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Acid-soluble collagens from European hake and Blue shark skin were isolated, characterized, and compared. As the structure of collagen determines its function, the final objective of this study was to investigate biochemical differences between both collagens to identify future potential applications. Chromatographic behavior revealed differences in collagen from both species. Increases of temperature and stirring time produced no effect on European hake collagen solubility in the mobile phase, resulting in the same chromatographic profiles. Conversely, the application of temperature and stirring-time increments showed a positive effect on Blue shark collagen solubility, resulting in different chromatographic profiles and observing higher molecular weight components when sample is incubated at 50 °C (15 min) after 48 h stirring. To test if the different chromatographic behavior exhibited by both collagens could be influenced by differences in subunit composition (alpha-chains), cation exchange chromatography was employed to separate collagen subunits. The electrophoretic patterns and gel permeation chromatography with light-scattering detection (GPC-LS) results of the obtained cation exchange peak fractions revealed differences regarding subunit composition between both species, influencing the crosslinking pattern. This is the first comparative study using GPC-LS to provide information of European hake and Blue shark collagen subunit composition.

Does Subunit Composition Influence the Intermolecular Crosslinking of Fish Collagen? A Study with Hake and Blue Shark Skin Collagens