6 Transglutaminase in Combination with other Ingredients


Opened Ajinomoto National Training Center in Tokyo, 2009.

We evaluate the composition of a mix of ingredients that complements transglutaminase applied in a meat processing and curing environment.  The enzyme is required in very small quantities in meat processing.  Experience has shown that it is best used along with a carrier that makes it more manageable as an ingredient on its own.  Secondly, when you are binding meat together with TG, then you need a connective protein.

Meat – Protein – Meat

Let’s look at some options.


The first such ingredient is gelatin or collagen which is a such a connective protein.  It is a structural protein that imparts rigidity.  It is made up of amino acids which comprise approximately 30% of the proteins within the body.  They represent rigid structures, found in bones, tendons and ligaments.  In the skin, its provides firmness, suppleness and constant renewal of skin cells. It is responsible for skin elasticity.  (Dr Ananya Mandal)

Gelatin is the heat-denatured, partially hydrolyzed form of native, insoluble collagen.  The temperature at which the collagen protein unfolds (denature) depends on the species and hydroxyproline content.  The unravelling of the collagen protein results in a viscous colloidal solution of gelatin. (Tarté, R.; 2009:  152)

Gelatin is in the first place a “thickening agent” with very good thermal stability.  Its value in meat processing where primals are injected is in the first place not in its ability to form cross-links through transglutaminase, but to thicken inside the meat before the enzyme had a chance to create the cross-links and as a result of this, to minimize syneresis of the injection brine after the tumbling phase under vacuum.

Gelatin is the ideal thickening agent to accompany transglutaminase since it contains a variety of different amino acids, including our old friends Glutamine and Lysine which are now cross-linked by the action of transglutaminase.  (Aguilar, M. R. and Román, J. S.; 2014:  186)  It is important to use the right kind of gelatin.  Fish and pork gelatin will be objectionable for either religious or allergen concerns by various processors in various parts of the world and it is an important consideration.


Why will collagen be preferred in certain conditions as opposed to gelatin in others?  Which condition will favour which application?

Is there a way to ensure maximum “retention” of TG within the meat matrix.  I deal wityh this in much greater detail in Part 2.

I.e. purge after tumbling may reduce the efficacy of the TG.  What hydrocolloids can possibly perform better in conjunction with a connective protein?

I recently learned about new technology that facilitates cold gelling when the brine enters the meat matrix.  How can this be used in combination to achieve greater retention of brine after tumbling and, at the same time, works well in combination with TG and collagen?

The second functional ingredient that becomes important in administering transglutaminase is polyphosphate.


Adding phosphates to the transglutaminase/ gelatin mix raises the pH of the solution so that transglutaminase does not begin to set while in solution.  As soon as the mix touches the substrate of the meat, the pH is lowered and the enzyme becomes active.  Phosphates are, however, not the only way that this can be achieved and a new formulation is currently being designed and tested by myself and various collaborators which will exploit other systems to achieve the same results.  The goal in this particular work is to design a phosphate free brine to be used in conjunction with the MTG.

Due to the importance of this topic will be considered in a separate article, “Curing Brine and Microbial Transglutaminase (MTG) – designing the optimal blend


From the perspective of MTG, it is useful to add a small amount of potassium salt to the brine mix.  There is an opportunity to re-design the brine system.

Due to the importance of this topic will be considered in a separate article, “Curing Brine and Microbial Transglutaminase (MTG) – designing the optimal blend


A further important ingredient is maltodextrin.  Maltodextrin is a bulking agent produced from starch and consists of beta-D-glucose.  (Kerry, P. and Kerry, J. F.; 2011: 262)  “Glycerol, maltodextrin, sorbitol, and xylitol are often used to preserve proteins and enzymes.”  “Glycerol and maltodextrin have long been regarded as proteins stabiliser or additives which have the ability to affect the equilibrium between the nature and the unfolded conformational state of the enzymes.

Moreover, glycerol and maltodextrin can evidently increase the viscosity of the enzyme solution, which may cause reduction of chemical or biological reaction rate which could result in inactivation of the enzymes.”  (Bourneow, C., et al. 2012)  An addition to these, it is the “carrier” for transglutaminase.  (Kerry, P. and Kerry, J. F.; 2011: 262)  It prevents clotting up of the ingredient mix.

There are other “ingredients” that comes from processing steps.


Vacuum tumbling is very important means of getting rid of air bubbles that result from mixing the solution. The surface tension of the bubbles interferes with the formation of the chemical bonds.  Extracting air bubbles from the solution and the meat is important for adhesion.


It is has been suggested by some that the minimum time required for the formation of bonds is anywhere from 4 to 6 hours.

In reality, it has been shown that effective bonds from as low as three hours. More formal work on this is currently being undertaken.  This is dealt with in great detail in Part 2.


When activity is measured using synthetic substrates, Transglutaminase shows high activity in a wide pH-range, i. e. between pH-value 5 and 8. Keep the temperature between 40 and 50 deg C.  For a curing and smoking processor, the denaturing of various proteins at different temperatures are important considerations from a perspective of overall colour development. It has been shown by ourselves that an internal core temperature of between 35 and 45 is sufficient to achieve more than adequate binding.  This range is important since visual denaturing and a “paling effect” starts taking place from a core temperature of 51 deg C.


It has been found that a slightly longer time is required for freezing meat that has been processed in the overall system.  The exact reasons for this are currently the subject of separate studies and will be reported on soon.  Several production managers have however been interviewed and the consensus is that this increase in freezing time is marginal and is easily accommodated within current processing environment.

These matters are all looked at in greater detail in Part 2.


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