The autumn light began to fade in the woods and my partner and I prepared a makeshift cooking area on a stack of logs. The heavenly scent of wood smoke and sizzling wild mushrooms wafting through the trees is a rich experience even without the tasting. Soon it was time to dish them up onto doorstops of bread. This was one thing that I was going to miss out on due to my wheat sensitivity, but I had my own gluten free ‘alternative’ so I wasn’t going to go without. I remember audible moans of pleasure as we tucked in.
I was awakened from my dreamy absorption into flavours by the alarmed cry of my partner, and realised that not only was this good, it was too damn good! I had inadvertently been eating the wrong bread and had consumed a fair amount of wheat by now. There would be consequences!
I could generally expect a pretty severe reaction from this much wheat; a systemic purging involving wheezy breathing, dry cracked skin, a growling belly, stomach cramps, exhaustion, cystitis, and finally diarrhoea. Looking at the possibility of six days off from my salaried job, my heart began to sink in despair when I suddenly remembered something I had read during the previous week.
I had been systematically reviewing the groups of known compounds found in medicinal mushrooms for a paper and had learned that the group of fungi known as ‘saprobes’, in furnishing their food supply predominantly by composting dead things, were likely to be rich in three groups of enzymes; phytases, proteases and amylases. These can potentially catalyse the breakdown and nutrient-mining of a wide variety of plant material, perhaps including complex structures like gluten.
“A HEALTHY MICROBIOTA IS CAPABLE OF SYNTHESISING SUITABLE ENZYMES TO ASSIST THE BODY TO DIGEST A WIDE DIVERSITY OF FOODS”
Unfortunately the majority of the mushrooms I had just eaten were not, in fact, saprobes at all but were mycorrhizal species. These, I reasoned, would not do nearly as well and I needed some mushrooms that fed primarily by directly composting plant material. Additionally, any mushrooms would have to be consumed raw to avoid denaturing their enzymes and the vast majority of wild mushrooms cannot be safely consumed without cooking.
The white button mushroom, Agaricus bisporus, is cultivated on compost and is rich in the enzymes necessary to break plant material down into mushroom food. I had nothing to lose and everything to gain so I obtained two punnets of choice organic white buttons and slowly ate my way through one of them on the journey home. Enzymes are quite specific things. One cannot simply consume any protease and expect it to catalyse the breakdown of any protein any more than one can consume any amylase and expect it to catalyse the breakdown of any carbohydrate or starch. The human body already produces a limited range of amylases and proteases, so was I right to assume that consuming different ones to those found endogenously within my GI tract could do a better job of breaking down the gluten complex, and if so why?
The evening came – and went – unusually – with no incident. Morning came and after a sound night’s sleep I still had not been troubled. I dressed, ate breakfast and went to work as normal – taking the other punnet of white button mushrooms with me as an insurance in case any signs of ‘wheat poisoning’ should ensue. Every two hours I consumed two button mushrooms and at the end of the day not only was the punnet empty but I had not experienced even the vaguest discomfort! This was a revelation to me and certainly piqued my curiosity.
When I got home I went to work once more trying to understand what those enzymes were supposed to do. I knew that it was still an assumption that the proteases, phytases and amylases in white button mushrooms had for me ‘done the trick’ but it was the best I had to go on and I was, remarkably, feeling very well. If this were to translate that others with intolerances and allergies to wheat proteins containing gliadins and glutenins were to gain the same benefit, in an age when 1% of the UK population are suffering from coeliac disease and 6% manifesting the symptoms of NCGS (non-coeliac gluten sensitivity), then combining these statistics with the relatively free availability of white button mushrooms to all, this question could be very important.
Gluten is not a simple molecule. It is composed of clusters from two groups of proteins, the prolamins and the glutelins, bound together with a variety of carbohydrates, giving it the classic glutinous or gloopy quality that makes it so useful for bread dough and pastries. The clusters are hard for the digestive system to penetrate and dismantle. The prolamins that make up gluten vary in structure based upon their cereal origin. Wheat gluten – the most common trigger for gluten sensitivities, allergies and coeliac disease, contains the prolamin structure known as gliadin.
