Transglutaminase enzyme food additive

Transglutaminase enzyme food additive

“Meat glue” is transglutaminase, an enzyme in powder form, derived from beef and pork blood plasma.

Application of Transglutaminase in cereal products, for seafood application, enzyme food additive, TG, an enzyme used in cheese, used in dairy products, in Tofu products.


Transglutaminase is an enzyme that has the property to bind protein rich foods like meat, poultry, fish and seafood, or foods mixed with gelatin. It is thus possible to bind small or irregular cuts of meat into larger pieces in order to allow for even cooking, or for a different presentation style.


Many types of transglutaminases are naturally part of animal, plant and microbe organisms.  A certain amount of transglutaminase is therefore already present in the meats, poulty, fish, seafoods and even vegetables that we eat.

Transglutaminase can also be industrially produced throught a fermentation process. It is sold as powdery mixes.


Transglutaminase is an enzyme, which is to say it is a protein that has the property to catalyse some chemical reactions. In this case, transglutaminase quickens the formation of covalent bonds between two amino acids : lycine and glutamine. Amino acids are a basic component of proteins.

Transglutaminase therefore helps « glue » protein rich foods like meat, poultry, fish and seafood, or gelatin. Binding will be especially strong with proteins rich in lycine and glutamine.

Industry applications

Transglutaminase has been used for many years by the food industry in the making of transformed meats and fish like saussages, patties and imitation crabmeat. It is also sometimes added to cheeses in order to obtain a better texture, or to yogurts to avoid liquid leeking (syneresis).

Creative cooking applications

Transglutaminase has multiple uses in creative cooking. It allows for the confection of original sausages without membranes that nonetheless hold very well even when cut. It enables a chef to serve as medallions meats and fish that couldn’t otherwise be c ut that way. It can permit original, and appetizing shapes.

By binding thin cuts of meat together, one can obtain bigger pieces that can consequentely be more easily cooked rare, for example. In the same way, irregular cuts can be « glued » together into a more regular shape and permit an even cooking.

Transglutaminase is sometimes used to glue bacon or chicken or fish skin unto other types of meat and fish.

It  is also used to make pasta out of protein foods such as puréed shrimp. These pasta’s texture, pliability and resistance to heat is very similar to that of flour based pasta.

In conjonction with the use of gelatin (which is a protein), transglutaminase can bind other foods like fruit, vegetables, cooked cereal and grains which can then be served as cold or hot chunks.

Tips and tricks

Transglutaminase can be sprinkled over meat or mixed with water into a slurry, to be  applied evenly with a brush. Foods then need to be hermetically wrapped in plastic and left aside for a few hours. The process can be quickened to about 15 to 20 minutes when the food binded with transglutaminase is heated to around 55°C (131°F).


‘Meat glue’ used as food additive in processed meat, other food

  • By ANDREW SCHNEIDER Scripps Howard News Service
  • Posted May 8, 2012

“Meat glue” is transglutaminase, an enzyme in powder form, derived from beef and pork blood plasma.

Every day, millions of Americans are likely putting something in their mouths that contains a substance called “meat glue” by critics of the food industry.

The additive with the unappetizing nickname is used to produce meats found in supermarkets, in local delis and in restaurants ranging from fast food to fine dining. Even vegetarian food isn’t exempt.

Marketing consultants and food scientists estimate — because no company will discuss sales figures– that anywhere from 11 to 35 percent of all packaged and sliced ham, beef, chicken, fish, pizza toppings and other deli products are enhanced, restructured or molded using the meat glue, which is made from one of two brands of protein adhesive.


