Wednesday , January 26 2022

A non-label add-on may cause celiac disease


1% of Europe's population and Argentina suffer from celiac disease, including gluten-free pathologies, such as wheat flour protein groups, which attack the intestinal immune system.

It is a common autoimmune disease that has no cure and has serious health consequences. But even though he learns more about it, he continues explaining his reasons.

The specific mutations of the most important genes related to HLA-DQ are necessary for the development of the celiac disease: two variants that can be found between almost two patients. But this is not enough to explain the presence of the disease, which accounts for about 30% of the genes.

There are many environmental factors that interact with genetic risk, which have been considered as the agents of the disease: infections, food, toxins, vaccines, medicines, surgeries …

For this time period, one of the most suspicious suspects It was transgluminasis microbial, food enzymes, according to food security consultant Beatriz Robles, It is normally used to prepare Surimi, Noodles, Tofu, Nuggets … That is, enter Restructured productsIt helps to maintain the texture of the foods it supports.

Several studies have a direct positive correlation in the increase in the use of industrial enzymes in bakeries and the increase in the cell phone disease in the last four decades.

And, despite the fact that the cause and effect of the transglutaminase and celiac disease is not yet proven, the research published in Pediatria Frontiers assures that it is enough to alert its presence to food.

And today, it is impossible to find out which enzyme products are, it is not necessary to appear on the label.

This is how transglutaminase works

"Microbial transglutaminase can bind proteins, so nutrition is used to improve texture, flavors and flavors," explains Aaron Lerner, a professor at the Aesku.Kipp Institute in Germany and a researcher on the presentation note. Here is "This enzyme is like transglutaminase caused by our bodies, that is, the goal of autoimmune disease of the celiac disease."

But if transglutaminase is normally produced in our tissues, and our intestinal microbes, what is the difference with what we eat a bit more?

"Especially on a scale matter," Lerner argues. "Our own transglutaminase has a structure with microbes that strictly controls its activity, and while the abundance of microbial transglutaminase usually produces our intestinal fauna, the amount of enzyme can be significantly increased by changing the microbial population, such as infections, antibiotics or stress, or even consumption as a process of industrialized foods. "

One of the main characteristics of gluten is protein rich in elasticity. It does not break slowly and is why it is essential in the manufacture of bread, which is why they spread and maintain the oven-baked grains. But this is celiac.

"The gluten-free protein parts or the digestive tracts remain" highly transputaminase peptides that change to make several peptides, "explains Lerner." Unusual peptides tend to suffer more decomposition and HLA-DQ HLA-DQ in the intestinal wall Immune recipients recognize "foreign", but only HLA-DQ that link celiac disease. "

This research suggests that microbial transglutaminase (linked to gluten bonding) could be the goal of the immunological response of the zelia disease, and the aggression of our transglutamine is a bad identity. Microbial transglutaminase is present in processed foods, therefore, an environmental cause for celiac disease.

Lack of research

Today we do not know for sure if this theory is correct. "As a result of this enzyme, studying whether testing or causing immune damage when it comes to celiac disease will require the experimentation of animal models, cell intestinal cells or biopsies," says the author of the review.

When enzymes are used as technologically responsible, accessing the list of components is not necessary.

But, on the other hand, without treatment for celiac disease, the treatment depends on preventative measures, that is, following a gluten-free diet. And in that sense, The research recommends that transglutaminase be labeled as something that happens in Switzerland.

Unnecessary alarm?

Juan Ignacio Serrano Vela, a researcher in the field of biology, Celiac and gluten-sensitive association, "is a key element in the participation of pathogens of transglutaminase (human) disease, but is not described as the cause of the disease, so that there is no reason that the microbes are the same"

"The task of improving the immune response to changing the gluten-free peptides must be confronted with previous episodes that occur in the intestine and, initially, those responsible for this enzyme," says Director al Paladar biologist. And the studies "have for now the point of indicators, but not the evidence."

For this reason, he explains, he does not think it's appropriate to label transglutaminase: "It can be overwhelmingly disturbing and I do not know if it's appropriate to label" appropriate "cases."

Source: Paladarra directly –

Celiac Association of Argentina


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