top of page



Parsley, parsnip, celery



Cooking and phase II liver detox.

Onions, shallots, leeks, chives, scallions, and garlic.


Bad breath, and bad body odor, indigestion, acid reflux, diarrhea, stomach pain, gas, anemia, reduced blood clotting of open wounds., allergic reactions, accidental abortions in humans. Disturbs a baby's ability to breast feed.

Alpha-amylase inhibitor

Partially by cooking, sprouting.

Grains, legumes, nuts skin, stevia leaves.


Dysbiosis (candidiasis). Deleterious histological changes to the pancreas.

Amylase inhibitors: Amylase inhibitors are also known as starch blockers because they contain substances that prevent dietary starches from being absorbed by the body. Starches are complex carbohydrates that cannot be absorbed unless they are first broken down by the digestive enzyme amylase and other secondary enzymes (Marshall and Lauda, 1975; Choudhury et al., 1996). Pigeon pea have been reported to contain amylase inhibitors. These inhibitors have been found to be active over a pH range of 4.5-9.5 and are heat labile. Amylase inhibitors inhibit bovine pancreatic amylase but fail to inhibit bacterial, fungal and endogenous amylase. Pigeon pea amylase inhibitors are synthesized during late seed development and also degraded during late germination (Giri and Kachole, 1998).

Benzyl acetate

Honey, basil, jasmine tea


Caffeic acid

Apple, carrot, celery, cherry, eggplant, endive, grapes, lettuce, pear, plum, potato, absinthe, anise, basil, caraway, dill, marjoram, rosemary, sage, savory, tarragon, thyme, coffee (roasted beans)



Liver and kidneys.

Green potatoes, egg plant, peppers, tomatoes, goji berries.

Calcinosis, muscle pain and tightness, morning stiffness, poor healing, arthritis, insomnia gall bladder problems.


Cooking and phase II liver detox and kidneys.

Alfalfa sprout.


Abnormal blood cell counts, spleen enlargement, Lupus (if big amount of juice sprouts is taken).

L-(+)-(S)-Canavanine is a non-proteinogenic amino acid found in certain leguminous plants. It is structurally related to the proteinogenic α-amino acid L-arginine, the sole difference being the replacement of a methylene bridge (-CH
2- unit) in arginine with an oxa group (i.e., an oxygen atom) in canavanine. Canavanine is accumulated primarily in the seeds of the organisms which produce it, where it serves both as a highly deleterious defensive compound against herbivores and a vital source of nitrogen for the growing embryo[citation needed] (see also L-canaline). The mechanism of canavanine's toxicity is that organisms that consume it typically mistakenly incorporate it into their own proteins in place of L-arginine, thereby producing structurally aberrant proteins that may not function properly.

The toxicity of canavanine may be enhanced under conditions of protein starvation,[1] and canavanine toxicity, resulting from consumption of Hedysarum alpinum seeds with a concentration of 1.2% canavanine weight/weight, has been implicated in the death of a malnourished Christopher McCandless.[2] (McCandless was the subject of Jon Krakauer's book (and subsequent movie) Into the Wild).

Chemical structure of canavanine compared to arginine

Some specialized herbivores tolerate L-canavanine either because they metabolize it efficiently (cf. L-canaline) or avoid its incorporation into their own nascent proteins. An example of this ability can be found in the larvae of the tobacco budworm Heliothis virescens, which can tolerate massive amounts of dietary canavanine. These larvae fastidiously avoid incorporation of L-canavanine into their nascent proteins (presumably by virtue of highly discriminatory Arginine—tRNA ligase, the enzyme responsible for the first step in the incorporation of arginine into proteins). In contrast, larvae of the tobacco hornworm Manduca sexta can only tolerate tiny amounts (1.0 microgram per kilogram of fresh body weight[3]) of dietary canavanine because their arginine-tRNA ligase has little, if any, discriminatory capacity. No one has examined experimentally the arginine-tRNA synthetase of these organisms. But comparative studies of the incorporation of radiolabeled L-arginine and L-canavanine have shown that in Manduca sexta, the ratio of incorporation is about 3 to 1.

Dioclea megacarpa seeds contain high levels of canavanine. The beetle Caryedes brasiliensis is able to tolerate this however as it has the most highly discriminatory arginine-tRNA ligase known. In this insect, the level of radiolabeled L-canavanine incorporated into newly synthesized proteins is barely measurable. Moreover, this beetle uses canavanine as a nitrogen source to synthesize its other amino acids to allow it to develop.[4]

NZB/W F1, NZB, and DBA/2 mice fed L-canavanine develop a syndrome similar to systemic lupus erythematosus,[1] while BALB/c mice fed a steady diet of protein containing 1% canavanine showed no change in lifespan.[5]

Alfalfa seeds and sprouts contain L-canavanine. The L-canavanine in alfalfa has been linked to lupus-like symptoms in primates, including humans, and other auto-immune diseases. Often stopping consumption reverses the problem.[6][7][8]

Role of non-protein amino acid l-canavanine in autoimmunity


Association of SLE and alfalfa was first reported in a volunteer who developed lupus-like autoimmunity while ingesting alfalfa seed for a hypercholesterolemia study. This was corroborated with studies in monkeys fed with alfalfa sprout that developed SLE. Re-challenge with l-canavanine relapsed the disease. Arginine homologue l-canavanine, present in alfalfa, was suspected as a cause. l-canavanine can be charged by arginyl tRNA synthetase to replace l-arginine during protein synthesis. Aberrant canavanyl proteins have disrupted structure and functions. Induction or exacerbation of SLE by alfalfa tablets reported in a few cases remains controversial. Epidemiological studies on the relationship between alfalfa and SLE are sparse. In mice, NZB/W F1, NZB, and DBA/2 mice fed with l-canavanine show exacerbation/triggering of the SLE, however, BALB/c studies were negative.

