Transglutaminase Enzyme CAS 80146-85-6

Transglutaminase enzyme, abbreviated as TG. Microbial Transglutaminase is widely present in nature in animals, plants and microorganisms. It is an acyl transferase that catalyzes acyl transfer reactions between (or within) proteins, thereby leading to covalent cross-linking between proteins (or polypeptides). This cross-linking has a significant impact on the properties, gelation ability, thermal stability and water-holding capacity of proteins, thereby improving the structural and functional properties of proteins and endowing food proteins with unique texture and taste. Therefore, Transglutaminase has been widely applied in the food processing industries such as meat products, aquatic products, bean products, flour products, rice products and dairy products.

The mechanism of action of Transglutaminase mainly depends on its catalytic activity. It can transfer glutamine residues from donor proteins to recipient proteins, forming covalently linked isopeptide bonds. The formation of this isopeptide bond enables protein molecules to connect with each other, forming a more complex network structure. In addition, Transglutaminase can also catalyze cross-linking reactions within protein molecules, enhancing the stability and functionality of proteins.

Transglutaminase has multiple physiological functions in organisms. Firstly, it participates in the formation and remodeling of the extracellular matrix and is of great significance for maintaining the structure and function of tissues. Secondly, Transglutaminase plays a key role in the process of apoptosis. By regulating the speed and degree of apoptosis, it participates in the occurrence and development of diseases. In addition, Transglutaminase is also involved in processes such as immune regulation and signal transduction, and plays an irreplaceable role in maintaining the normal physiological functions of organisms.