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#1 nowash

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Posted 02 February 2010 - 11:35 PM

This might explain some things. Shoot me if you've heard this one before.

So today I recently just tested sunflower seeds and concluded that they did cause irritation. Thing is though, I sprouted, fermented, and roasted them long enough so that I could see if the lectins would be reduced, yet they still bother me. I decided to search for some more research on lectins, but as before, there were still no real explanations to be had except from the alternative medicine scene. It's ridiculous how split the two forces of medicine are today, wouldn't you agree? Anyways so I let my mind wonder a bit and was looking up recipes for fermented rice, my next test.

All the traditional culture got me to wonder why anyone would ferment a grain such as rice when it would be quicker to cook it straight off the plant. Then an idea came to me and I typed in "does fermenting reduce food allergies?" and sure enough there was research (finally!). Research such as this on soy: http://www.agweb.com...x?pageid=141576. It's funny how we're learning to re-feed ourselves as a race.

Anyways the second link that came up was this:

http://www.eufic.org...gy-intolerance/

QUOTE
3.4.3. Other common food allergens

Other foods that are more likely to be associated with allergic reactions include fruits, pulses (including soya beans), eggs, crustacean (crab, crayfish, lobster and shrimps), fish and vegetables, sesame seeds, sunflower seeds, cottonseed, poppy seeds and mustard seed. The allergenic capacity of some food allergens is destroyed by cooking and food processing, when the proteins are denatured. Newer processing techniques, such as high-pressure treatment of foods, fermentation and enzyme treatment, can help to reduce the allergenicity of some food proteins. Moreover, allergens can be removed from oils by refining. Some of the unresolved problems of food allergy are concerned with the presence of low amounts of a given allergen in processed foods or recipe dishes served out of home.


I always thought it was a queer idea how someone could suddenly stop making enzymes. I'm sure it's possible, such as lactase, but that makes sense to me since adults don't shouldn't be still drinking their mother's milk (yeurk). I guess it's more of a chronic irritation thing, like SweetJade and others beat to death, but I've never heard it explained this way, or rather connected this way.

So instead of killing candida in your blood (looool.) maybe enzymes are just breaking down food allergens? Also there are studies that show certain parasites in the gut as well as certain bacteria modulate the immune system (hygiene hypothesis as well?). Well maybe everyone is allergic to these things, just to a certain degree, and perhaps the organisms are just reducing the allergen content, IOW clipping the troublesome proteins into amino acids before they can cause a problem? Also, the more stimulated one part of the immune system, the more down-regulated others are and more so up-regulated it is (ie Th1/Th2 balance).

There is no lack of enzymes (other than anti-amylases and the sort), just that foreign ones break down allergens. So what say you, holisticans? Enzymes digest allergens, Y/N?

#2 AussieSmile

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Posted 03 February 2010 - 12:50 AM

I loved reading this post, thank you nowash. I assume your talking about digestive enzymes here. Modern day food as you know is insanely processed (heated, oiled, fried, destoryed e.t.c), one result of this tampering is a loss of enzymes. Enzymes are most prominent in raw foods which can be properly digested.

I think that they definitely help with allergens but maybe indirectly? I mean, D. enzymes break nutrients into smaller molecules for better absorption, otherwise the food would putrefy inside the digestive tract which = toxins=bad! So D.enzymes help regulate and improve digestion, break down food and eliminate/decrease allergens? eusa_eh.gif

BTW, if you have food sensitivities such as to nuts, this is generally due to leaky gut.

#3 alternativista

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Posted 03 February 2010 - 08:23 AM

Well, the allergens are protein which the enzymes breakdown. Also, lectins are proteins, and the highest lectin containing foods also happen to be the most allergenic foods. Some of the articles on lectins that I posted in the ZAG enzyme thread also mentioned that candida diets tend to avoid most lectins and that is probably what is really helping.

Edited by alternativista, 04 February 2010 - 10:40 AM.


#4 Dotty1

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Posted 03 February 2010 - 08:48 AM

I wanted to mention that "enzymes" are listed as a probable source of gluten for those of you who are gluten-sensitive. You must call the enzyme company and ask if a gluten-containing grain was used, if it was used as a by-product or if it is in one of the ingredients.

