Abstract

Irradiation can promote the cross-linking of collagen to enhance its biological properties, but the molecular changes in irradiated collagen have few been investigated. This study aimed to explore the impact of irradiation treatment on the molecular structure stabilization and cross-linking degree of skin collagen. The results showed that collagen in solution was more susceptible to Co-60 gamma irradiation than that in fish skin and in sponge forms. The solubility of collagen in solution decreased by more than 80% and the carbonyl content increased by more than 4 times compared with the control group after 12 kGy irradiation. Spectroscopic analysis and sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) showed that collagen in solution was cross-linked, especially at high irradiation doses. However, the triple helical structure of skin collagen and collagen sponge remained intact. Furthermore, irradiation also reduced the sensitivity of collagen to collagenase. Gastrointestinal digestion results showed that the antioxidant activity of collagen increased at 1–3 kGy doses and decreased at 9–12 kGy doses. Collagen irradiated at high doses (9–12 kGy) was more difficult to digest and had a larger average particle size. This study provides a potential new approach for the preparation of stable fishery-derived collagen with excellent antioxidant activity and resistance to digestion by irradiation treatment.

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