Archive for April 2006
Certain bacteria produce the enzyme histidine decarboxylase during growth. This enzyme reacts with free histidine, a naturally occurring chemical that is present in larger quantities in some fish than in others. The result is the formation of histamine. [...]
Once the enzyme histidine decarboxylase has been formed, it can continue to produce histamine in the fish even if the bacteria are not active. The enzyme can be active at or near refrigeration temperatures. The enzyme is likely to remain stable while in the frozen state and may be reactivated very rapidly after thawing.
Freezing may inactivate the enzyme-forming bacteria. Both the enzyme and the bacteria can be inactivated by cooking. However, once histamine is formed, it cannot be eliminated by heat or freezing. After cooking, recontamination of the fish with the enzyme-forming bacteria is necessary for additional histamine to form. For these reasons, histamine development is more likely in raw, unfrozen fish. [...]
The potential for histamine formation is increased when the flesh of the fish is directly exposed to the enzyme-forming bacteria. This occurs when the fish are processed (e.g. butchering or filleting).
At least some of the histamine-forming bacteria are halotolerant (salt-tolerant) or halophilic (salt-loving). This causes some salted and smoked fish products produced from scombrotoxin-forming species to continue to be suspect for histamine development. Further, a number of the histamine-forming bacteria are facultative anaerobes that can grow in reduced oxygen environments. Scombrotoxin Formation in Fish
For those who are curious: no, candida yeasts do not produce significant quantities of amines. In fact, candida growth appears to be inhibited by putrescine and cadaverine, and serotonin. This is not surprising. We have been using yeasts and moulds to kill bacteria and vice versa for over a centuary now.
One more nail in the coffin for those alternative therapists who eagerly diagnose “a candida overgrowth” without any proof, for those of us who are actually experiencing the symptoms of food intolerance and/or intestinal dysbiosis caused by amine-producing bacteria.
Candida is the cholesterol of alternative medicine: it gets blamed for everything.
Different strains of amine producing bacteria grow under different circumstances:
Dimethylamine, methylamine, propylamine, and pyrrolidine were the major amines formed by Bacteroides fragilis NCDO 2217 during the active phase of growth in batch culture. Production of these metabolites was strongly pH dependent and was optimal under acidic conditions (pH 6.0). Low pH also favored the formation of pyrrolidine, cadaverine, and dimethylamine by Clostridium perfringens C523, but the reverse was the case with putrescine, butylamine, and propylamine, where production was maximal at neutral pH. B. fragilis was grown in continuous culture under either starch or casein limitation. Amine formation was influenced by carbohydrate availability and was greatest when the bacteria were grown at high growth rates (dilution rate, 0.20/h) under starch limitation, where they constituted about 18% of the total fermentation products measured. Amine production was optimal and increased concomitantly with growth rate when C. perfringens was grown in glucose-limited continuous culture. Under conditions of high growth rate and glucose limitation, amines accounted for approximately 27% of the fermentation products measured. When glucose in the feed medium was increased from 5 to 15 g/liter, amine production was repressed, and under these nutritional conditions the growth rate had little effect on the process. Influence of pH, nutrient availability, and growth rate on amine production by Bacteroides fragilis and Clostridium perfringens
