Description
Microbial transglutaminase cross‑links legume proteins to create a meat‑like matrix.
Technical
The enzyme catalyzes the formation of ε‑(γ‑glutamyl)lysine isopeptide bonds between glutamine and lysine side chains, generating a three‑dimensional protein network. Reaction proceeds optimally at 37–45 °C and pH 6.0–7.5, with gelation achieved in 30–60 min. Inhibitory factors such as ≥0.5 M NaCl, >10 % v/v alcohol, excessive protein loading (>30 % w/w) or temperatures >55 °C diminish cross‑linking efficiency.
Science
Primary Reaction
ε‑(γ‑glutamyl)lysine isopeptide bond formation via transglutaminase‑catalyzed acyl transfer
Sensory Profile
Aroma ()
neutralearthylightly roastedmildprotein-richsubtle fermentation
Wine Analogy
Like the protein-binding effect of egg whites in fining wines
Coffee Analogy