Wool is a natural fibre with a diversity of applications in the textile industry. Its nature as a protein-rich fibre constituted of several distinct but interrelated regions, confers its unique mechanical properties. Due to the competition with superfine wools and the emergence of synthetic alternatives, coarser wools from the Northern hemisphere have suffered from a lack of valorising paths. Recently, studies successfully extracted wool polypeptides using sulphur-based reducing agents, such as sodium sulphite. These methods can separate fibres from textile blends for recycling purposes. In addition, the different wool protein types could be isolated to explore their post-consumer valorisation into new applications. In this study, the effectiveness of the amino acid, L-cysteine, as a sustainable reducing agent, combined with the activity of a protease on wool hydrolysis and proteins’ extraction was assessed, under different concentrations of L-cysteine and enzyme and duration of the reaction. Understanding the chronological order of the wool regions’ lysis during the extraction process is crucial for the control of specific parameters to selectively recover microfibrils or matrix proteins – which exhibit different protein structures. This selective recovery of the different wool proteins could support their regeneration into innovative materials, for applications in composites, packaging or construction.
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