The glutelins found in gluten (known as glutenins) present an even greater structural variability to the digestive process, yet in order for gluten to be adequately digested these must be separated from the prolamin component, requiring a diversity of enzymes to be present. It seems clear from this model of gluten structure that a variety of enzymes from the protease and amylase groups will be required in order to ‘dismantle’ gluten into its constituent parts, prior to digestion. Further proteases will then be required to catalyse the destruction of the gliadin component, and if there is any inherent sensitivity or allergy to this, or there is coeliac disease present, then the longer the GI tract is exposed to gliadins, or even glutelins of wheat origin, then the more severe the immunological reaction that cascades forward is likely to be.
So how is gluten processed and broken down in the gut? The key players here are phytases, proteases, and amylases. Phytases catalyse the breakdown of phytic acid (also known as inositol hexakisphosphate), an organic acid that is found underneath the seed coatings of grains, seeds and nuts, in the cotyledons of beans, and in some other types of plant tissue (e.g. potato tubers). It is abundant in a wide range of raw foraged foods, wholegrain flour and bread, brans and nuts.
“THE HUMAN BODY ALREADY PRODUCES A LIMITED RANGE OF AMYLASES AND PROTEASES, SO WAS I RIGHT TO ASSUME THAT CONSUMING DIFFERENT ONES TO THOSE FOUND ENDOGENOUSLY WITHIN MY GI TRACT COULD DO A BETTER JOB OF BREAKING DOWN THE GLUTEN COMPLEX?”
Phytic acid is used by plants to store phosphorus. It is known to cause digestive problems for some people, acting as an irritant in the lower GI tract as well as binding to and preventing the uptake of certain minerals. Some have dubbed phytic acid an ‘anti-nutrient’ however this is an over-reaction since not only is phytic acid found in an enormously wide variety of plant based foods but it has also been demonstrated to act as an antioxidant in the body. Its ability to chelate minerals is also reduced when there is adequate dietary vitamin C. I think it would be fair to say that phytic acid could act as an irritant in too high a quantity or in the GI tract of individuals with inflammatory disorders.
Since mushrooms also require phosphorus they can liberate it from plant based sources by deploying phytases. Wholegrain foods (e.g. wild rice and wholegrain brown rice) contain some of the highest concentrations of phytic acid, and I had consumed these with no ill effect, so phytic acid is unlikely to be the major culprit in my own history of gastro-intestinal distress. In my case at least, the prevalence of phytases in saprobic mushrooms may be a red herring.
Proteases facilitate the breaking down of a structurally diverse range of proteins into amino acids and peptides, the protein building blocks. They are highly specialised enzymes and often work in concert with other enzymes. For example pepsin has much better success with breaking down casein from milk when it is first acted upon by another protease called renin. Since white button mushrooms thrive on composted plant material they ought to be a good source of suitable proteases to augment the action of human proteases in helping to digest protein-rich plant material. That might include plant material containing gluten-like protein complexes, since these Agaricus mushrooms in the wild thrive by composting dead cereals.
“THE LONGER THE GI TRACT IS EXPOSED TO GLIADINS, OR EVEN GLUTELINS OF WHEAT ORIGIN, THEN THE MORE SEVERE THE IMMUNOLOGICAL REACTION THAT CASCADES FORWARD IS LIKELY TO BE”
Amylases are a group of enzymes that catalyse the breakdown of carbohydrates into sugar. Since gluten is in fact a protein complex composed of gliadin and glutenin subunits that are bound to carbohydrates, it is reasonable to suspect that amylases will play a very important role in the breakdown of gluten in the digestive tract, and again this could be the type of mechanism that prevented the development of symptoms when consuming raw mushrooms after eating gluten. Specific amylases are selective in terms of their potential to catalyse the breakdown of certain classes of carbohydrates. Grassland loving Agaricus species are therefore likely to be good sources of more specialist amylases that are well matched to taking-apart the gluten complex; once again because of their natural role in breaking down and composting cereals.
