Type I collagen is the main component of the extracellular matrix that acts as the physical and biochemical support of tissues. Thanks to its characteristics, collagen is widely employed as a biomaterial for implantable device fabrication and as antiaging food supplementation. Because of the BSE transmission in the 1990s, aquatic animals have become a more suitable extraction source than warm-blooded animals. Moreover, as recently demonstrated, a supplementing diet with fish collagen can increase the body’s collagen biosynthesis. In this context, Tilapia feeding was supplemented with hydrolyzed collagen in order to enhance the yield of extracted collagen. Tilapia skin was investigated with wide and small angle scattering techniques, analyzing the collagen structure from the submolecular to the nanoscale and correlated with Differential Scanning Calorimetry (DSC) measurements. Our studies demonstrated that the supplementation appears to have an effect at the nanoscale in which fibrils appear more randomly oriented than in fish fed with no supplemented feed. Conversely, no effect of a collagen-rich diet was observed at the submolecular scale.

{WAXS} and {SAXS} Investigation of Collagen-Rich Diet Effect on Multiscale Arrangement of Type I Collagen in Tilapia Skin Fed in Aquaponics Plant

Davide Altamura;Nunzia Gallo;Maria Lucia Natali;Alessandro Sannino;Luca Salvatore;Federica Stella Blasi;Angelo Corallo;
2022

Abstract

Type I collagen is the main component of the extracellular matrix that acts as the physical and biochemical support of tissues. Thanks to its characteristics, collagen is widely employed as a biomaterial for implantable device fabrication and as antiaging food supplementation. Because of the BSE transmission in the 1990s, aquatic animals have become a more suitable extraction source than warm-blooded animals. Moreover, as recently demonstrated, a supplementing diet with fish collagen can increase the body’s collagen biosynthesis. In this context, Tilapia feeding was supplemented with hydrolyzed collagen in order to enhance the yield of extracted collagen. Tilapia skin was investigated with wide and small angle scattering techniques, analyzing the collagen structure from the submolecular to the nanoscale and correlated with Differential Scanning Calorimetry (DSC) measurements. Our studies demonstrated that the supplementation appears to have an effect at the nanoscale in which fibrils appear more randomly oriented than in fish fed with no supplemented feed. Conversely, no effect of a collagen-rich diet was observed at the submolecular scale.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11587/471095
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