ArticlePolymers2025
Transglutaminase Crosslinking Enhances Functional and Structural Properties of Fish Gelatins.
Article in Polymers, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Enhancing the thermal stability of cowhide jelly through transglutaminase and agar.Food chemistry: X · 2026Article
- Protein-polysaccharide conjugation in food systems: Design principles, material and processing constraints, and functional outcomes.Food chemistry: X · 2026Review
- Valorization of the Invasive FishFoods (Basel, Switzerland) · 2026Article
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Abstract
Fish gelatins are increasingly recognized as sustainable biopolymers for food, packaging, and biomedical applications; however, their functional performance often requires improvement. In this study, the effects of transglutaminase (TG) modification on the physicochemical and structural properties of trout (T) and sea bass (SB) gelatins were systematically investigated. TG treatment enhanced gel strength in a species- and concentration-dependent manner, with trout increasing from 100 g (control) to 108 g at 0.04% TG and SB reaching a maximum of 163 g at 0.01% TG. Rheological measurements confirmed improved viscoelastic behavior, particularly in trout samples (G' > G″). Emulsifying activity was optimized at 0.02-0.04% TG in trout, while excessive cross-linking reduced interfacial activity; nevertheless, emulsion stability was improved in both species. Foaming capacity and stability reached 195% and 148%, respectively, in trout, whereas higher TG concentrations led to reductions in SB foaming performance. Scanning electron microscopy revealed denser and more homogeneous networks in TG-modified gels, correlating with their enhanced rigidity. Transparency remained high, while zeta potential shifted toward more negative values, indicating improved colloidal stability. FTIR, UV-Vis, and DSC analyses confirmed conformational rearrangements and thermal stabilization after cross-linking. Minor decreases in oil-binding capacity and slight color changes were also observed. Overall, TG cross-linking significantly enhanced the functional and structural properties of fish gelatins in a source-dependent manner, supporting their potential as versatile and sustainable biopolymers for diverse industrial applications.
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