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.
Subject
Inorganic Chemistry,Condensed Matter Physics,General Materials Science,General Chemical Engineering
Cited by
2 articles.
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