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Transglutaminase

Transglutaminases are a family of enzymes (EC 2.3.2.13) 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.

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.

Contents

Applications

Transglutaminase is now produced by Streptoverticillium mobaraense fermentation in commercial quantities and is used in a variety of industrial 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").
  • 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 yoghurt creamier.
  • Making noodles firmer.

Besides its "orthodox" uses, transglutaminase can be used to create some weird 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.

Other transglutaminases

  • Tissue transglutaminase (TGM2, implicated in celiac disease)
  • Keratinocyte transglutaminase (TGM1)
  • Hair follicle transglutaminase (TGM3)
  • Prostate transglutaminase (TGM4)

See also

External links

10-26-2009 08:16:03
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