Ahh I think I had a small breakthrough. Here's something, from the first study I found, except elaborated:
Fermentation was carried out on cracked soybeans inoculated with Aspergillus oryzae, Rhizopus oryzae and Bacillus subtilis or in a soybean flour suspension fermented with bacteria naturally present in soybeans or by inoculation with Lactobacillus plantarum. Of all the microorganisms tested, Lactobacillus plantarum showed the highest reduction in immunoreactivity: 96 to 99 percent. Molds grown on cracked soybeans showed a reduced the immunoreactivity by about 67 percent. Fermentation by molds showed weaker efficacy to eliminate immunoreactive proteins than bacterial proteolysis, probably because of the slower growth rate of the molds during the fermentation process.
So I searched for that particular strain of bacteria and:
Lactobacillus plantarum is a widespread member of the genus Lactobacillus, commonly found in many fermented food products as well as anaerobic plant matter. It is also present in saliva (from which it was first isolated). It has the ability to liquefy gelatin. L. plantarum has one of the largest genomes known among the lactic acid bacteria and is a very flexible and versatile species.
Which reminded me of a technique I read about that the Aztecs and Mayans used on corn. They made a drink, that was also a staple, called chicha:
In some cultures, instead of germinating the maize to release the starches therein, the maize is ground, moistened in the chicha maker's mouth, and formed into small balls which are then flattened and laid out to dry. Naturally occurring ptyalin enzymes in the maker's saliva catalyses the breakdown of starch in the maize into maltose. (This process of chewing grains or other starches was used in the production of alcoholic beverages in pre-modern cultures around the world, including, for example, sake in Japan.)
I've made that before, and it's weird. You can put lemon peel in with it, and if you get it just right it tastes like mildly carbonated lemonade.
Anyways, so then I found a link to the digestive enzymes wiki:
I remembered the Weston A Price foundation mentioned anti-amylases which prevent starch from being broken down by amylase (indigestion anyone? small bowel bacteria overgrowth?), but looking down the line we got:
Complex food substances taken by animals and humans must be broken down into simple, soluble and diffusible substances before they can be absorbed into the body. In the oral cavity, salivary glands secrete (or create) ptyalin. It is a type of Î±-amylase, which digests starch into small segments of multiple sugars and into the individual soluble sugars. Secreted by small and large salivary glands.
Salivary glands also secrete lysozyme, which kills bacteria but is not classified as a digestive enzyme.
Summary of the actions of digestive enzymes:
* Bromelaine tenderizes meat and acts as an anti-inflamatory agent.
* Betaine effects cell fluid balance as osmolytes
* Salivary Amylase (also known as ptyalin) (Mouth) produced by salivary glands breaks down starch into sugar.
The enzymes that get secreted in the stomach are called gastric enzymes. These are the following:
* Pepsin is the main gastric enzyme. It breaks proteins into smaller peptide fragments.
* Gelatinase, degrades type I and type V gelatin and type IV and V collagen, which are proteoglycans in meat.
* Gastric amylase degrades starch, but is of minor significance.
* Gastric lipase is a tributyrase by its biochemical activity, as it acts almost exclusively on tributyrin, a butter fat enzyme.
* Pepsin enzyme is secreted by gastric glands
* Renin enzyme change the liquid milk to solid
The pancreas is the main digestive gland in our body. It secretes the enzymes:
* Trypsin, is a protease that cleaves proteins at the basic amino acids.
* Chymotrypsin, is a protease that cleaves proteins at the aromatic amino acids.
* Steapsin, degrades triglycerides into fatty acids and glycerol.
* Carboxypeptidase, is a protease that takes off the terminal acid group from a protein
* Several elastases that degrade the protein elastin and some other proteins.
* Several nucleases that degrade nucleic acids, like DNAase and RNAase
* Pancreatic amylase that, besides starch, and glycogen, degrades most other carbohydrates. Humans lack the enzyme to digest the carbohydrate cellulose.
* Pancreatic Secretion: Bile from the liver, which emulsifies fat, allowing more efficient use of lipase in the duodenum in converting lipids to smaller more manageable sizes. Bile is not considered an enzyme, but aids macronutrient degradation.
Proper small intestine enzymes
* Several peptidases.
* The jejunum and ileum secretes a juice called succus entericus which contains the following:
Five types of enzymes degrade disaccharides into monosaccharides:
* Sucrase, which breaks down sucrose into glucose and fructose
* Maltase, which breaks down maltose into glucose.
* Isomaltase, which breaks down maltose and isomaltose
* Lactase, which breaks down lactose into glucose and galactose
* Intestinal lipase, which breaks down fatty acids
The small intestine receives lipase, trypsin and amylase from the pancreas. They are transported from the pancreas to the duodenum through the pancreatic duct. Protein, fats and starch are broken down into smaller molecules. However, they are not fully broken down yet. This causes the enzymes of the small intestine to act upon them. These enzymes include peptidase, which breaks down peptides into amino acids and the enzyme maltase acts upon maltose which produces glucose. These molecules are absorbed by the villi in the small intestine and according to the molecule they are either absorbed by the lacteal or blood capillaries.
