Vibrational study on the interactions between yak keratin fibres and glyoxylic acid

Raman and IR spectroscopy were used to investigate the changes induced in yak hair keratin by the straightening treatment based on glyoxylic acid. The amino acidic residues that appeared involved in the reaction with glyoxylic acid were serine and lysine; the involvement of the latter was deduced by the spectroscopic detection of iminic species, resulting from the reaction between the aminic group of lysine and the carbonyl group of glyoxylic acid. The reaction with glyoxylic acid induced conformational rearrangements that mainly involved the fibre bulk rather than the cuticle. Changes in the average tyrosine environment and its hydrogen-bonding state were detected: at increasing glyoxylic acid incorporation, the tyrosine residues appeared more exposed, probably because of H-bond interactions with the COOH group. The distribution of the disulfide bridge conformation was also affected, although no cleavage of the S-S bond was detected, in agreement with the shiny and healthy appearance of the fibres.