Abstract

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.

Highlights

  • Keratin is a type of scleroprotein made up of amino acids that are linked by both intramolecular and intermolecular interactions, including disulfide bonds, ionic bonds, hydrogen bonds, and hydrophobic interaction

  • There are a lot of disulfide bonds in aforementioned materials which are responsible for its chemical stability and high mechanical strength [1], its application has been limited, resulting in a severe waste of resources and major accumulation of environmental pollution

  • Waste resulted from rabbit hairhair with poor spinnability hashas caused environmental

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Summary

Introduction

Keratin is a type of scleroprotein made up of amino acids that are linked by both intramolecular and intermolecular interactions, including disulfide bonds, ionic bonds, hydrogen bonds, and hydrophobic interaction. Keratin can be extracted from the waste fiber by several methods, such as crushing (to produce feed additives), burning, and burying (to produce fertilizers) [8,9,10] To study the recovery and utilization of the fiber waste, to prevent the environmental pollution, and to appropriately utilize the resources, most research mainly concentrate on the extraction and purification of keratin from low quality animal fibers by disrupting disulfide bonds and peptide bonds using chemical substances [11,12]. Main keratin extraction methods (from protein fibers) include physical method (e.g., microwave irradiation) [13], steam explosion method [14], and chemical method (e.g., hydrolysis, oxidation, reduction, and ionic liquids). The above description shows that to obtain high solubility when ionic liquids are used, the dissolution temperature should be high

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