protective fabrics) to biomedical commodities and devices such as bandages, membranes, bioactive surfaces, and porous substrates for tissue engineering, for which biocompatible polymers play an essential role. In this work, wool keratin/poly(ethylene oxide) nanofibers were electrospun from aqueous solutions of polymer blends under different operating conditions. The filaments were characterized with scanning electron microscopy, Fourier transform infrared, and differential scanning calorimetry analyses and compared with films of the same materials produced via casting with the aim of investigating structural changes due to the electrospinning process.

A wool fiber sample was submitted to chemical-free steam explosion in view of potential exploitation of keratin-based industrial and farm wastes. Fiber keratin was converted into a dark-yellow sludge that was submitted to phase separation by filtration, centrifugation, and precipitation of the soluble materials from the supernatant liquid. The resulting products, when compared with the original wool, showed the extent of disruption of the histology structure, reduction of the molecular weight to water-soluble peptides and free amino acids, and change of the structure of the remainder of the protein associated with breaking of disulfide bonds and decomposition of the high-sulfur-content protein fraction.

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Keratin regenerated from wool and fibroin regenerated from silk were mixed in different proportions using formic acid as the common solvent. Both solutions were cast to obtain films and electrospun to produce nanofibers. Scanning electron microscopy investigation showed that, for all electrospun blends (except for 100% keratin where bead defects are present), the fiber diameter of the mats ranged from 900 (pure fibroin) to 160 nm (pure keratin). FTIR and DSC analysis showed that the secondary structure of the proteins was influenced by the blend ratios and the process used (casting or electrospinning). Prevalence of beta-sheet supramolecular structures was observed in the films, while proteins assembled in alpha-helix/random coil structures were observed in nanofibers. Higher solution viscosity, thinner filaments, and differences in the thermal and structural properties were observed for the 50/50 blend because of the enhanced interactions between the proteins.

Wool fibers were submitted to “green hydrolysis” with superheated water in a microwave reactor, in view of the potential exploitation of keratin-based industrial and stock-farming wastes. The liquid fraction was separated by filtration from the solid fraction, which consists mainly of small fragments of wool fibers and other insoluble protein aggregates. The liquid fraction contains free amino acids, peptides and low molecular weight proteins, with a small amount of cystine and lanthionine, and has a different secondary structure when compared with keratins extracted from wool via reductive or oxidative methods. Cleavage of the cystine disulfide bonds without the use of harmful, often toxic, reductive or oxidative agents allows the extraction of protein material from keratin wastes, offering the possibility of larger exploitation and valorization.