Transglutaminase (TG) — an enzyme that forms covalent bonds between glutamine and lysine amino acid residues in proteins — allows the physical bonding of separate pieces of protein into a seamless whole. A salmon-scallop "tenderloin," a mosaic of different proteins, or a perfectly uniform cylinder of ground meat that can be sliced thinly without crumbling are all TG applications. The bond formed is as strong as the protein's original structure.
- **How it works:** TG catalyses the formation of isopeptide bonds between glutamine residues (donor) and lysine residues (acceptor) in protein — the bond is irreversible and not broken by heat. - **Application:** Applied in powder form to clean, dry protein surfaces, which are pressed together, wrapped tightly in plastic, and refrigerated for 4–6 hours until the bonds form. - **Temperature:** The enzyme is active at 4–55°C — it works during refrigerated rest and is deactivated during cooking above 55°C. - **Binding strength:** The longer the bond formation time, the stronger the bond. 4 hours: sufficient for slicing. 24 hours: maximum strength. - **Food safety note:** Transglutaminase-bonded meat must be cooked throughout to the safe temperature — the bonding creates internal surfaces that may harbour bacteria between the original protein pieces. Rare service requires extremely fresh, verified-safe protein.
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