Acute laminitis has been associated with the overgrowth of gram-positive bacteria within the equine hindgut, causing the release of factor(s) leading to ischemia-reperfusion of the digits. The products of fermentation which trigger acute laminitis are, as yet, unknown; however, vasoactive amines are possible candidates. The objectives of this study were to use an in vitro model of carbohydrate overload to study the change in populations of cecal streptococci and lactobacilli and to establish whether certain species of these bacteria were capable of producing vasoactive amines from amino acids. Cecal contents from 10 horses were divided into aliquots and incubated anaerobically with either corn starch or inulin (fructan; both at 1 g/100 ml). Samples were taken at 6-h intervals over a 24-h period for enumeration of streptococci, lactobacilli, and gram-negative anaerobes by a dilution method onto standard selective growth media. The effects of the antibiotic virginiamycin (1 mg/100 ml) and calcium hydrogen phosphate (CaHPO4; 0.3 g/100 ml) were also examined. Fermentation of excess carbohydrate was associated with increases in numbers of streptococci and lactobacilli (2- to 3.5-log unit increases; inhibited by virginiamycin) but numbers of gram-negative anaerobes were not significantly affected. A screening agar technique followed by 16S rRNA gene sequence analysis enabled the identification of 26 different bacterial strains capable of producing one or more vasoactive amines. These included members of the species Streptococcus bovis and five different Lactobacillus spp. These data suggest that certain bacteria, whose overgrowth is associated with carbohydrate fermentation, are capable of producing vasoactive amines which may play a role in the pathogenesis of acute laminitis. Identification of Equine Cecal Bacteria Producing Amines in an In Vitro Model of Carbohydrate Overload
Bacteroides fragilis and many species of lactobacillus are normal inhabitants of the gut. They produce amines when they are allowed to feed on poorly digested protein, particularly in the presence of carbohydrate fermentation. Bacteria can even liberate phenols from phenol containing amino acids like tyrosine and phenylalanine. It seems that undigested starch and protein can both play a role in the production of amines. I have yet to find any information that implicates fat, since bacteria don’t really digest fat.
These are some statistics from Sue Dengate’s “Fed Up with Asthma”:
In the Children’s Hospital study:
70% of asthmatic children reacted to metabisulphite
20% reacted to salicylates in food
In RPAH studies:
50% of people with food related eczema reacted to salicylates
70% of people with food related irritable bowel (as opposed to non-food factors like stress), headache, or ADHD symptoms reacted to salicylates
Nicotine is an alkaloid found in the tobacco plant, and in the following foods:
- Eggplant (aubergine)
- Capsicum peppers
Nicotine is also used as a pesticide in organic farming, so residues may remain on any vegetables that are not thoroughly washed. (I find it quite disturbing and upsetting that both sulfites and nicotine are allowed in organic farming). Nicotine is extremely toxic. The LD50 of nicotine is around 40-60mg.
Sixty milligrams of nicotine (about the amount in three or four cigarettes if all of the nicotine were absorbed) will kill an adult, but consuming only one cigarette’s worth of nicotine is enough to make a toddler severely ill!
What happens to people after ingesting nicotine? Nicotine poisoning causes vomiting and nausea, headaches, difficulty breathing, stomach pains and seizures. Each of these symptoms can be traced back to excessive stimulation of cholinergic neurons. People poisoned by organophosphate insecticides experience the exact same symptoms. With organophosphates, acetylcholine builds up at synapses and overstimulates the neurons. Because nicotine is so similar to acetylcholine, and binds to cholinergic receptors, nicotine in excess produces the same overstimulation and toxicity. The more nicotine binding to the nicotinic cholinergic receptors, the more acetylcholine is subsequently released and free to activate other subsets of cholinergic receptors. How stuff works
Though many epilepsy charities protest (pathetically) that smoking “does not cause seizures”, the clinical evidence indicates that nicotine can and does cause some kinds of seizures. In fact, nicotine is used to induce seizures in rat models of epilepsy.
Here’s the connection between fibromyalgia and homocysteine.
Studies regarding the correlation between coronary artery disease incidence and abnormally high blood levels of the amino acid homocysteine have been appearing with increasing regularity. Relatively overlooked among the research articles is a recently published Swedish study, the results of which demonstrate consistently high homocysteine levels and low concentrations of vitamin B12 in the cerebrospinal fluid (CSF) of patients meeting established clinical criteria for Chronic Fatigue Syndrome and Fibromyalgia. [...]
