The application of Fourier-transform infrared (FTIR) and Raman spectroscopy (FTR) to the evaluation of structural changes in wool fibre keratin after deuterium exchange and modification by the orthosilicic acid

Abstract

An injury of hair macrostructure and substantial alkalinity of the water–lipid shield medium on wool fibre surface is conducive to a transition of heavy metal elements into ion forms. It also helps SiO 2 in a transition into a colloidal form of orthosilicic acid and its penetration in this form of the wool fibre structure. Consequently, it leads to the biomineralization of the wool fibre [J. Mol. Struct. 511–512 (1999) 307; J. Mol. Struct. 511–512 (2000) 397]. Changes taking place in the process of biomineralization, mainly in the amorphous region, may be responsible for the effectiveness of the technological processes and the properties of ready wool products [3]. Wool fibres obtained from Polish Merino sheep were treated with solution of orthosilicic acid (H 4SiO 4· nH 2O) in experimental conditions during which fibres first underwent extraction with methylene chloride and them with asolution of orthosilicic acid in alkaline medium. Studies of deuterium exchange in the wool fibre keratin were applied to study changes in the structure of wool fibre keratin in the process of orthosilicic acid treatment. The changes in the structure of wool fibre were studied by means of infrared spectroscopy (FTIR) and Raman spectroscopy (FTR).