Coeliac or Celiac Disease

Celiac Disease, a.k.a. Celiac Sprue or Coeliac Disease, is classified as an autoimmune disorder, and is essentially an adverse immune system response to Gluten (i.e. Gliadin/Gluten Intolerance). It can affect genetically predisposed individuals of all ages, from middle infancy onwards. Celiac Disease is the result of a combination of the action of Anti-Gliadin Antibodies (AGAs) against the presence of ingested Gliadin , but more importantly the production of Anti-Tissue Transglutaminase Antibodies (anti-tTG antibodies). Whilst non-Celiac sufferers can have AGAs, i.e. Gliadin/Gluten Intolerance, they do not have measurable levels of anti-tTG antibodies, which are a genetic-based response in Celiac sufferers to the ingestion of Gliadin. Celiac Disease is therefore a specific type of Gliadin(Gluten)-intolerance.

Approximately 0.5-1% of the population of the USA suffer from Celiac Disease. There are a number of genes that are involved in controlling the excessive immune response to Gliadin (Gluten), that may lend an individual predisposed or more likely to develop such a condition, and according to the studies of Kenneth Fine, M.D., of Enterolab, is found in approximately 60% of Americans. There may be other, currently undefined genes, that control whether such a toxic reaction occurs and if and to what extent damage will occur to the intestines and other tissues or not. Research suggests that as many as 30% of Americans may be Gluten sensitive, with 1 in 225 having the sensivity as severe to cause the intestinal damage associated with Celiac Disease. Please seee the Genetic Testing section below for more discussion of the Celiac genes present in the US population.

Transglutaminase is family of enzymes that catalyse the formation of a covalent bond between a free amine group (e.g. from lysine groups found in a protein or peptide) and the gamma-carboamid group (e.g. from glutamine groups found in another protein or peptide). The bonds formed by transglutaminase are highly resistant to proteolytic degradation. Tranglutaminase enzymes are generally found in the intestines and also in the tissues. It is referred to as ‘meat glue’ in the food processing industry. They play an important part in blood clotting.

One subclass of Transglutaminase is known as Tissue-Transglutaminasen (TG2 or tTG). It is classed as an ‘auto-antigen’. It’s natural affinity to binding with Gliadin, and the resulting protein crosslinking stimulates the immune B-cell responses that eventually result in the production of the problematic overproduction of the ATA IgA and IgG antibodies (examined below).

Whilst associated with Celiac Disease, high levels of Tissue Transglutaminase enzymes are found in sufferers of Huntingdon’s and Parkinson’s Disease. A study by Griffin M, Casadio R, Bergamini CM. ‘Transglutaminases: nature’s biological glues’. Biochem J 2002;368:377-96 suggests that tTG plays an important role in inflammation, degenerative diseases and tumor biology.

In Celiac Disease, antiendomysial antibodies (EMAs) are produced. These mainly consist of Anti-Transglutaminse Antibodies (ATAs) against the enzyme Transglutaminase and Tissue-Transglutaminase. ATAs are types of IgA and IgG antibodies, and their relative proportions in Celiac Disease sufferers depends on the phenotypes involved. Please note that these EMAs are different to Anti-Gliadin Antibodies (AGAs), consisting of IgA and IgG antibodies, that attack Gliadin directly. IgA antibodies can be found in the stool and also the blood to a lesser extent, and the presence of anti-tTG antibodies in high numbers can predict the onset of Celiac Disease. anti-tTG antibody production can also be stimulated by the presence of the Rotavirus protein VP7. A Rotavirus is a genus of double-stranded RNA virus from the Retroviridae family and is known to cause diahrrea.

‘For tTG autoimmunity (CD), T-cells are generated against wheat gliadin and similar gluten proteins of the trib Triticeae. The T-cells are defined by the ability to react to HLA-DQ8 and DQ2.5 restricted antigens and gliadin is one of the antigens. Gliadin is a favored dietary substrate for transglutaminase because of many enzyme reaction sites on gliadin. In disease, transglutaminase reacts with gliadin forming a linkage. In forming this bond transglutaminase becomes linked to T-cell epitopes on gliadin. B-cells with surface IgM that react to transglutaminase can present it with bound gliadin peptides to T-cells which stimulate B-cell maturation and proliferation to plasma cells making IgA or IgM.’




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