The use of Fourier transform-infrared (FTIR) and Raman spectroscopy (FTR) for the investigation of structural changes in wool fibre keratin after enzymatic treatment

Keratin of wool fibres obtained from Polish Merino Sheep was treated with proteolytic enzyme in buffered conditions. The zoll of orthosilicic acid was applied as a pretreatment, before enzymatic attack. It has been shown that buffer environment has significant influence on the changes in the structure of wool fibre keratin. Depending of the type of buffer utilised, different conformational changes are observed. Ammonia and tetraborate buffers were used (within pH ¼ 8.2). Each of the used buffers had a different influence on the changes in the structure of wool fibre keratin. Ammonia buffer caused bigger conformational changes in the region of disulphide bonds while tetraborate buffer disrupted the stability of amide components. To evaluate the changes of wool keratin structure infrared spectroscopy and Raman spectroscopy were applied. q 2004 Elsevier B.V. All rights reserved