| Abstrakt: |
A knowledge of the influence of several factors on the stability and properties of collagen and preparations thereof precedes their industrial application. The results of such a study are reported in this paper. The mechanical properties of skin samples vary significantly with location and direction of cutting. The properties of isolated fibres from these locations, however, did not differ significantly, in a single animal. Collagen fibres from tendons and skins of several mammalian and other species exhibited under identical conditions of testing differences in their physical properties. The influence of factors like composition, shrinkage temperature, non-collagenous components, fibril width and age, on the properties is discussed individually. A slight increase in strength was observed in deaminated and deguanidinated collagen fibres while all the other treatments studied, viz. modification of side chains, crosslinking, tanning and irradiation with gamma-rays decreased the strength. An inverse correlation was observed between shrinkage temperature and strength of treated collagen fibres. The strength was also found to be influenced by the morphological structure of collagen. Irradiation with gamma-rays caused a reduction of not only the strength and shrinkage temperature of collagen but also caused severe destruction of the fibrillar structure at the X-ray and electronmicroscopic levels. The degradation was progressive with dosage. Non-hydrolytic scission of the polypeptide chains seemed to be responsible for the changes observed, which were also species specific. |