SAM is an important cofactor in the metabolism of central nervous system monoamine neurotransmitters, including dopamine, norepinephrine and serotonin. It has also been used successfully to treat both Fibromyalgia and depression. Unfortunately, SAM was not measured in the Swedish study.
Another explanation for high cerebrospinal fluid homocysteine levels was considered by the Swedish authors. Nitric oxide, which is an inhibitor of the enzyme that converts homocysteine to methionine, is produced as a result of inflammatory reactions. Most of the patients in the study, in addition to their neurological condition, had accompanying symptoms of viral or bacterial infections. Theoretically, the inflammation caused by these infections increased nitric oxide levels, which in turn increased homocysteine levels. Immune Support
Interesting. This may explain why I have had some positive results with my 1000mcg methyl-B12 tablets. I wonder if we should reduce nitric oxide levels? And if so, how?
The Wiki entries on nitric oxide and asymmetric dimethylarginine offer a lot of insight.
In the body, nitric oxide serves several roles, mainly involving small blood vessels. Nitric oxide is synthesized from L-arginine and oxygen by various nitric oxide synthase (NOS) enzymes. The endothelium (inner lining) of blood vessels uses nitric oxide to signal the surrounding smooth muscle to relax, thus dilating the artery and increasing blood flow. This phenomenon is thought to be central to endothelial health. A large percentage of humans are deficient in their manufacture of nitric oxide, placing them at increased risk of cardiovascular disease. This underlies the action of nitroglycerin, amyl nitrate and other nitrate derivatives in the treatment of heart disease: The compounds are converted to nitric oxide (by a process that is not completely understood), which in turn dilates the coronary artery (blood vessels around the heart), thereby increasing its blood supply. A chemical known as asymmetric dimethylarginine can interfere with the production of nitric oxide and is considered a marker of cardiovascular disease.
Macrophages, cells of the immune system, produce nitric oxide in order to kill invading bacteria. Under certain conditions, this can backfire: Fulminant infection (sepsis) causes excess production of nitric oxide by macrophages, leading to vasodilatation (widening of blood vessels), probably one of the main causes of hypotension (low blood pressure) in sepsis.
Nitric oxide also serves as a neurotransmitter between nerve cells. Unlike most other neurotransmitters that only transmit information from a presynaptic to a postsynaptic neuron, the small nitric oxide molecule can diffuse all over and can thereby act on several nearby neurons, even on those not connected by a synapse. It is conjectured that this process may be involved in memory through the maintenance of long-term potentiation. Nitric oxide is an important non-adrenergic, non-cholinergic (NANC) neurotransmitter in various parts of the gastrointestinal tract. It causes relaxation of the gastrointestinal smooth muscle. In the stomach it increases the capacity of the fundus to store food/fluids. Nitric Oxide
Asymmetric dimethylarginine (ADMA) is a naturally occurring chemical found in blood plasma. It is a metabolic by-product of continual protein modification processes in the cytoplasm of all human cells. It is closely related to L-arginine, a conditionally-essential amino acid. ADMA interferes with L-arginine in the production of nitric oxide, a key chemical to endothelial and hence cardiovascular health. [...]
Asymmetric dimethylarginine is created in protein methylation, a common mechanism of post-translational protein modification. This reaction is catalyzed by an enzyme set called S-adenosylmethionine protein N-methyltransferases (protein methylases I and II). The methyl groups transferred to create ADMA are derived from the methyl group donor S-adenosylmethionine, an intermediate in the metabolism of homocysteine. (Homocysteine is an important blood chemical, because it is also a marker of cardiovascular disease). After synthesis, ADMA migrates into the extracellular space and thence into blood plasma. [..]