#5 Dotty1

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Posted 03 February 2010 - 08:54 AM

"So instead of killing candida in your blood (looool.) maybe enzymes are just breaking down food allergens?"

For me, that appears to be what is happening. I read that protein must be broken down into amino acids before entering the blood stream. If it isn't broken down, water follows protein (literally), pushing its way through tiny capillaries that aren't meant to carry that much water. This is one of the causes of edema around acne sites (mine would fill up with 1-2 marble-size lumps of water!).

It is like my body has an "allergic reaction" to ANY protein not broken down into amino acids. It has also become worse over the years, perhaps starting with meat and then including nuts, lentils, soy, etc. In the end, it was all protein sad.gif.

Why it only causes breakouts on the face, I do not know. But for me, it is obvious that the protein must be broken down into amino acids if I am to have clear skin.

Edited by Dotty1, 03 February 2010 - 08:57 AM.


#6 nowash

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Posted 03 February 2010 - 09:28 AM

Ahh I think I had a small breakthrough. Here's something, from the first study I found, except elaborated:

http://www.soya.be/s...soy-allergens-f

QUOTE
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:

http://en.wikipedia....illus_plantarum

QUOTE
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.[1] 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:

http://en.wikipedia.org/wiki/Chicha

QUOTE
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:

http://en.wikipedia....igestive_enzyme

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:

QUOTE
Oral cavity

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 α-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.

Stomach

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

Small intestine
Pancreatic enzymes

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:

http://www.ncbi.nlm....mp;ordinalpos=6

QUOTE
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:

http://www.ncbi.nlm....=pmcad6_article

QUOTE
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, Facoltà 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.


And lastly:

http://www.ncbi.nlm....mp;ordinalpos=4

QUOTE
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.

Holisticans?

#7 alternativista

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Posted 04 February 2010 - 11:15 AM

L. plantarum , Lactobacillus brevis and others are in my probiotic which I add when I make yogurt, which I add when soaking things.

The strain name L. sanfranciscensis is amusing. It must have been originally identified in sourdough starter associated with San Francisco. Like yogurts made with L bulgaricus and S thermophilus, referring to Bulgaria/Eastern Europe and Greece.

You should look into what bacteria are involved in traditional fermented soy products.

Here's a WHO report that I don't have time to read, but might have some useful info specific to anti-nutrients/allergens.

http://www.who.int/f.../probiotics.pdf

Edited by alternativista, 04 February 2010 - 11:36 AM.


#8 LiliVG

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Posted 04 February 2010 - 04:40 PM

I've been wondering if we are suffering from some kind of complex carbohydrate deficiency.

Nature is full of all kinds of complex sugars, some of which we absorb, some of which we don't and are not meant to. Not everything we consume gets used for nutrition purposes. For instance, D-mannose is a complex sugar that is not digested in the gut. Instead, it gets absorbed into the blood stream within 15 minutes, and is very quickly excreted by the kidneys, mostly within an hour. The interesting thing about this though, is that D-Mannose naturally prevents urinary tract infections. E.Coli are responsible for 90% of UTI's, and D-mannose gums up e.coli bacteria rendering them unable to stick to the cells walls in your bladder. The bacteria and the d-mannose get flushed away when you pee. I have used D-Mannose to clear up a UTI, and it is very effective, my UTI was gone in 3 days.

That's just one example that we know of. Over hundreds of thousands of years of a diet high in a multitude of natural complex sugars performing any number of functions, our body likely came to rely on them. But now suddenly, all of our carbohydrates are refined, complex carbohydrates are missing, and any number of problems could result.

And this is a subject that hasn't been studied in depth. There is an assumption that if we don't digest something, it serves no purpose. But I disagree. A urinary tract infection can lead to a kidney infection, and a kidney infection can kill you. If you are eating something every day that is naturally protecting you from that, you will be more likely to survive and have children, and feed them what you eat, etc. generation after generation who's very survival may in fact hinge on the protective benefits of a complex sugar that we supposedly don't "use" because our digestive system doesn't break it down. I think our digestive system doesn't break it down because it's far more useful as it is than for the small number of calories that may be gained by converting it to glucose.

#9 alternativista

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Posted 04 February 2010 - 05:01 PM

QUOTE (LiliVG @ Feb 4 2010, 04:40 PM) <{POST_SNAPBACK}>
I've been wondering if we are suffering from some kind of complex carbohydrate deficiency.

