The effect of shrinkproofing processes on the surface of wool was studied. Tops were subjected to the individual steps of various industrial antifelting processes. Two shrinkproofing procedures involving resins and one oxidative chlorination procedure were investigated. The samples were characterized by analyzing the whole fiber. Chemical and physical data from equivalent processing steps were compared. The cuticle from the modified fibers was isolated and investigated by means of amino acid analysis. Based on these results, the morphological composition of the isolated cuticle was determined. Calculations involving the known composition of the isolated cuticle cells and the amount of proteins dissolved during the cuticle isolation procedure give information about the loss of exocuticle during industrial shrinkproofing. The findings reflect the role of pH value and nature of active oxidative agents in shrink proofing procedures. Short chlorination procedures at low pH values caused more drastic damage than extremely lengthy chlorination procedures at higher pH values.
The cuticle plays a decisive part in wool processing, and changes in its morphological composition after industrial finishing are of particular interest. The known enzymatic method for determining the content of endo- and exocuticle is not applicable to chemically modified keratins. A new method was developed for calculating the com position of the cuticle from industrially finished wool on the basis of the results of amino acid analysis. The cuticle was isolated by mechanical treatment of wool in sodium dodecyl sulfate solution. A linear relationship was found between the content of the characteristic amino acids, aspartic acid and leucine, and the amount of en docuticle in isolated cuticle. The results were confirmed by quantitating the diagnostic compounds asparagine and N'-(γ-glutamyl)lysine by means of enzymatic hydrolysis. Shrinkproofing processes effected a specific destruction of the exocuticle, while chrome dyeing caused a loss of nonkeratinous proteins from the endocuticle.
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