Enzyme Transglutaminase (TG) is an enzyme which can catalyze the reaction of transamination. It catalyzes the L-Lysine's r-aroylamino-hydroxybutyrate binding to the glutamic acid's. So the covalent crosslinking among the proteins or peptides is happened and the polymer of covalent compounds is formed. In the food industry, TG is applied to improve several functional characteristics of meat and protein products, such as improving the meat's structure, gel characteristic, elasticity, keeping the water and grease and so on.  

Wide ph stability 
Although the optimum ph of crude TGase is 6.0, it also functions with high activity in the wide range of ph 5.0 to 8.0. on account of this wide ph range, a variety of applications can be effective in various food processes, regardless of food type.

High thermal-stability

The optimum temperature of TGase is about 50. It also has high activity in the range of 45-55. A major advantage of TGase is that it becomes inactive when the internal temperature of food is at 75 or more in normal foods.

Strong binding force 
The covaient bond cataiyzed by TGase is hard to rupture under the conditions of non-enzymic reactions. Once the minced meat which was treated by TGase is shaped, the shape is kept, even though it is frozen or sliced or cooked.