Nature is full of all kinds of complex sugars, some of which we absorb, some of which we don't and are not meant to. Not everything we consume gets used for nutrition purposes. For instance, D-mannose is a complex sugar that is not digested in the gut. Instead, it gets absorbed into the blood stream within 15 minutes, and is very quickly excreted by the kidneys, mostly within an hour. The interesting thing about this though, is that D-Mannose naturally prevents urinary tract infections. E.Coli are responsible for 90% of UTI's, and D-mannose gums up e.coli bacteria rendering them unable to stick to the cells walls in your bladder. The bacteria and the d-mannose get flushed away when you pee. I have used D-Mannose to clear up a UTI, and it is very effective, my UTI was gone in 3 days.

That's just one example that we know of. Over hundreds of thousands of years of a diet high in a multitude of natural complex sugars performing any number of functions, our body likely came to rely on them.


I just posted something along those lines in the ZAG thread. Specific sugars bind up specific lectins. Sugars that probably aren't in white flour, white sugar or white potatoes, which are all the carbs so many people eat and the majority of the carbs most people eat.


Edited by alternativista, 04 February 2010 - 05:34 PM.


#10 alternativista

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Posted 04 February 2010 - 05:49 PM

QUOTE (LiliVG @ Feb 4 2010, 04:40 PM) <{POST_SNAPBACK}>
I've been wondering if we are suffering from some kind of complex carbohydrate deficiency.

Nature is full of all kinds of complex sugars, some of which we absorb, some of which we don't and are not meant to. Not everything we consume gets used for nutrition purposes. For instance, D-mannose is a complex sugar that is not digested in the gut.


Speaking of Mannose, here's a list of 'eight essential sugars' and some food sources.

http://heartspring.n...nt_sources.html


#11 alternativista

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Posted 04 February 2010 - 06:10 PM

QUOTE
Mucin, like lectin, is a glycoprotein in the mucous lining of the intestines. When lectins travel through the intestines, they should have mucin to bind to, rather than intestinal cells. But if mucin is missing, lectins will bind to intestinal cells instead.

http://www.acne.org/...p...t&p=2800233

Article says that gut flora is the answer.

Edited by alternativista, 04 February 2010 - 06:22 PM.


#12 Dotty1

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Posted 04 February 2010 - 06:37 PM

I am becoming more and more suspicious that I have a gluten-sensitivity. Up to 30% of the Caucasian population in some areas of Europe have it.

Such a sensitivity could easily diminish flora and everything else that is related to healthy digestion. So I am cutting out gluten now and now I can concentrate on the flora and digestive problems caused by years of gluten. Do I purchase gut flora in pill form? eusa_think.gif

Edited by Dotty1, 04 February 2010 - 06:39 PM.


#13 nowash

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Posted 04 February 2010 - 11:48 PM

QUOTE (alternativista @ Feb 4 2010, 07:10 PM) <{POST_SNAPBACK}>
QUOTE
Mucin, like lectin, is a glycoprotein in the mucous lining of the intestines. When lectins travel through the intestines, they should have mucin to bind to, rather than intestinal cells. But if mucin is missing, lectins will bind to intestinal cells instead.

http://www.acne.org/...p...t&p=2800233

Article says that gut flora is the answer.

Mmm, yeah perhaps, but I don't think flora help make mucin directly. Seems like they're just a buffer since bacteria cell walls are made up of NAG which is what wheat and some other lectins bind to.

Could be why probiotic pills help people a lot, too. They're in a pill, how could anything survive? or survive your gastric acid? To me it makes most sense that they're dead; all it is is just a glorified NAG supplement. Same with any probiotic I bet.

And dotty I can't believe you haven't given up gluten. Geezus.

#14 nowash

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Posted 05 February 2010 - 10:07 AM

Wow, so I just tested the spit-fermented rice and it reduced the effects tremendously.

It may have been a fluke, but this is high glycemic white rice that had been grounded down into a mush. Even more, I had about 300 calories worth, which about one serving normally (150 cal) would cause horrible problems. It smelled like horrible cheese, but tasted just like a normal block of rice. I'm going to try fermenting some masa flour and see if it helps.

