The liquid retention properties of wool fibers were investigated for those structurally modified by chemical and mechanical processes, such as treating with solvents and enzyme, heating in 8.0M LiBr solution and stretching in steam.
The extraction of nonkeratinous proteins with organic solvents and pronase was found to cause an increase in the liquid retension of wool fiber. Particularly, the removal of nonkeratinous proteins had marked effects on the retractive forces opposing the swelling pressure of the liquid in the cell membrane complex.
The supercontracted wools in which the original oriented α-structure was transformed to disoriented β-structure in the microfibril, had high liquid retension values at pH2 and 8, distant from the iso-electric point, pH5, whereas the stretched wools in which the oriented β-structure was effected, was little affected in the liquid retention throughout the pH range examined. These results suggest that the extent of the liquid retention of wool is dependent not on the secondary structure of the microfibrillar peptide chains, but on the orientation of the peptide chains which is closely associated with the retractive forces opposing the swelling pressure of liquid in the microfibril.
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