Abstract

The porcine dermal collagen molecules were successfully digested by clostridium histolyticun collagenases (CHC) and then ultra-filtrated using varying grades of ultra-filtration membranes. Gel permeation analyses revealed that collagen fragments with varying molecular weights were successfully segregated using ultra-filtration membranes with varying grades of pore sizes. Fourier transform infra-red analyses suggest that digested collagen fragments and digested collagen fragments prepared after ultra-filtration still preserve certain percentages of triple helix structures of collagen molecules, although the percentages of preserved triple helix structures present in digested and ultra-filtrated collagen fragments reduce significantly as their Mw values reduce. Thermal and denaturation temperature analysis suggest that denaturation temperature and thermal degradation temperature values of digested collagen fragments and ultra-filtrated collagen fragments decrease significantly as their Mw values reduce. The absorbed/desorbed amounts of digested and ultra-filtrated collagen fragments in PA6/PP flocking specimens are significantly higher than those of the original collagens, and increase significantly as their Mw values reduce. Possible reasons accounting for the above degradation, ultra-filtration physicochemical, absorbing and desorbing properties of original, digested and ultra-filtrated digested collagen molecules are reported.

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