Collagen is the major fibrillar component and protein in both human and animal connective tissue. It is applied in medical preparations, e.g. wound dressings and tissue engineering. Meat and poultry production industries result in large amounts of organic waste, rich in collagen. Our aim was to isolate and characterize pepsin soluble collagen from turkey tendon. Structural analysis indicated the presence of α-chains from both collagen type I and III, β-dimers and γ-trimers, consistent with the estimated molecular weight of 477.3 kDa. Circular dichroism spectroscopy confirmed an intact triple helix. The collagen demonstrated excellent thermal stability, with denaturation temperatures (Tmax) at 38.5 °C and 44.5 °C and partial refolding after extensive heating. Biocompatibility was confirmed through cell viability tests. The collagen was investigated for its potential drug carrier ability. Freeze dried collagen scaffolds containing prilocaine hydrochloride and riboflavin were prepared in the presence or absence of photo-crosslinking. Photochemical crosslinking was confirmed by SEM and enhanced mechanical properties were observed. Scaffolds had a significant slower in vitro release of the active ingredient than a reference solution. Altogether, our study suggests collagen from turkey tendon as a promising sustainable biomaterial for pharmaceutical use.
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