Science of GluteGuard
Gluten, Gluten Digestion and GluteGuard
GluteGuard assists in reducing the occurrence of symptoms caused by inadvertent gluten ingestion in susceptible individuals. It was developed after many years of Australian and international scientific research, including double-blind, randomised, placebo-controlled clinical trials.
What is gluten, where is it found and what is it used for?
Gluten is a natural protein found in wheat, barley, rye and some other cereal grains. These grains have been part of the human diet for thousands of years, and most people eat them without any problems.
Gluten contains two main protein groups: gliadins and glutenins, in roughly equal proportions. Different grains have different kinds of gluten proteins. For example, the gliadin protein in barley is called hordein, and in rye it’s secalin. Oats contain avenin proteins, but the toxicity of avenins is not fully understood and researchers are still debating what effect these might have on gluten-sensitive individuals. Gluten helps bread dough to rise, and improves the texture of bread and other grain products such as pasta, noodles, biscuits, breakfast cereal and many others.
Gluten is commonly hidden in many other food ingredients, even those that are not made from the cereals that naturally contain this protein. Products that can contain hidden gluten include sauces, marinades, gravies, processed meats, meat alternatives for vegetarians, and spices. Other sources include products manufactured on equipment that also processes gluten-containing foods, and some of the ingredients used to produce dietary supplements.
Prevalence and typical symptoms of gluten sensitivities
Roughly 1 in 13 individuals suffers some form of gluten sensitivity[1] [2] and many millions of people are affected worldwide. While these problems appear to be more common in people from European backgrounds, they’re also found in South Asia, the Middle East and some parts of Africa. People of all ages can be affected, and women are more likely than men to report being sensitive to gluten.
Gluten sensitivities such as coeliac disease, non-coeliac gluten sensitivity and dermatitis herpetiformis cause symptoms ranging from mild digestive problems to seriously debilitating cramps, bloating, diarrhoea, fatigue, headaches to skin eczema and rashes. Not surprisingly, people who have some form of gluten sensitivity often have a lower quality of life.
[1] Anderson et al. 2013. A novel serogenetic approach determines the community prevalence of celiac disease and informs improved diagnostic pathways. BMC Med 2013;11:188
[2] CSIRO Food and Health Survey – Australia, December 2010-February 201
Gluten digestion
When food is eaten that contains gluten, the body’s pancreatic enzymes (pepsin, trypsin, and chymotrypsin), which are found in the stomach and small intestine, cannot fully digest the gluten protein. They can only partly break it down, leaving smaller peptide sections that can cause problems for people who are on the spectrum of gluten-sensitivities. The peptides may be directly toxic for intestinal cells, or provoke an autoimmune response that leads to inflammation and bloating, and eventually to intestinal damage.
The only available treatment for gluten sensitivities is the lifelong adherence to a gluten-free diet. However, maintaining a strict diet is very difficult due to accidental gluten ingestion. Gluten contamination can happen when domestic or commercial food preparation practices don’t ensure the preparation of gluten-free foods in a separate area from gluten-containing foods, or the separate storage of duplicate sets of utensils. Contamination can also occur when people accidentally use food ingredients that contain hidden gluten. Gluten contamination is surprisingly common. For example, a 2018 Australian study[1] found detectable gluten in 14 out of 158 ‘gluten-free’ foods purchased in Melbourne.
[1] Halmos, E.P. et al. (2018) ‘Gluten in “gluten-free” food from food outlets in Melbourne: A cross-sectional study’ Med. J. Aust, 2018, 209, 42–43 https://www.ncbi.nlm.nih.gov/pubmed/29793402
Gluten science and the development of GluteGuard
Former RMIT professor Professor Hugh Cornell and his colleagues studied gluten for many years. They showed that gluten is only partly broken down under human digestive system conditions, where it forms complex peptides that can affect individuals on the spectrum of gluten sensitivities.
This important research was followed by the discovery that one particular papaya enzyme is uniquely able to break down the complex gluten peptides left undigested by the human digestive tract. The enzyme, which is extracted from the skin latex of the unripe papaya fruit (scientific name Carica Papaya Linn), is called caricain.
GluteGuard contains caricain.
