The impacts of different modification techniques on the gel properties and structural characteristics of fish gelatin

Abstract

Fish gelatin hydrogels are typically characterized by weak texture and poor thermal stability. To address this issue, fish gelatin (FG) was modified using κ-carrageenan (κC) and transglutaminase (TG). FG-κC, FG-TG, and FG-κC-TG gels were prepared. The results demonstrated that the particle size and textural properties of FG gels were significantly enhanced by κC and κC-TG composite modifications, and their zeta potential was reduced (P < 0.05). As opposed to that, the improvement effects of TG modification were weaker. The highest particle size and hardness, along with the lowest zeta potential, were exhibited by the FG-κC-TG0.06% gel. Additionally, the FG-κC-TG gel system possessed higher apparent viscosity and elastic storage modulus. Fluorescence spectroscopy and UV absorption analysis indicated that fluorescence intensity was reduced by all three modification methods, and the conformational structure of FG was altered to varying degrees. Microstructure, FTIR, and XRD results revealed that the number of hydrogen bonds and isopeptide bonds in the composite gel systems was increased by κC and κC-TG modifications, enhancing the stability and orderliness of the gel's helical structure, and forming larger aggregates and denser network structures. Furthermore, due to the presence of covalent cross-linking, improved thermal stability was exhibited by the modified gelatin hydrogels. This study not only provides theoretical support for enhancing the performance of fish gelatin but also facilitates the application of modified fish gelatin in improving the sensory quality and flavor characteristics of food, as well as in serving as a matrix material in the biomedical field.