Okay I highlighted some things I'm gonna use to make a few points.
My main point is with trypsin. Seeing trypsin reminded me yet again of Weston A Price and his mention of anti-nutrients. Well he mentions trypsin inhibitor as one of them, an anti-enzyme so to speak, that's present in most, if not all, grains, especially whole grains. So why is this important? Let me explain.
Lectins and allergens are mostly proteins, right? Gluten is a mix of protein, gliadan and glutenin(?), and likewise with other problematic foods. So what breaks down protein? Pepsin. I didn't mention any pepsin inhibitors, so if we create an enzyme that can break down protein why do we still have problems? Take a look at what I bolded, with what it says about pepsin. Pepsin is secreted in the stomach and breaks down proteins into peptides
. You can think of peptides as smaller proteins; they're broken down, but they're not quite pure amino acids yet. So what enzyme breaks down peptides? That's right, trypsin.
So we take in these enzyme inhibitors which include trypsin inhibitor. We make it through the stomach all right, pepsin does it's job breaking down protein into peptides, but then we hit a snag. We head into the small intestine and the trypsin inhibitors stop trypsin from doing its job, leaving a bunch of peptides free floating around in our intestine. It is my assumption, my theory, that these peptides, and not the original lectin proteins, are the ones that react in our gut, causing all our problems.
Well it's just a theory however, but I believe we might already have some circumstantial evidence that supports my claim. You all know how celiac disease works, right? Gluten contains a protein that binds to our intestine leading to an immune reaction that attacks ourselves. There was a thread going around about lectins and fermentation, and I think one article was cited saying traditional sourdough bread was tolerated in some celiac diagnosed patients. It's true, too, there's anecdotal evidence around celiac forums and blogs that claim some people can stand traditional sourdough fermented for long periods of time. Anyways, here's the study the article was mentioning:
Sourdough bread made from wheat and nontoxic flours and started with selected lactobacilli is tolerated in celiac sprue patients.
Di Cagno R, De Angelis M, Auricchio S, Greco L, Clarke C, De Vincenzi M, Giovannini C, D'Archivio M, Landolfo F, Parrilli G, Minervini F, Arendt E, Gobbetti M.
Department of Plant Protection and Applied Microbiology, University of Bari, 70126 Bari, Italy.
This work was aimed at producing a sourdough bread that is tolerated by celiac sprue (CS) patients. Selected sourdough lactobacilli had specialized peptidases capable of hydrolyzing Pro-rich peptides, including the 33-mer peptide, the most potent inducer of gut-derived human T-cell lines in CS patients. This epitope, the most important in CS, was hydrolyzed completely after treatment with cells and their cytoplasmic extracts (CE). A sourdough made from a mixture of wheat (30%) and nontoxic oat, millet, and buckwheat flours was started with lactobacilli. After 24 h of fermentation, wheat gliadins and low-molecular-mass, alcohol-soluble polypeptides were hydrolyzed almost totally. Proteins were extracted from sourdough and used to produce a peptic-tryptic digest for in vitro agglutination tests on K 562(S) subclone cells of human origin. The minimal agglutinating activity was ca. 250 times higher than that of doughs chemically acidified or started with baker's yeast. Two types of bread, containing ca. 2 g of gluten, were produced with baker's yeast or lactobacilli and CE and used for an in vivo double-blind acute challenge of CS patients. Thirteen of the 17 patients showed a marked alteration of intestinal permeability after ingestion of baker's yeast bread. When fed the sourdough bread, the same 13 patients had values for excreted rhamnose and lactulose that did not differ significantly from the baseline values. The other 4 of the 17 CS patients did not respond to gluten after ingesting the baker's yeast or sourdough bread. These results showed that a bread biotechnology that uses selected lactobacilli, nontoxic flours, and a long fermentation time is a novel tool for decreasing the level of gluten intolerance in humans.
Another study, also selecting specific strains for their abilities to break down the irritating peptide:
Proteolysis by sourdough lactic acid bacteria: effects on wheat flour protein fractions and gliadin peptides involved in human cereal intolerance.
Di Cagno R, De Angelis M, Lavermicocca P, De Vincenzi M, Giovannini C, Faccia M, Gobbetti M.
Dipartimento di Protezione delle Piante e Microbiologia Applicata, FacoltĂ di Agraria di Bari, Via G. Amendola 165/a, 70126 Bari, Italy.
