Collagen is a ubiquitous protein present in the extracellular matrix of all major metazoan
animals, with approximately 28 different human collagen types described in the literature, each
with unique physicochemical properties. Collagens found broad application in the cosmeceutical,
pharmaceutical, and biomedical fields and can be isolated from environmentally sustainable sources
such as marine byproducts, which are abundant in the fish processing industry and are highly
appealing low-cost sources. In this study, marine collagen was isolated from the skins of Greenland
halibut (Reinhardtius hippoglossoides), an unexplored byproduct from fish processing plants, using
three different collagen extraction methods, due to the use of distinct salting-out methods using a
solution of 2.6 M NaCl + 0.05 M Tris-HCl pH = 7.5, (method I); a combination of 0.7 M NaCl followed
by a solution of 2.3 M NaCl + 0.05 M Tris-HCl pH = 7.5 (method II); and one method using only
0.9 M NaCl (method III), yielding COLRp_I, COLRp_II, and COLRp_III collagens. These extracted
type I collagens were produced with a yield of around 2 and 4% and characterized regarding the
physicochemical properties, considering possible biotechnological applications. This work evidenced
that the typical triple helix structure conformation was preserved in all extraction methods, but
influenced the thermal behavior, intrinsic morphology, and moisture capacity of the collagens, with
interest for biotechnological application, as the incorporation as an ingredient in cosmetic formulation.
Furthermore, the use of collagen isolated from skin byproducts represents a high economic value
with decreasing collagen cost for industrial purposes and is also an environmentally sustainable
source for industrial uses.
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