#15 acne_combat

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Posted 05 February 2010 - 11:01 AM

Hey, great topic!
But I'm a bit lost here... My question is: why do acne-patients lack those enzymes then? Is it hereditary or could it be because of external influences like mercury toxicity for example?
Also, I don't know what to conclude of this, please help:
- are non-refined carbs actually good for you then?
- is candida real?
- what foods should be eaten?

I'm really confused atm confused.gif

#16 alternativista

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Posted 05 February 2010 - 11:24 AM

QUOTE (acne_combat @ Feb 5 2010, 11:01 AM) <{POST_SNAPBACK}>
Hey, great topic!
But I'm a bit lost here... My question is: why do acne-patients lack those enzymes then? Is it hereditary or could it be because of external influences like mercury toxicity for example?
Also, I don't know what to conclude of this, please help:
- are non-refined carbs actually good for you then?
- is candida real?
- what foods should be eaten?

I'm really confused atm confused.gif



Lots of people lack enzymes not people with acne. That's why they have allergies, IBS and other digestion problems and all kinds of health issues.

One reason is the lack of them in our diet which tends to be low in raw or not overcooked veggies and fruit with other foods like grains and nuts, dairy, etc heat treated until everything is dead.

Edited by alternativista, 05 February 2010 - 11:32 AM.


#17 nowash

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Posted 05 February 2010 - 12:03 PM

QUOTE (acne_combat @ Feb 5 2010, 12:01 PM) <{POST_SNAPBACK}>
Hey, great topic!
But I'm a bit lost here... My question is: why do acne-patients lack those enzymes then? Is it hereditary or could it be because of external influences like mercury toxicity for example?
Also, I don't know what to conclude of this, please help:
- are non-refined carbs actually good for you then?
- is candida real?
- what foods should be eaten?

I'm really confused atm confused.gif

No, they do not lack the enzyme, they are inhibiting the enzyme. They still have it (trypsin), it just can't work since the anti-nutrients are inhibiting it (specifically trypsin inhibitors). You'll want to degrade those anti-nutrients by fermenting. If you've read anything about Weston A. Price's observations, it'll make more sense.

Either that or inhibit the lectins by consuming the sugars that bind them at the same time, which is what alternativista is promoting in her ZAG enzyme thread. Thing is, I'm not sure if your amylase digests those sugars therefore rendering them useless. Perhaps you'll have to cook the lectins and them together.

Either way, my theory was trying to prove why digestive enzymes work (Virastop, etc.).

I'm not so sure about non-refined carbs yet. Most if not all major civilizations milled their grains (Egypt and wheat, Asia and rice, Aztecs and corn), but another half ferment, too. There are even cases where they milled and fermented (Egypt again, India with Idli or Dhokla). I really hate the idea of throwing away nutrients in bran, but there seem to be major benefits to it. IBS sufferers cannot STAND any kind of that fiber, from what I know, but if it were the lectins instead that are the problem, perhaps we could ferment whole grains. Keep the nutrients and inhibit the lectins. Lectins are most concentrated in the germ and bran though. Tell you what, I'll try fermenting brown rice the same way I did white and tell you if I see the same benefits.

IMO, candida is a big ol' bag of B.S. that naturopaths use to get you to buy their products. I don't doubt the anti-candida diets work, though, since they avoid lectins. In retrospect, candida should be GOOD for you since the chitin in all fungi contains NAG which inhibits some lectins. But then I don't understand how sourdough bread is better than yeasted bread, specifically in the insulin index. If both yeast and bacteria contain NAG, shouldn't they both be effective in inhibiting WGA?

If you want to try a diet, go for the low lectin/elimination/failsafe diet. It's similar to the paleo diet, except you avoid nuts and seeds as well. So avoid: dairy, all grains, all nuts, all seeds, all legumes, and the nightshade family. Anything that causes inflammation get rid of. Anything that causes indigestion get rid of. Cook all your foods. I have personally cleared up with a red meat/leafy greens/sweet potato/carrots/salmon diet, but that's expensive as hell so I'm testing foods. I have broken out yet again just from sunflower seeds, white rice, and masa/cornmeal.