Sourdough lactic acid bacteria were preliminarily screened for proteolytic activity by using a digest of albumin and globulin polypeptides as a substrate. Based on their hydrolysis profile patterns, Lactobacillus alimentarius 15M, Lactobacillus brevis 14G, Lactobacillus sanfranciscensis 7A, and Lactobacillus hilgardii 51B were selected and used in sourdough fermentation. A fractionated method of protein extraction and subsequent two-dimensional electrophoresis were used to estimate proteolysis in sourdoughs. Compared to a chemically acidified (pH 4.4) dough, 37 to 42 polypeptides, distributed over a wide range of pIs and molecular masses, were hydrolyzed by L. alimentarius 15M, L. brevis 14G, and L. sanfranciscensis 7A. Albumin, globulin, and gliadin fractions were hydrolyzed, while glutenins were not degraded. The concentrations of free amino acids, especially proline and glutamic and aspartic acids, also increased in sourdoughs. Compared to the chemically acidified dough, proteolysis by lactobacilli positively influenced the softening of the dough during fermentation, as determined by rheological analyses. Enzyme preparations of the selected lactobacilli which contained proteinase or peptidase enzymes showed hydrolysis of the 31-43 fragment of A-gliadin, a toxic peptide for celiac patients. A toxic peptic-tryptic (PT) digest of gliadins was used for in vitro agglutination tests on K 562 (S) subclone cells of human myelagenous leukemia origin. The lowest concentration of PT digest that agglutinated 100% of the total cells was 0.218 g/liter. Hydrolysis of the PT digest by proteolytic enzymes of L. alimentarius 15M and L. brevis 14G completely prevented agglutination of the K 562 (S) cells by the PT digest at a concentration of 0.875 g/liter. Considerable inhibitory effects by other strains and at higher concentrations of the PT digest were also found. The mixture of peptides produced by enzyme preparations of selected lactobacilli showed a decreased agglutination of K 562 (S) cells with respect to the whole 31-43 fragment of A-gliadin.
Highly efficient gluten degradation by lactobacilli and fungal proteases during food processing: new perspectives for celiac disease.
Rizzello CG, De Angelis M, Di Cagno R, Camarca A, Silano M, Losito I, De Vincenzi M, De Bari MD, Palmisano F, Maurano F, Gianfrani C, Gobbetti M.
Department of Plant Protection and Applied Microbiology, University of Bari, Bari, Italy.
Presently, the only effective treatment for celiac disease is a life-long gluten-free diet. In this work, we used a new mixture of selected sourdough lactobacilli and fungal proteases to eliminate the toxicity of wheat flour during long-time fermentation. Immunological (R5 antibody-based sandwich and competitive enzyme-linked immunosorbent assay [ELISA] and R5 antibody-based Western blot), two-dimensional electrophoresis, and mass spectrometry (matrix-assisted laser desorption ionization-time of flight, strong-cation-exchange-liquid chromatography/capillary liquid chromatography-electrospray ionization-quadrupole-time of flight [SCX-LC/CapLC-ESI-Q-TOF], and high-pressure liquid chromatography-electrospray ionization-ion trap mass spectrometry) analyses were used to determine the gluten concentration. Assays based on the proliferation of peripheral blood mononuclear cells (PBMCs) and gamma interferon production by PBMCs and intestinal T-cell lines (iTCLs) from 12 celiac disease patients were used to determine the protein toxicity of the pepsin-trypsin digests from fermented wheat dough (sourdough). As determined by R5-based sandwich and competitive ELISAs, the residual concentration of gluten in sourdough was 12 ppm. Albumins, globulins, and gliadins were completely hydrolyzed, while ca. 20% of glutenins persisted. Low-molecular-weight epitopes were not detectable by SCX-LC/CapLC-ESI-Q-TOF mass spectrometry and R5-based Western blot analyses. The kinetics of the hydrolysis of the 33-mer [a peptide] by lactobacilli were highly efficient. All proteins extracted from sourdough activated PBMCs and induced gamma interferon production at levels comparable to the negative control. None of the iTCLs demonstrated immunoreactivity towards pepsin-trypsin digests. Bread making was standardized to show the suitability of the detoxified wheat flour. Food processing by selected sourdough lactobacilli and fungal proteases may be considered an efficient approach to eliminate gluten toxicity.
So we have multiple examples of researchers agreeing it is peptides that are the problem. Need more proof? Let me ask you this: where does most of the damage to the intestines occur in celiac disease? To the villi in the small intestine
. Now take a look at the digestive enzymes wiki and tell me where trypsin comes from. From the pancreas, secreted into the small intestine
Also, small bowel
bacterial overgrowth. Where are they getting the food? Either undigested peptides or undigested starch due to the anti nutrients in food.
I'm sure there's many other examples of diseases that I cannot think of right now. Anyways, I'm inclined to believe that the scientists above are missing the point.
Or maybe not... Maybe enzymes wouldn't help celiacs. Do they put trypsin into supplements? Would it even survive the gut? Enzymes are proteins as well, so my thought is they'd be broken down by pepsin like every other protein. That's probably the reason the pancreas secretes in the small intestine, after the acid is neutralized pepsin wouldn't work anymore.
Anyways, I have a feeling trypsin inhibitors are our main cause of problems right now. Maybe L. plantarum neutralizes these; I'm going to try spitting in the rice I was going to ferment and test it and see what happens. Perhaps L. plantarum hydrolyzes certain peptides, too. Maybe we should spit in our sourdough? Either way it's something worth trying. There's little room for confounding factors, too, since lysozome in saliva (my last point) would prevent other bacteria from taking hold.
It's amazing how widespread fermentation is.
Regimen caveman style: Not washing my face AT ALL currently, helps a lot. (thanks wapak + others)
Also following a no-dairy (trying for no-gluten) low insulin index/glycemic load diet while intermittent fasting, helps tons too.
Researching Th1/Th2 balance currently as well as histadelia.