ADMA concentrations are substantially elevated by native or oxidized LDL cholesterol. Thus a spiralling effect occurs with high endothelial LDL levels causing greater ADMA values, which in turn inhibit NO production needed to promote vasodilation. The elimination of ADMA occurs through urine excretion and metabolism by the enzyme dimethylarginine dimethylaminohydrolase (DDAH). The role of homocysteine as a risk factor for cardiovascular disease is suggested to be mediated by homocysteine down-regulating production of DDAH in the body. Asymmetric Dimethylarginine
The “cardiovascular” effect of NO is basically vasodilation. Asymmetric dimethylarginine is being painted as a bad guy for reducing vasodilation in people with heart disease, however, too little is as bad as too much.
I wonder if too much nitric oxide is a problem, particularly as an inhibitor of the enzyme that converts homocysteine to methionine, as per my last post. The fact that ADMA is produced in the presence of SAM (derived from methionine) when methylation is increased, is part of an interesting feedback loop that could be out of sorts.
If levels of nitric oxide are a problem, I wonder if this would explain why nitrate and nitrite additives cause reactions in the food chemical intolerant, by further supplying fuel to the NO fire? Or are nitrates interfering with the production of NO and the opposite is true? This is of course pure speculation. Nitric oxide may just be a symptom of something else. It would also contradict the asthma issue, for which nitric oxide is extremely important in relaxing the bronchi.
Unfortunately for those of us relying on potatoes, one of the highest sources of natural nitrates and nitrites (even higher than the average additive-containing slice of bacon) is potatoes grown in artificially fertilised soil.
Folks with food chemical intolerance tend to have too much vasoconstriction: histamine, serotonin, dopamine, and tyramine all have vasoactive effects and lead to some of the unpleasant effects we experience, from skin flushing and inflammation, to varicose veins and headaches. Tyramine is a vasoconstrictor. Histamine is supposed to have mediatory effects. Perhaps nitric oxide levels are high for the same reason? And this then inhibits methylation?
Serotonin has a perverse effect, it can produce both vasoconstriction and vasodilation, depending on the receptors present. Serotonin migraines seem to be produced firstly by constriction, then the pain occurs on dilation.
I’m being controversial again. I seem to find myself nit-picking over details. I’m told it’s bad form to quote oneself. With that in mind, here’s what I just posted on LCHF:
I feel somewhat misinterpreted again: I didn’t say calories don’t count, I said they aren’t the one and only factor.
The basal metabolic rate of normal, healthy adults with normal thyroid hormone levels still varies between +/- 15% of the mathematic calculation. A calculator might calculate you to have a BMR of 1,800 kcals, but different individuals of the same weight, size, age and activity level may burn anywhere between 1,530 – 2070 kcals per day in reality.
This is even before we consider individuals with an underactive thyroid, who may burn as much as 25% less energy than predicted. The same study you describe that shows the clear underreporting in energy intake in obese patients (presumably “The Calorie: Myth, Measurement and Reality“) admits this metabolic fact but sweeps it under the rug. Furthermore, the study only deals with subjects who are maintaining their weight, not with what happens when calories are genuinely reduced. Nor does it consider that obese patients may be reporting lower calorie intakes to scientists and doctors because they feel ashamed, it doesn’t necessarily mean they are underreporting those additional calories to themselves.
I should be eating around 1,800 kcals a day to maintain my weight, yet I maintain my weight on 2,000 kcals a day, and I maintain my weight on 1,500 kcals a day. I don’t lose weight until I go as low as 1,200-1,300 kcals a day. I use scales religiously when I want to lose weight. This suggests to me at least that my metabolism varies on demand to keep me in a status quo.
Starvation and serious or abrupt calorie restriction can dramatically reduce BMR by up to 30%. Low calorie diets can cause a drop by as much as 20%, which is why people experience stalls on genuine calorie restriction. There are numerous other issues that affect the metabolic rate: exercise, genetics, sex hormones, thyroid hormones, external temperature, illness, insulin, and nutrients like vitamin A, zinc, iodine, calcium, magnesium.
