Highly efficient extraction of large molecular-weight keratin from wool in a water/ethanol co-solvent

A large number of wool fiber by-products, short and coarse wool fibers are difficult to spin and are disposed of by the wool industry, creating a burden on the environment. In this study, L-cysteine hydrochloride and sodium sulfite were used as reducing agents to extract keratin from natural wool in an ethanol-water mixed system. The molecular weight of the extracted keratin is up to 130 kDa with a high yield of 67%. It has been proven that the reducing agent destroyed partial disulfide bonds, ethanol destroyed partial hydrogen bonds and hydrophobic interactions, and the alpha-helix chain was converted into a beta-folded chain and random coil after extraction by instrumental analysis using a Fourier transform infrared spectrometer and X-ray diffraction. The recombination of small keratin molecules can be proven by the increase in protein particle size and molecular weight via a particle size analyzer and SDS-PAGE respectively.