From my observations and research I have a few theoretical assertions. My first assertion, based on the untested assumption of all of the above, is that fungi – and particularly fungi of the right type, can provide a series of supplemental enzymes that will assist the body in the early breakdown of gluten. If they are combined with the gluten in the stomach before the chyme containing that gluten is released into the duodenum (so ideally consumed within an hour or two of accidental wheat consumption), then there is a distinct possibility that some people may obtain symptomatic relief. Significant levels of damage or inflammation could still occur though, even with enhanced breakdown and digestion of gluten taking place, so in no way am I advocating the use of these mushrooms as a prophylactic dietary measure.
My second assertion is that reduced biodiversity in the enteric biome can predispose to gluten intolerance. Many of the micro-organisms that populate the human enteric biome also have an ability to produce a range of beneficial proteases and amylases, including bacterial and fungal species (even Candida albicans). There is some evidence suggesting that coeliac sufferers produce antibodies to organisms that are routinely found in the enteric biome of other individuals and that the spectrum of organisms present has characteristic differences. This will therefore affect the range of available digestive enzymes produced by the symbiont organisms within the GI tract.
“IN FULL-BLOWN COELIAC DISEASE SERIOUS DAMAGE TO THE LINING OF THE GI TRACT CAN OCCUR ASYMPTOMATICALLY AND PROPHYLACTIC TREATMENT COULD INDUCE A FALSE PERCEPTION OF SAFETY”
This has been demonstrated in a humanised mice study, in which microoganism free mice developed signs of gluten sensitivity including antibodies to gliadins and appropriate matching T-cell responses. According to Dr. Verdu, who conducted the study, “the recognized increase in coeliac disease prevalence in the general population over the last 50 years could be driven, at least in part, by perturbations in intestinal microbial ecology.” She adds that “Specific microbiota-based therapies may aid in the prevention or treatment of coeliac disease in subjects with moderate genetic risk”.
My third assertion is that it is possible to supplement with enzymes from an external source to replace enzymatic material that would be made available by a diverse biome with the correct species present for the types of food being consumed. This is not a new idea. People who are lactose intolerant can consume lactase with dairy products, or consume live dairy products containing lactase producing microbiota, and often become more or less symptom free. The enzyme Dipeptidyl peptidase-IV or DPP-IV is included in a range of supplements targeted towards people with gluten sensitivity, and has comparatively recently been shown to assist with breaking down gluten into much smaller peptide fragments and thus deconstructing the gliadin / glutenin units before they descend deeper into the GI tract. This mechanism, which has already been demonstrated, could also be the type of mechanism at work with my consumption of raw white button mushrooms.
My fourth and final assertion is that a healthy microbiota is capable of synthesising suitable enzymes to assist the body to digest a wide diversity of foods. The presence or absence of certain organisms within the GI tract as a whole appears to play a role in constellating the presentation of systemic immune reactions and also has a direct regulatory function in connection with the gut-brain-endocrine axis. This may well be the remaining part of the picture.
Although I am not in a position to prove that the enzymes in white button mushrooms can prevent a person from developing the symptoms of gluten intolerance, it seems logical that this may be the case. I have received a reasonable amount of positive spontaneous feedback from the people who have either used this principle in their treatment protocols or who have tried it for their own condition, certainly enough to warrant further interest.
However, in full-blown coeliac disease serious damage to the lining of the GI tract can occur asymptomatically and prophylactic treatment could induce a false perception of safety. I think the consumption of raw white button mushrooms after accidental gluten ingestion is generally a good idea, but I think it is an unsuitable protocol for prevention, and more work would be needed to ensure its safety for this type of use. I suspect that the best results of all would be obtained by working with the gut microbiota in tandem with the immune system to restore the production of the necessary enzymes endogenously within the body instead. Enjoy them raw – sparingly!
