Structural and Dynamic Properties of Chemically Crosslinked Mammalian and Fish Gelatin Hydrogels

Gelatin is a collagen-derived biopolymer widely used in food, pharmaceutical and biomedical applications due to its biocompatibility and gelling ability. However, gelatin hydrogels suffer from unstable mechanical strength, limited thermal resistance and susceptibility to microbial contamination. The main aim of the present study is to investigate the influence of gelatin cryostructuring followed by photo-induced menadione sodium bisulfite (MSB) chemical crosslinking on the structural and functional characteristics of mammalian and fish gelatin hydrogels. The integration of scanning electron microscopy, dielectric spectroscopy and rheological experiments provides a comprehensive view of the of molecular, morphological and mechanical properties of gelatin hydrogels under photo-induced chemical crosslinking. The SEM results revealed that crosslinked hydrogels are characterized by enlarged pores compared to non-crosslinked systems. For mammalian gelatin, multiple pores with thin partitions are formed, giving a dense and stable polymer network. For fish gelatin, large oval pores with thickened partitions are formed, preserving a less stable ordered architecture. Rheological data show strong reinforcement of the elastic and thermal stability of mammalian gelatin. The crosslinked mammalian system maintains the gel state at higher temperatures. Fish gelatin exhibits reduced elasticity retention even after crosslinking because of a different amino acid composition. Dielectric results show that crosslinking increases the portion of bound water in hydrogels considerably, but for fish gelatin, bound water is more mobile, which may explain weaker mechanical properties.