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Even though wool has excellent fabric properties, its low absorption capacity hinders its efficient application in the textile industry and material field. Surface modification is one of the efficient ways of improving its inherent properties. However, the effect of surface modification on its absorption properties is not well understood. Herein, surface modification of wool was performed using deep eutectic solvent method. Several physical and chemical properties of the modified wool including chemical bonds, surface topography, and absorption capacity were analyzed. FTIR revealed that surface modification retained keratin molecular structure but only cleaved disulfide bonds. The second-derivatization of FTIR spectra further indicated that the secondary structure was also retained. SEM and EDS analyses revealed that scale modification etched the wool surface. Together, these changes improved the absorption capacity of wool. BET further revealed that surface modification increased the pole size of wool, a property that improves the adsorption capacity. Further analyses on diffusion coefficient, adsorption isotherm, adsorption kinetics, and thermodynamic parameters at a lower temperature revealed that surface modification followed Langmuir to Freundlich isotherm and pseudo-first-order model to pseudo-second-order model transformation. In particular, the adsorption content, rate and diffusion coefficient increased with decrease in the entropy and enthalpy of wool. [ABSTRACT FROM AUTHOR]

Dyeing rates of raw wool and modified wool at different time (standard errors) The dye performance evaluation The dyeing performance of the wool samples was evaluated by the color depth (K/S) and compared as shown in Table 3. Keywords: Thiol groups; ionic liquid; wool; hydrophilic performance; dye; surface modification; ; ; ; ; ; EN Thiol groups ionic liquid wool hydrophilic performance dye surface modification ZH 9729 9740 12 11/21/22 20221220 NES 221220 Introduction Wool is a widely used natural protein fiber due to its warmth, comfort and wear- proof properties (Wang et al. [34]; Zhou, Di, and Wang [40]). The FTIR spectra of raw wool and modified wool (95% confidence limit bands) Crystallinity test The XRD spectra of wool samples (raw wool and wool treated for 3 min) are shown in Figure 4. [Extracted from the article]

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]

Wool is a natural biopolymer with excellent biocompatibility. This dense structure makes it difficult to recycle the millions of wool textiles discarded annually. This study reports, for the first time, the regeneration of keratin using thiourea dioxide. Disulfide bonds were cleavage from the result of Raman test. FTIR, XRD and 13C-NMR tests determined that regenerated wool keratin retained protein macromolecule backbone, though the crystallinity degree and α-helix structure content decreased slightly. SDS-PAGE results demonstrated that the process contributed to an increase of low molecular weight keratin. All the results in this study indicate that thiourea dioxide is an effective solvent for the regeneration of wool keratin. The study offers a novel approach for the regeneration and recycle of other natural protein-based material. [ABSTRACT FROM AUTHOR]