New Strategy to Cope with Common Fishery Policy Landing Obligation: Collagen Extraction from Skins and Bones of Undersized Hake ().

In order to promote sustainable fishing practices within European fishing fleets and to avoid the large waste of valuable fish biomass through the practice of fish discarding, the new reform of the common fisheries policy includes the obligation of landing all species under total allowable catch (TAC) regulations. The new policy also prohibits the use of specimens under minimum conservation reference size for direct human cons38umption. In this context, it is necessary to find new uses for undersized fish, which might help to alleviate the costs associated with the landing obligation but without prompting the creation of a market. European hake (EH) (), which is one of the most important commercial fish species for the Spanish fishing industry, with a total TAC for 2018 of 3,7423 t, is used for this study. Consistent with the current policy framework and taking into account the commercial importance of this species, the aim of this work is to study a new strategy for the extraction of collagen from the skin and bone fraction of undersized discards. Three collagen fractions are successfully isolated for the first time from the skin of skin and bone discarded raw material: acid-soluble collagen (ASC) fraction 1 and pepsin-soluble collagen (PSC) fraction 2 from the skin and ASC fraction 3 from bones. The total collagen yield of the process is 13.55 ± 3.18% in a dry basis (g collagen/100 g of skin and bone fraction (SBF)) and 47.80 ± 9.83% (g collagen/100 g of collagen determined by the hydroxyproline content in SBF). The three fractions are further characterized by using different physical and chemical analysis techniques, with the conclusion drawn that the triple helix structure is preserved in the three fractions, although ASC fractions (F1 and F3) present more or stronger hydrogen bonds than the PSC fraction (F2). With the process herein presented, deboned and skinned hake specimens could represent an interesting source of high quality type I collagen, which could be useful as a raw material for the biomedical, cosmetic, and nutraceutical industries.