What You Need to Know
Transglutaminase catalyzes the formation of ε‑(γ‑glutamyl)lysine isopeptide bonds between glutamine and lysine residues, creating a covalent network that enhances gel strength. The reaction is pH‑ and temperature‑dependent, with optimal activity at 37–40 °C and pH 6.0–7.5, and is inhibited by high salt, high fat, chelators, or excessive calcium.
The Science
Primary Reaction
ε‑(γ‑glutamyl)lysine isopeptide bond formation between glutamine and lysine residues in plant proteins