Premium
Surface studies of keratin fibres and related model compounds using ESCA, 2—intermediate oxidation products of cystyl residues on keratin fibre surfaces and their hydrolytical stability
Author(s) -
Baumann H.,
Setiawan L. D.,
Gribbin D.
Publication year - 1986
Publication title -
surface and interface analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.52
H-Index - 90
eISSN - 1096-9918
pISSN - 0142-2421
DOI - 10.1002/sia.740080505
Subject(s) - chemistry , cystine , keratin , cysteine , organic chemistry , inorganic chemistry , polymer chemistry , medicine , pathology , enzyme
S 2p binding energies of the surfaces of keratin fibres oxidized to different degrees under industrially applied oxidative wet finishing conditions have been estimated using ESCA. With the help of S 2p data obtained from chosen model compounds qualitative identification of the oxidation products of cystyl residues on the surfaces of partially oxidized wool has been made. The oxidation products identified are the residues of cystine monoxide, cysteine sulphinic acid and sulphonic acid. The hydrolytical stability of the intermediate oxidation products of cystyl residues on the fibre surface seems to be comparable with that of the model compounds (cysteine sulphinic acid>cystine monoxide>cystine dioxide). The reaction conditions determine the partial oxidation products which are analysed on the fibre surface. However, in the present study a conclusive evidence for the existence of dioxycystyl residues cannot be given.