L-canavanine incorporation may be more efficient in the presence of inflammation or other conditions that can cause arginine deficiency. The l-canavanine induced apoptotic cells can be phagocytosed and a source of autoantigens processed by endosomal proteases. Endogenous canavanyl proteins are ubiquitinated and processed via proteasome. Incorporation of l-canavanine into proteasome or endosome can also cause disruption of antigen processing. Alfalfa/l-canavanine-induced lupus will be an interesting model of autoimmunity induced by the modification of self-proteins at the translational level.


Coffee (roasted beans)



Partially by cooking.

Corn and plants of the Solanaceae family.

Digestive issues.

Chlorogenic acid (caffeic acid)

Apricot, cherry, peach, plum, coffee (roasted beans)


Chlorogenic acid: Sunflower meal contains high levels of chlorogenic acid, a tannin like compound that inhibits activity of digestive enzymes including trypsin, chymotrypsin, amylase and lipase (Cheeke and Shull, 1985). Because chlorogenic acid is uncondensed and non-hydrolyzable, its content of 1% or more of a total of 3-3.5% phenolic compounds in sunflower meal is not reported in tannin assays. Chlorogenic acid is also a precursor of ortho-quinones that occur through the action of the plant enzyme polyphenol oxidase. These compounds then react with the polymerize lysine during processing or in the gut. Although the toxic effects of chlorogenic acid can be counteracted by dietary supplementation with methyl donors such as choline and methionine. Chlorogenic acid is reported to be readily removed from sunflower seeds using aqueous extraction methods (Dominguez et al., 1993)


Cooking and phase II liver detox.

Beans, manioc, and many fruit pits (such as apricot kernels and apple seeds).


Cerebral damage and lethargy.

Cyanogenic glycosides: Some legumes like linseed, lima bean, kidney bean and the red gram contain cyanogenic glycosides from which Hydrogen Cyanide (HCN) may be released by hydrolysis. Some cultivars Phaseolus lunatus (lima bean) contain a cyanogenic glycoside called phaseolutanin from which HCN liberated due to enzyme action, especially when tissues are broken down by grinding or chewing or under damp conditions (Purseglove, 1991). Hydrolysis occurs rapidly when the ground meal is cooked in water and most the liberated HCN is lost by volatilization. HCN is very toxic at low concentration to animals. HCN can cause dysfunction of the central nervous system, respiratory failure and cardiac arrest (D’Mello, 2000).


Orange juice, mango, black pepper



Basil, fennel


Ethyl acrylate




Gluten-containing cereals are a main food staple present in the daily human diet, including wheat, barley, and rye.


Gluten intake is associated with the development of celiac disease (CD) and related disorders such as diabetes mellitus type I, depression, and schizophrenia. However, until now, there is no consent about the possible deleterious effects of gluten intake because of often failing symptoms even in persons with proven CD. Asymptomatic CD (ACD) is present in the majority of affected patients and is characterized by the absence of classical gluten-intolerance signs, such as diarrhea, bloating, and abdominal pain. Nevertheless, these individuals very often develop diseases that can be related with gluten intake. Gluten can be degraded into several morphine-like substances, named gluten exorphins. These compounds have proven opioid effects and could mask the deleterious effects of gluten protein on gastrointestinal lining and function. Here we describe a putative mechanism, explaining how gluten could mask its own toxicity by exorphins that are produced through gluten protein digestion. The precise pathway leading to the development of ACD still needs to be discovered. However, the putative mechanism presented in this review could explain this intruding phenomenon. The incomplete breakdown of the gluten protein, resulting in the presence of gliadin peptides with opioid effects, makes it plausible to suggest that the opioid effects of gluten exorphins could be responsible for the absence of classical gastrointestinal symptoms of individuals suffering from gluten-intake-associated diseases. Moreover, the partial digestion of gluten, leading to DPP IV inhibition, could also account for the presence of extra-intestinal symptoms and disorders in ACD and the occurrence of intestinal and extra-intestinal symptoms and disorders in CD and NCGS patients. If so, then individuals suffering from any of these conditions should be recognized in time and engage in a gluten-free lifestyle to prevent gluten-induced symptoms and disorders.


All natural and unprocessed plants and mushrooms

Diverticular disease, constipation, haemorrhoids, bloating, anal bleeding, abdominal pain, leaky gut syndrome, inflammatory bowel diseases, a host of other autoimmune diseases, bowel cancer, depletes vitamins and minerals from the body


Barley, buckwheat, durum wheat, bulgur, wheat bran, wheat germ, triticale, quinoa, millet, spelt and teff.

Incidentally, antibodies to gliadin are capable of binding to nervous system tissue and may contribute to immune-mediate neurological impairment, such as cerebellar ataxia and gluten encephalopathy. Gliadin, particular the omega fraction, is also responsible for allergic responses, including Bakers� asthma and the odd wheat-dependent, exercise-induced analyphylaxis (WDEIA).)





All wheat, rye and barley plants.

Digestive problems, leaky gut syndrome or autoimmune disease, allergic reactions, and cognitive problems.


Cooking, fermenting.

Soy, peanuts and cruciferous vegetables.




Goitrogenic substances, which cause enlargement of the thyroid gland, have been found in legumes such as soybean and groundnut. They have been reported to inhibit the synthesis and secretion of the thyroid hormones. Since thyroid hormones play an important part in the control of body metabolism their deficiency results in reduced growth and reproductive performance (Olomu, 1995). Goitrogenic effect have been effectively counteracted by iodine supplementation rather heat treatment (Liener, 1975).

bottom of page