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Transglutaminases are a family of enzymes () that catalyze the formation of a covalent bond between a free amine group (e.g., protein- or peptide-bound lysine) and the gamma-carboxamid group of protein- or peptide bound glutamine. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation.
Transglutaminases were first described in 1957.Clarke DD, Mycek MJ, Neidle A, Waelsch H. The incorporation of amines into proteins. ''Arch Biochem Biophys 1957;79:338–354.. The exact biochemical activity of transglutaminases was discovered in blood coagulation protein factor XIII in 1968.Pisano JJ, Finlayson JS, Peyton MP. Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine. Science 1968;160:892-3. PMID 4967475.
Mechanism of action
Transglutaminases form extensively cross linked generally insoluble protein polymers. These biological polymers are indispensable for the organism in order to create barriers and stable structures. Examples are blood clots (coagulation factor XIII) as well as skin and hair. The catalytic reaction is generally viewed as being irreversible and must be closely monitored through extensive control mechanisms.
Recent research indicates that sufferers from neurological diseases like Huntington's, and Alzheimer have unusually high levels of transglutaminases.
Physiological transglutaminases
Eight transglutaminases have been characterisedGriffin M, Casadio R, Bergamini CM. Transglutaminases: nature's biological glues. Biochem J 2002;368(Pt 2):377-96. PMID 12366374.
| Name | Activity | Chromosome | OMIM |
|---|---|---|---|
| Factor XIII (fibrin-stabilizing factor) | coagulaton | 6p25-p24 | |
| Keratinocyte transglutaminase (TGM1) | skin | 14q11.2 | |
| Tissue transglutaminase (TGM2) | ubiquitous | 20q11.2-q12 | |
| Epidermal transglutaminase (TGM3) | skin | 20q12 | |
| Prostate transglutaminase (TGM4) | prostate | 3p22-p21.33 | |
| TGM X or TGM5Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF. Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. J Biol Chem 1998;273:3452-3460. PMID 9452468. | skin | 15q15.2 | |
| TGM Y or TGM 6 | unclear | 20q11-15 | not assigned |
| TGM Z or TGM 7 | testis, lung | 15q15.2 |
Industrial applications
Industrial transglutaminase is produced by Streptoverticillium mobaraense fermentation in commercial quantities and is used in a variety of processes, including the production of processed meat and fish products. It can be used as a binding agent to improve the texture of protein-rich foods such as surimi or ham.
Transglutaminase can be used in these applications:
- Binding small chunks of meats into a big one ("portion control"), such as in sausages, hot dogs, restructured steaks
- Improving the texture of low-grade meat such as so-called "PSE meat" (pale, soft, and exudative meat; caused by stress and a rapid postmortem pH decline)
- Making milk and yogurt creamier
- Making noodles firmer
Besides its "orthodox" uses, transglutaminase can be used to create some unusual foods. "Cold Set Bound Fish Kebabs" are made from alternating layers of salmon and cod which are "glued" together by transglutaminase. Wylie Dufresne, chef of New York's avant-garde restaurant WD-50, invented a "pasta" made by over 95% shrimps thanks to transglutaminase.
See also
References
External links
"Transglutaminase"