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Besides, the cuticle-L + U lane showed a lighter blue band than that of the raw wool and cuticle-FA, indicating the cuticle-L + U was more difficult to be dissolved than cuticle-FA. Keywords: Wool fibers; cuticle isolation; keratin; l-cysteine; secondary structure; thermal stability; ; ; ; L- ; ; EN Wool fibers cuticle isolation keratin l-cysteine secondary structure thermal stability ZH L- 7714 7727 14 11/21/22 20221220 NES 221220 Introduction Wool has been widely used in the textile industry due to its excellent elasticity and heat retention property. FT-IR spectrum of the raw wool, cuticle-FA, and cuticle-L + U FTIR spectra comparison between the raw wool, cuticle-FA, and cuticle-L + U showed differences in 1200-1000 cm SP -1 sp . SDS-PAGE analysis of the raw wool (Lane 1), cuticle-FA (Lane 2), cuticle-L + U (Lane 3) Conclusion Taken together, our data demonstrated that pure and flaky-shaped cuticle cells could be effectively isolated with the L-cysteine and formic acid methods, respectively. [Extracted from the article]

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Regenerated keratin from waste wool is one of the most critical modern biomaterials due to its intrinsic biodegradability, biocompatibility, and mechanical durability. However, the most common keratin regeneration methods use hazardous reducing reagents and a high dose of chaotropic reagents, leading to high cost and secondary environmental pollution. We used L-cysteine as a reducing reagent to extract wool keratin without using a high amount of urea, high-temperature, and hazardous chemicals compared to the traditional reduction methods. L-cysteine aqueous solutions at pH 11–13.5 can dissolve wool fibers efficiently to regenerate keratin. The extracted keratins were then characterized using infrared spectroscopy, sodium dodecyl sulfate–polyacrylamide gel electrophoresis, and thermogravimetry analysis. At pH 12, L-cysteine aqueous solution dissolved about 67.84% of wool fiber, and the yield of keratin was about 56%. The extracted keratin exhibited characteristic keratins bands with molecular weights of approximately 100 kDa (keratin dimer), 45–65 kDa (type I and II keratins), and 10–38 kDa (keratin associated keratin, KAP), indicating that the keratins retained their structural integrities. Economic analysis revealed that avoidance of the use of 8 M urea in the reduction method significantly decreased the total cost of the extraction method. [ABSTRACT FROM AUTHOR]

The environmental benefits of utilizing protease as a biocatalyst for wool shrink-resist finishing have been widely recognized. However, the efficacy of individual protease treatment is unsatisfactory due to its incapability towards the outermost cuticle layer of wool fibers that contains hydrophobic fatty acids. In order to weaken the structural integrity of the highly cross-linked scales and promote the enzymatic anti-felting, sodium sulfite and tris (2-carboxyethyl) phosphine hydrochloride (TCEP) were employed in combination with papain, respectively, aiming at obtaining a low shrinkage without unacceptable fiber damages. Based on the synergistic effect of papain and TCEP, the edges of wool scales were slightly destroyed by the reduction of disulfide bonds, accompanied by enzymatic hydrolysis of the keratin component. Through the controlled reduction and hydrolysis of wool scales, satisfactory anti-felting result was achieved without causing severe damage to the fiber interiors. In the presence of 0.25 g/L TCEP and 25 U/mL papain, the area shrinkage of wool fabric decreased to approximately 6 %, with a low strength loss of less than 8 %. Meanwhile, the dyeing behavior of the wool fabric under low-temperature conditions was dramatically improved, leading to decreased energy consumption during production. The present work provides an alternative for eco-friendly finishing of wool fabrics, which can be applied commercially. • A facile strategy was proposed to achieve anti-felting of wool through the combined use of papain and reductant. • Synergistic effect of reductant and papain endows wool with satisfactory anti-felting property and less fiber damage. • A felting shrinkage of less than 6 % was obtained while treating with 25 U/mL of papain and 0.25 g/L of TCEP. • Low-temperature dyeing and less energy consumption were realized after the combined anti-felting finishing of wool fabric. [ABSTRACT FROM AUTHOR]