Description
Enzyme‑mediated cross‑linking uses transglutaminase to bond glutamine and lysine residues in proteins.
Technical
Transglutaminase catalyzes the formation of ε‑(γ‑glutamyl)lysine isopeptide bonds, creating covalent inter‑ and intra‑molecular links that increase network rigidity. The reaction proceeds optimally at 37–45 °C and pH 6.5–7.5, where the enzyme’s active site aligns the γ‑carboxamide of glutamine with the ε‑amine of lysine. Reaction kinetics are governed by temperature, pH, enzyme concentration, and the presence of inhibitors such as high salt or proteases.
Science
Primary Reaction
transglutaminase-catalyzed ε-(γ-glutamyl)lysine bond formation
Sensory Profile
Aroma ()
neutralmildsubtleproteinaceousclean
Origin & History
Civilization
Japanese and Chinese food technologists
Era