The study concludes: “Although our results strongly indicate that [the 17] patients referred to us for disturbances in body weight regulation were underreporting their food intake, we did observe one patient with a resting and total energy expenditure 25% below that predicted based on body composition. It is thus possible to have a modest reduction in energy requirements, and more research is needed to explore the underlying causes of a low resting metabolic rate in the presence of normal serum thyroid hormones.” It neither mentions nor explains the +/- 15% that is so important to most normal individuals, instead singles this patient out as being some sort of freak of nature, which is a distortion of fact.
The “modest reduction in energy needs” referred to is the whopping difference between me eating 1,800 kcal a day or eating 1,350 kcal a day.
Caloric control isn’t about a fine line (1 kcal over or under 1,800 would cause weight gain or loss), it’s a wide band, for which most people must transgress +/- 15% to see weight gain or loss. The occasional pat of butter is irrelevant.
This page has a slightly broader view:
Fat loss = 12 – 13 calories per lb. of bodyweight
Maintenance (TDEE) = 15 – 16 calories per lb. of bodyweight
Weight gain: = 18 – 19 calories per lb. of bodyweight
If I reduced my calories to 1,550 a day, I should lose half a pound a week, right? Well I don’t. If I increase my calories to 2,000 a day, I should gain half a pound a week, right? Well I don’t.
I lost 12 pounds in two weeks when I first went on Atkins. There is no way on this earth that 8-10 pounds of that was water weight. Sure, I ate less. But I didn’t eat THAT much less. At the start of my fat fast, I lost weight too quickly, then my weight loss slowed down to a crawl and I repeatedly plateaued on an average of 1,200 kcals per day. I went cold, and I had to add high-calorie days back in to get my weight to shift.
You must push beyond that 15% band to lose weight: sometimes people have a band of 20-30%, which makes life hell. But woe betide you if you push too far beyond the band, because your metabolism suffers long term.
As yet there are no studies to determine BMR variation in one individual during calorie restriction in a calorie chamber. So what evidence do we have?
Well, there are studies like this that show the effects of micronutrients on BMR. And in athletic women with menstrual disorders. Studies of fat free mass show big differences in BMR. Elderly Italians have a significantly lower BMR than matched elderly French, independently of the measured thyroid hormones (the French of course eat more fat, and Italians more carbohydrate). There are studies that show differences in BMR in acutely ill patients. And reductions in the BMR of mice on calorie restricted diets. And this study claims a reduction of BMR of 25% in fasting patients, but no change in those who eat a very low calorie diet, though thyroid hormones are changed in both groups!
Messageboards are so bad for me. I have to stop reading them and posting replies.
I finally had a “Fed Up” book arrive the other day. At last. They’re like gold dust. Or rocking horse droppings. Amazon decided they couldn’t get them after all. I’ve had to order a couple second hand direct from Australia.
Yep, decaf coffee bothers me. I had some more yesterday and before I’d even finished it the inside of my nose was inflamed. Thanks to Annabelle I now know why – apparently my fine organic swiss water decaf filter coffee has more salicylates than the harsh chemically decaffeinated instant stuff. No more coffee for me. I’m now limited to warm milk when I want something hot. I can see myself in Nonna’s now: could I have a latte without the coffee in it?
I read a bit of hearsay in Karen DeFelice’s book that TMG might actually make autism worse. This fits the theory that overdosing one part of the cycle can cause a block in another part. In this case (potentially) the methyl donors remethylating homocysteine and the presence of glycine dragging cysteine into glutathione formation, could cause a lack of sulphate to be available for use in phenol detoxification. It’s a very tricky balance. Depending on one’s symptoms and one’s particular reactions, this could be a make or break situation with the supplements.
I’ve got to clean up my diet before I can continue with the vitamin experiments. I’ve transgressed every day since my partner got back from India. I was irritable yesterday and the day before. I’ve been running on about 60-70% most days. I haven’t had any really bad days, but my head is full of “noise” at the moment.
