Abstract
Fish discards and subproducts may represent an important source of raw material, not only for the food industry, but for other different kind of industries, such as the nutraceutical and cosmetic industries. Collagen, which is mainly obtained from animal skins, is an important structural protein in the animal kingdom having many different applications. It is well known that fish skins constitute a significant subproduct in the fishery industry, especially in the case of some species, where fish skins may represent up to 20% of the total body weight of fish. Peptides from collagen hydrolysates have been described to be useful for preventing skin aging and osteoarthritis, however, the mechanism for these biological activities is not well known. Fibroblasts are the main cell types involved in the collagen synthesis, and in the present work, human dermal fibroblasts have been exposed to the treatment of collagen peptides of two different molecular weight ranges. Results show that higher molecular weight collagen peptides produce higher synthesis of collagen type I mRNA and, therefore, it may suggest that prior molecular weight selection may be an important step to maximize the effect of collagen hydrolysates on collagen type I synthesis by dermal fibroblasts.
Highlights
Collagen is the main structural protein in connective, skin, and osteoarticular tissues of animal organisms [1]
Prionace glauca (PGLA)-collagen hydrolysates (CH), achieving a final hydrolysis degree of 16.52 ± 3.74%. This hydrolysate was freeze-dried and suspended in water, ultrafiltrated, and two fractions were obtained: permeate fraction (PF), which represents the part of the PGLA-CH which went through the 3000 Da cut-off membrane; and the retained fraction (RF), which did not break through the membrane
In this work we have used pepsin soluble collagen (PSC) from the skin of Prionace glauca and produced an alcalase hydrolysate which was characterized by HPLC, and this hydrolysate was compared with a commercial one, and it was found that the average molecular weight of both hydrolysates was different
Summary
Collagen is the main structural protein in connective, skin, and osteoarticular tissues of animal organisms [1]. The characteristic rope structure of collagen fibrils are organized by the union of basic units of collagen, formed by three subunit protein chains which are arranged as a triple helix and form large fibril stretches, which confer this protein its essential role in support tissues [2]. Collagen synthesis is essential for maintaining different body structures, such as skin, bones, and cartilage. Dermal fibroblasts usually present a higher collagen synthesis rate than other tissues, since collagen plays an important role in the maintenance of skin integrity [3]. Some approaches to prevent or retard the apparition of wrinkles in humans are to use cosmetics or to intake nutritional supplements which help to maintain collagen molecules in the skin at optimum
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