Mechanically Enhanced Salmo salar Gelatin by Enzymatic Cross-linking: Premise of a Bioinspired Material for Food Packaging, Cosmetics, and Biomedical Applications

Marine animal by-products of the food industry are a great source of valuable biomolecules. Skins and bones are rich in collagen, a protein with various applications in food, cosmetic, healthcare, and medical industries in its native form or partially hydrolyzed (gelatin). Salmon gelatin is a candidate of interest due to its high biomass production available through salmon consumption, its biodegradability, and its high biocompatibility. However, its low mechanical and thermal properties can be an obstacle for various applications requiring cohesive material. Thus, gelatin modification by cross-linking is necessary. Enzymatic cross-linking by microbial transglutaminase (MTG) is preferred to chemical cross-linking to avoid the formation of potentially cytotoxic residues. In this work, the potential of salmon skin gelatin was investigated, in a comparative study with porcine gelatin, and an enzymatic versus chemical cross-linking analysis. For this purpose, the two cross-linking methods were applied to produce three-dimensional, porous, and mechanically reinforced hydrogels and sponges with different MTG ratios (2%, 5%, and 10% w/w gelatin). Their biochemical, rheological, and structural properties were characterized, as well as the stability of the material, including the degree of syneresis and the water-binding capacity. The results showed that gelatin enzymatically cross-linked produced material with high cross-linking densities over 70% of free amines. The MTG addition seemed to play a crucial role, as shown by the increase in mechanical and thermal resistances with the production of a cohesive material stable above 40 degrees C for at least 7 days and comparable to porcine and chemically cross-linked gelatins. Two prototypes were obtained with similar thermal resistances but different microstructures and viscoelastic properties, due to different formation dynamics of the covalent network. Considering these results, the enzymatically cross-linked salmon gelatin is a relevant candidate as a biopolymer for the production of matrix for a wide range of biotechnological applications such as food packaging, cosmetic patch, wound healing dressing, or tissue substitute.

Automated summary

Marine animal by-products, such as salmon skins and bones, are valuable sources of biomolecules, particularly collagen. Salmon gelatin, due to its high biomass production and biocompatibility, shows potential for various applications. However, its low mechanical and thermal properties can be overcome through enzymatic cross-linking using microbial transglutaminase (MTG). In this study, the potential of salmon skin gelatin was compared to porcine gelatin, and the effects of enzymatic and chemical cross-linking were analyzed. The results showed that enzymatically cross-linked gelatin had high cross-linking densities and improved mechanical and thermal resistances, making it a suitable candidate for biotechnological applications.