What You Need to Know
The enzyme catalyzes the formation of ε‑(γ‑glutamyl)‑lysine isopeptide bonds between glutamine and lysine residues in gluten proteins. This covalent crosslinking enhances the viscoelastic network, allowing better gas trapping and increased loaf volume. Optimal activity occurs at neutral pH and mild temperatures, but the enzyme is sensitive to thermal denaturation and substrate availability.
The Science
Primary Reaction
Covalent crosslinking between the γ‑carboxamide group of glutamine residues and the ε‑amino group of lysine residues in gluten proteins, forming ε‑(γ‑glutamyl)‑lysine isopeptide bonds.