Transglutaminase
A transglutaminase is an enzyme that forms a chemical bond between two protein molecules. The reaction also produces a molecule of ammonia. Transglutaminases were first described in 1959.[1] In 1968 it was discovered they form a role in blood coagulation.[2]
Transglutaminase have many uses. They can be used as a binding agent to improve the texture of protein-rich foods such as surimi or ham.[3] Other examples of foods made using transglutaminase include imitation crabmeat, and fish balls.
Transglutaminase Media
Three bistro tenders being joined together with transglutaminase "meat glue". They will set overnight before being unwrapped, sliced into portions, cooked, and served.
Transglutaminase treated chicken terrine.
.jpg)
References
- ↑ Clarke DD, Mycek MJ, Neidle A, Waelsch H. The incorporation of amines into proteins. Arch Biochem Biophys 79 (1959). p. 338–354. doi:10.1016/0003-9861(59)90413-8.
- ↑ Pisano JJ, Finlayson JS, Peyton MP. [Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine.]. Science 160 (3830) (1968). p. 892–3. doi:10.1126/science.160.3830.892.
- ↑ Yokoyama K, Nio N, Kikuchi Y. Properties and applications of microbial transglutaminase. Appl. Microbiol. Biotechnol. 64 (4) (2004). p. 447–54. doi:10.1007/s00253-003-1539-5.