I’m stopping all the vitamins as of tomorrow until I clean things up. I still have to get my supplements right, but I can’t do it while I’m still reacting to foods and smells. My face hasn’t been so great the last week or two, but I can’t separate that from all the transgressions. Probably everyone needs different amounts of different supplements, and I’ve been getting very big doses of B12 and B6 because I can’t get them smaller!
Vaseline: I have been using this in tiny amounts on my face because someone mentioned it on the Fed Up site as a lip moisturiser. However I’m unhappy with the smell (strong, unpleasant) and the potential chemistry of it. As a mineral oil it may contain benzenes. I think I am going to swap over to pure glycerin. I’m also going to get hold of some pure lanolin from Soap Kitchen and try that. When I was in France I used to use olive oil on my face. I suppose butter is also an option. Before moisturisers were invented, people used to use goose grease. Theoretically the oils of low salicylate plants should work. Wheatgerm oil? Mango butter?
There’s a lot of confusion around regarding what animal foods are allowed on the elimination diet and how long they should be kept before discarding. I thought I’d go through a few points.
Most failsafers are fine with fresh milk, cream, and butter. There are other problems with dairy that I’ll deal with elsewhere (allergy, additives, salicylates, opioids). Sue Dengate says that extra-sensitive amine responders will not manage sour cream or sharp yoghurt. I sometimes appear to have a very small response to these items. Some amine responders will manage fresh cheeses like mascarpone, ricotta, or cream cheese. Failsafers should not eat cheese.
Fresh eggs keep well. I have not knowingly experienced any egg-related reactions yet. Raw egg whites can trigger histamine release in some people. They can also contain food colourings if the birds have been fed rubbish. Stick to organic eggs.
Fish decays very rapidly after it has been caught and is a very common source of histamine reactions. Most sources recommend it be eaten within 24-36 hours of being caught. The ‘fishy’ smell we associate with fish is in fact from the breakdown of the proteins into amines (in this case trimethylamine). Fresh fish does not smell fishy. I invariably react to oily fish, and find the taste unpleasant. Fresh white fish, crab, oyster, lobster, mussels, and scallops are low in amines. Prawns (which may also be sprayed with sulphites), and dark/oily fish like salmon, tuna, mackerel and sardines are high in amines. Smoked, canned, or preserved fish is liable to cause greatest problems. Smoked fish like kippers often have bright yellow food dyes added. Farmed salmon are often fed carotinoid food dyes in order to increase the colouring of their flesh but these should be safe. Farmed fish are also regularly fed chicken manure! RPAH say that fish frozen within 12 hours of being fished will be low enough in amines to be failsafe for two weeks.
Joan Breakey allows fresh pork, but most other sources say that pork and pork products are high in amines. Ham, bacon, sausages, and other preserved pork products are high in amines and contain additives like nitrates, nitrites, sulphites, and MSG (‘seasonings’). Fresh pork is lower in amines than these sources. Today I ate fresh pork and experienced a brief spell of itchiness and urticaria. This was in no way comparable in severity to the powerful histamine reactions I have had from other foods like aged beef. I have been trying to figure out why pork should be high in amines. Whilst all meats differ in composition to some extent (different ratios of amino acids, different amounts of vitamins, for example: pork is very high in thiamin compared to other meats), surely it is abnormal for an animal to have vast quantities of amines racing around its system? Perhaps there are metabolic differences in pigs that we are unaware of, or perhaps their meat is subject to more rapid decay after death – called autolysis, this is the process by which the body’s own enzymes begin to digest the body.
Game is usually hung to aide the development of ‘gamey‘ flavours. In the past pheasants would sometimes be hung by the neck until the body fell off! Game is hung in normal, cool outdoor weather conditions from anywhere between two days to three weeks, with one week being the average. Remember game season is the late autumn/early winter months, so the game does not overtly rot in the heat but is still allowed to auto-digest. Despite this game is high in amines.
