Transglutaminaaseihin

Transglutaminaaseihin are a group of enzymes that catalyze the formation of isopeptide bonds. This involves the transfer of an acyl group from a glutamine residue to a primary amine. In many biological systems, this primary amine is the epsilon-amino group of a lysine residue, leading to the cross-linking of proteins. This cross-linking can significantly alter the physical and functional properties of proteins, affecting their structural integrity, solubility, and susceptibility to enzymatic degradation.

Transglutaminases play crucial roles in various physiological processes. For instance, they are involved in blood coagulation, wound healing, and the formation of the epidermal barrier in the skin. In the food industry, transglutaminase is used as a food additive to improve the texture and stability of various food products. It can be employed to bind together pieces of meat or fish, enhance the elasticity of dough, or stabilize dairy products. The use of transglutaminase in food processing is often referred to as "meat glue" due to its adhesive properties.

There are several isoforms of transglutaminase, each with slightly different substrate specificities and tissue distributions. The activity of transglutaminases can be influenced by factors such as calcium ion concentration. Dysregulation of transglutaminase activity has been implicated in certain diseases, including celiac disease and neurodegenerative disorders. Research continues to explore the diverse functions and potential therapeutic applications of these versatile enzymes.