Transglutaminase-Catalyzed Gelation of Protein Systems

Transglutaminase-catalysed gelation harnesses microbial or tissue-derived enzymes to form ε-(γ-glutamyl)lysine isopeptide bonds between protein molecules, transforming soluble proteins into three-dimensional gel networks with tunable mechanical and functional properties. Substrates span animal sources (myofibrillar proteins from meat and fish, dairy proteins such as casein and whey) and plant sources (soy, pea, mung bean and nut isolates). Reaction parameters—including enzyme concentration, temperature, pH and co-factors such as Ca2+—govern the extent of cross-linking, network architecture and rheological profile. Pre-treatments like heat, ultrasound or pulsed electric fields further modulate protein conformation and residue accessibility, enhancing gel strength and uniformity. Transglutaminase-structured gels exhibit high water-holding capacity, improved texture and stability under freeze–thaw or digestive conditions, finding applications in food systems (meat analogues, dairy formulations, encapsulation vehicles) and emerging biomedical fields (tissue scaffolds, controlled-release matrices). Foundational work on fish and muscle transglutaminases has paved the way for current advances in plant protein structuring and composite gels with non-meat emulsions, underscoring a global drive towards sustainable, high-performance protein gels.

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Transglutaminase-Catalyzed Gelation of Protein Systems publication trend

The graph below shows the total number of articles in transglutaminase-catalyzed gelation of protein systems across all publications each year (not limited to Nature Index journals).

Technical terms

Transglutaminase: An enzyme that catalyses the formation of covalent isopeptide bonds between glutamine and lysine residues in proteins.

Cross-linking: The enzymatic creation of covalent bonds between protein chains, forming a network structure.

Gel network: A three-dimensional matrix formed by interconnected protein molecules trapping water and other components.

Myofibrillar proteins: Muscle proteins, including myosin and actin, that readily undergo enzymatic cross-linking to form gels.

Water-holding capacity: The ability of a gel matrix to retain water against external forces such as centrifugation or freeze–thaw cycles.

References

1. Analysis of the gel properties, microstructural characteristics, and intermolecular forces of soybean protein isolate gel induced by transglutaminase. Food Science & Nutrition (2022).
2. Transglutaminase Activity in Alaska Pollack Muscle and Surimi, and its Reaction with Myosin B. Nippon Suisan Gakkaishi (1990).
3. Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel. Journal of Dairy Science (2022).
4. Effects of Transglutaminase on Myofibrillar Protein Composite Gels with Addition of Non-Meat Protein Emulsion. Gels (2023).