Beef is qute tough and ‘needs’ to be hung to tenderise before eating, though the length of time it is hung varies. Whilst Palaeolithic man usually ate his meat before it had even entered rigor mortis, nowadays we don’t have that option unless we hunt it ourselves. Beef marketed as ‘quality’ beef is often hung for as much as six weeks in a refrigerator, but more usually three. By contrast supermarket beef is rarely hung properly at all, but is instead vacuum packed and stored for as much as three months before going on sale. This three month timespan is quite normal, not the exception! There is therefore not really any difference between the two extremes. Small butchers sometimes operate differently. Beef may only be hung for a week or so, some may not even hang the beef at all before sale. Our local organic farm sends their beef cows off to slaughter every fortnight on the Monday morning, hangs the beef until the end of the week, and then vacuum packs it and puts on sale. This means I don’t usually eat beef that is older than one to two weeks. Unfortunately, I think the meat still suffers for being vacuum packed, and I don’t think their refrigerator is cold enough either!
Lamb is not hung to nearly the same extent as beef and whilst supermarket sources are likely to be totally untrustworthy, independent butchers and farm shops can provide a safe alternative. Lamb is also thought to be the least allergenic meat.
Poultry usually has a very short time from slaughter to sale as it is not hung like red meat. There are concerns about chicken skin. Why chicken skin should be high in amines I don’t know, but again this may be an issue of quality. The organic chicken I eat is killed and plucked on the farm without ever being commercially processed. Commercial poultry is kept in dreadful conditions, the diet is high in grains and deficient in insects to make the meat tender. Poultry frequently have their beaks removed in order to prevent birds from pecking each other’s feathers out. Factory processing of birds involves hot liquid baths to remove the feathers. Carcasses are injected with legal and illegal mixtures of salt, water, MSG and even beef and pork proteins which may be high in amines and glutamates. Choose your chicken from a clean, trustworthy source, not from your local supermarket unless it is organic.
Offal like liver, kidney, and presumably brains(!) is typically higher in amines than other flesh meats due to the function of the organs in the body. Not only do organ meats contain some natural amounts of amines, organs generally contain higher levels of enzymes, and so undergo autolysis at an increased rate. I first noticed unpleasant itching and headache reactions to liver and kidneys over two years ago, long before I started the failsafe diet.
Most sites suggest that fresh meat should be eaten the day it is bought and stored for no longer than two to four weeks in the freezer. Ideally cooked meat should be eaten the same day. Cooked meat can be refrozen. Canned or preserved fish or meat should not be eaten.
Some people’s advice on amines goes to extremes. Some people need to be extremely careful, but others don’t. It is worth everyone trying to be very careful with amines for a couple of weeks to see if they affect any lingering symptoms. If you are unable to find a fresh source of red meat you may want to try restricting to fresh fish, chicken and eggs for a fortnight.
Autolysis is self-decomposition by enzymes that exist in the tissues. As well as being formed via autolysis, amines are also formed when bacteria break down proteins. The types and amount of bacteria present and the environmental conditions influence the amounts of amines. Different bacteria degrade foods in different ways and have different potential to form amines. Putrefaction is an anaerobic rotting of organic matter that produces ammonia and hydrogen sulphide as byproducts. Fermentation on the other hand is a different process that produces carbon dioxide and water as byproducts. Both form amines. Some amines are particularly associated with putrefactive bacteria (putrescine, cadaverine, histamine, spermidine, and spermine). An interesting subject, about which little is known.
Amines can also be formed by certain bacteria in the bowel under certain conditions. Eating an excess of protein (from any source) that is not digested properly will aide the formation of amines and hydrogen sulphide. This is a reason not eat meat or other protein foods to excess. However, amine formation is quite slow, and the amine-degrading enzymes are at their highest concentration in the bowel. You are more likely to react to a large single dose of ingested amines that exceeds your body’s enzyme making capacities than to a chronic very low-level production in the bowel, as your body should be able to keep up with this.