From Simple English Wikipedia, the free encyclopedia

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.

References[change | change source]

  1. Clarke DD, Mycek MJ, Neidle A, Waelsch H (1959). "The incorporation of amines into proteins". Arch Biochem Biophys. 79: 338–354. doi:10.1016/0003-9861(59)90413-8.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. Pisano JJ, Finlayson JS, Peyton MP (1968). "[Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine.]". Science. 160 (3830): 892–3. doi:10.1126/science.160.3830.892. PMID 4967475. S2CID 95459438.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. Yokoyama K, Nio N, Kikuchi Y (2004). "Properties and applications of microbial transglutaminase". Appl. Microbiol. Biotechnol. 64 (4): 447–54. doi:10.1007/s00253-003-1539-5. PMID 14740191. S2CID 19068193.{{cite journal}}: CS1 maint: multiple names: authors list (link)