Anywhere you look it is easy to find all kinds of dietary restrictions. They are so persistent, these days, that most restaurants carry options for people who request vegan, dairy-free, nut-free, vegetarian, and gluten-free requests, whether because of allergy or preference. Of course, these are only a few of the dozen or so dietary requests that diners can make while eating out.
The gluten-free diet is particularly interesting because even though it is popular, there does not exist much evidence to support that it is better for your health. If you happen to be among the one percent (or so) of the population with Celiac disease, though, gluten can cause intolerable issues in your digestive system. But that still does not explain why some people have such issues with it.
To try to understand this, we must first realize that gluten is the name given to the protein content in bread grains like wheat, rye, and barley. We do know that mutations in a very important immunity-related gene—HLA-DQ—appears to be necessary for the development of Celiac disease since one of two variants of this gene are present in nearly every person who suffers from Celiac disease. However, these variants are also present in nearly one-third of the general human population (and not everyone seems to be affected by gluten the same way).
Because of this interesting contradiction of facts, scientists suspect perhaps certain environmental factors interacting with genetic risk are what result in Celiac disease. Such variables could include things like infection, food allergy, toxins, vaccinations, and drugs or surgeries.
Food additives have come under scrutiny much more lately, of course, since they are a relatively new development at a time when metabolic conditions are on the rise. Of these, it appears microbial transglutaminase has emerged as the most likely culprit; this is a bacterial enzyme used widely in the industrial processing of meat, dairy and baked goods, among other products.
Visiting professor from the Aesku.Kipp Institute, in Germany, Aaron Lerner, co-authored a recent study investigating the relationship between food additives and Celiac disease. He comments, that microbial transglutaminase can bind proteins together, and that is why it is commonly used to improve traits like food texture palatability, and even shelf-life. He goes on to say, “This enzyme functions like the transglutaminase produced by our body, which is known to be the target of autoimmunity in celiac disease.”
Truly, the increased use of industrial enzymes like these in bakery products appears to coincide with the rise in celiac disease over the last forty years.
A review of this study has been published in Frontiers in Pediatrics.