#18 alternativista

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Posted 05 February 2010 - 12:14 PM

QUOTE (nowash @ Feb 5 2010, 12:03 PM) <{POST_SNAPBACK}>
But then I don't understand how sourdough bread is better than yeasted bread, specifically in the insulin index. If both yeast and bacteria contain NAG, shouldn't they both be effective in inhibiting WGA?


They probably do, but not in the hour they get to work before being killed in today's bread making methods. Before instant yeast, it used to take at least overnight to raise bread.

Did you see the link to a method for fermenting whole brown rice that Venem posted to the ZAG thread? It's in the first couple of pages.

#19 nowash

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Posted 05 February 2010 - 12:17 PM

QUOTE (alternativista @ Feb 5 2010, 12:24 PM) <{POST_SNAPBACK}>
QUOTE (acne_combat @ Feb 5 2010, 11:01 AM) <{POST_SNAPBACK}>
Hey, great topic!
But I'm a bit lost here... My question is: why do acne-patients lack those enzymes then? Is it hereditary or could it be because of external influences like mercury toxicity for example?
Also, I don't know what to conclude of this, please help:
- are non-refined carbs actually good for you then?
- is candida real?
- what foods should be eaten?

I'm really confused atm confused.gif



Lots of people lack enzymes not people with acne. That's why they have allergies, IBS and other digestion problems and all kinds of health issues.

One reason is the lack of them in our diet which tends to be low in raw or not overcooked veggies and fruit with other foods like grains and nuts, dairy, etc heat treated until everything is dead.

Eh? You still think we get enzymes from foods? Only people with rare genetic disorders lack necessary enzymes (except lactose intolerant people). I think we might get some unknown nutrient from raw food, but not enzymes. I think the raw-food diet only works because it avoids lectins. Enzymes could work on the food itself (like after crushing, soaking), but you'd still be able to cook them as they already did their job. I doubt we utilize enzymes from food in our gut.

Any luck on that traditional food combination theory, though? I know that Norse peoples used to ferment shark underground, which one of the sites you linked mentioned shark cartilage as major source of N-acetylglucosamine and N-acetylgalactosamine. I also know Weston Price utilized bone broth (bovine connective tissue) as part of his dental caries regimen. I also know bone broth is said to help heal celiacs faster. Lard (connective tissue?) is traditionally put on bread. Whey contains slialic acid(?) which binds to WGA(?) along with NAG. Also tomatoes and mushrooms. Can't think of anything else.

#20 nowash

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Posted 05 February 2010 - 12:35 PM

QUOTE (alternativista @ Feb 5 2010, 01:14 PM) <{POST_SNAPBACK}>
QUOTE (nowash @ Feb 5 2010, 12:03 PM) <{POST_SNAPBACK}>
But then I don't understand how sourdough bread is better than yeasted bread, specifically in the insulin index. If both yeast and bacteria contain NAG, shouldn't they both be effective in inhibiting WGA?


They probably do, but not in the hour they get to work before being killed in today's bread making methods. Before instant yeast, it used to take at least overnight to raise bread.

Did you see the link to a method for fermenting whole brown rice that Venem posted to the ZAG thread? It's in the first couple of pages.

Oh right right, duh. Always wondered why you had to pound down the dough 3 times, too.

And yeah, I saw it. Good stuff.

I still need to read half the things you've guys have linked, as well as try to do my own research. I think it's ridiculous lectins do not get any kind of media attention or acknowledgment from mainstream medical. Seems like the cause of so many problems, and just that one .pdf you linked describes how it all fits together. Didn't realize the lectins attached to so many things, including mucin. That lets certain bacteria get into our body through the gut, which have been implicated in autoimmune diseases, including psoriasis, as well as IBS. Explains why there's an epidemic in diabetes and IBS (55% in Mexico, seriously) in latin american countries. It's not just the bacteria. SweetJade's posts always made it seem like the inflammation itself was causing leaky gut, which I couldn't explain to myself as to why.

It explains SO many things, yet it sounds SOO damn crazy. I saw a short latino chick in class the other day, cute as hell, but she had this little peach fuzz thing going on which reminded me of SweetJade's posts. I thought about telling her about gluten and dairy and I wondered if either it'd be rude as hell or helpful to try to explain things to her. I wonder if I could even explain it at all. If I told her, she'd probably think I was a nut.