Keratin is widely recognized as a high-quality renewable protein resource for biomedical applications. A large amount of rabbit hair waste is produced in textile industries, because it has high medullary layer content, but poor spinnability. Therefore, it is of great significance to extract keratin from waste rabbit hair for recycling. In this research, an ultrasonic-assisted reducing agent-based extraction method was developed and applied to extract keratin from rabbit hair. The results showed that the ultrasonic treatment had a certain destructive effect on the structure of the fiber, and when combined with reducing agent, it could effectively promote the dissolution of rabbit hair, and extract keratin with high molecular weight between 31 and 94 kDa. The structure and properties of keratin were studied. Compared to the rabbit hair, the cystine content of keratin was significantly reduced, and the secondary structure changed from α-helix to β-sheet. The keratin products show excellent biocompatibility and antioxidant capacity. In addition, large keratin particles can be formed by assembly with a balance between intermolecular hydrophobic attraction as the concentration of urea in keratin solution decreased during dialysis.
Keywords: biocompatibility; keratin; protein structure.