Microbial Transglutaminase

Transglutaminases (TGs) are multifunctional proteins having enzymatic and scaffolding functions that participate in regulation of cell fate in a wide range of cellular systems and are implicated to have roles in development of disease. Transglutaminases (EC 2.3. 2.13) are a class of enzymes that catalyze the formation of a covalent bond between the γ-carboxamide group of protein- or peptide-bound glutamine (acyl donors) and the free amine group of protein- or peptide-bound lysine (acyl acceptors).

Transglutaminase is a common food additive. Its ability to change the characteristics of proteins is useful in food production. With transglutaminase, different meats and other foods can combine to make products that look and taste better. Transglutaminase catalyzes the cross-link of side chains of 2 amino acids that are lysine and glutamine in liquefied proteins. This leads to the yielding of ε-(γ-glutamyl)-lysine bond and the formation of iso-peptide bonds between proteins. This bond can withstand physical stress and heat treatment.