It is important how food is prepared, whether it’s cooked or eaten raw.

Cultures came up with elaborate preparation methods to mitigate the antinutrients and enhance the nutrient bioavailability of grains. Traditional cultures who ate grains managed to stay relatively free of degenerative diseases through traditional grain preparation, including soaking, sprouting, and fermentation. Each step alters the nutritional experience of the grain to varying degrees, making it more digestible, less toxic, and tastier.

Traditional cultures used soaking and sprouting, followed by fermentation to make grains less toxic and more digestible.

Soaking and Sprouting
The grains are covered with water, placed in a preferably warm place, and soaked for between 12 and 24 hours. After soaking, you drain them, rinse them, and let the grains sit out for a couple days. To get grains to sprout, rinse and drain them a couple times each day until sprouts emerge.

Fermentation
After soaking and grinding, grains are traditionally mixed with a starter culture or allowed to wild ferment. Starter cultures often include whey, kefir, yogurt, or left over fermentation medium from the previous batch. Wild fermentation occurs when the grain mixture employs bacteria already present on the grains, or picks up wild yeasts and bacteria from the environment. Both methods are far more effective than just soaking and sprouting at deactivating antinutrients and improving digestibility. Plus, fermentation lends interesting flavors to and enhances the shelf-life of the resultant food (which was extremely valuable in the days before refrigeration and canning).

What is toxic in grains?

Gluten: Found in wheat, rye, durum, spelt, kamut, semolina and barley. Gluten is a composite formed from several different proteins. Gluten adds texture and chewiness to baked goods, and is used in a wide variety of other foods as a thickener and binder, flavor enhancer, and protein supplement. Some people can develop an intolerance to these proteins. Fermentation can break down gluten, but not all of it.
Soaking and sprouting effect on gluten: Sprouting reduces gluten to some extent, but not by very much.
Fermentation effect on gluten: No store bought garden variety sourdough you find is going to be gluten-free. A team from Italy was able to produce a gluten-free sourdough wheat bread by using specific bacterial strains from all over the world and subjecting the bread to many days of fermentation. The process was totally unfeasible for the home or average commercial baker. There’s also a guy who sells monthlong fermented sourdough bread out of LA-area farmers’ markets and claims celiacs can eat it without issue. Reviews on Yelp seem to corroborate. Maybe I’ll swing by his stand and give it a shot, but I’m skeptical. And besides, I’m personally more worried by WGA, which is biologically active at nanomolar concentrations and which may not be fully degraded by fermentation.

Foods containing gluten used to enhance the flavor and protein of foods, as well as to bind and thicken their consistency, the grains are often found in breakfast cereals and various baked goods, Used as a thickener, gluten can be found in soups and broths, as well as gravies and sauces such as ketchup, salad dressings, or marinades. Since it enhances flavor, it is used in bouillon, spice blends, and other foods such as coffees, dairy products, vinegars, and liquors. It can also be found in the substance used to seal envelopes since it acts as a stabilizer.


Phytic acid: Phytic acid is the main storage form of phosphorus in grains. Phytate also binds to many minerals, including zinc, magnesium, calcium, and iron, to name several. And, since non-ruminants don’t possess phytase, which digests phytate and releases the bound minerals for easy absorption, eating large quantities of phytate-containing foods results in mineral deficiencies for meat-eating apes. These deficiencies, taken to an extreme, can manifest as tooth decay, which might explain why early grain eating populations had worse teeth than the hunter-gatherers who preceded them.
Soaking and sprouting effects on phytate: If the grain contains phytase, some of the mineral-binding phytic acid will be deactivated, but not much. And if the grain has been heat-treated, which destroys phytase, or it contains very little phytase to begin with, the phytic acid will remain completely intact. Overall, neither soaking nor sprouting deactivates a significant amount of phytate.
Fermentation effects on phytate: Phytase is an enzyme that deactivates phytate, and it really gets cooking during fermentation. In grains that contain high amounts of phytase, like wheat, rye, and buckwheat, a day of fermentation deactivates most of the phytate. To degrade the phytate in low-phytase grains, however, the fermentation time must be extended. Adding small amounts of phytase-containing grain to the mix will also speed up the process. Increasing the temperature also improves phytate breakdown. In millet, a low-phytase grain, it took 72 hours to completely degrade the phytate. In wheat, it took ten hours to reach a maximum of 88.8% phytate reduction using a specific bacterial strain. Standard quick rise baker’s yeast only reduced 16% of phytate (that’s what 99% of wheat eaters are eating nowadays, remember!). Ten hours may not always be enough, however.

Enzyme inhibitors: Grains are seeds that require certain wet, nutrient rich conditions for proper growth. Spontaneous germination is counterproductive, so enzyme inhibitors prevent it. When moisture abounds (like, when soaking grains), the inhibitors are deactivated and sprouting occurs. Certain enzyme inhibitors also inhibit our ability digest the grains.
Sprouting and soaking effect on enzyme inhibitors: When the seed has been placed in a wet medium and allowed to sprout, the enzyme inhibitors are obviously mostly deactivated. Digestion is much improved (cooking will improve it further).
Fermentation effect on enzyme inhibitors: Fermentation also significantly reduces enzyme inhibitor activity but it is important to know that it has different effects on different enzyme inhibitors in different grains. In 24 hour traditional sorghum fermentation, both trypsin inhibitor and amylase inhibitor (which impedes starch digestion) were reduced by up to 58% and 75%, respectively. In millet, a 48 hour fermentation was required to completely deactivate amylase inhibitor. One study found that 48 hours of fermentation resulted in maximum wheat starch digestibility, presumably by deactivating amylase inhibitor.

Lectins: Lectins are nature’s pesticides, protecting the tiny grain from predation. They can perforate the intestinal lining, disrupt our immune systems, and there’s even evidence that they bind to leptin* receptors in the hypothalamus (potentially triggering leptin resistance).
Sprouting and soaking effect on lectins: It seems to depend on the grain. Sprouted wheat, for example, is extremely high in WGA, the infamous wheat lectin. As the wheat grain germinates, the WGA is retained in the sprout and is dispersed throughout the finished plant. In other grains, sprouting seems more beneficial, but there’s always some residual lectins that may need further processing to deactivate.
Fermentation effect on lectins: Fermentation reduces lectin load fairly comprehensively across the board, but it takes a long time. In lentils (I know, not a grain, but with similar antinutrient issues), 72 and 96 hours of fermentation at 42 degrees C eliminated 98% and 97.8% of the lectins, respectively. Overall, fermentation appears to be pretty effective at reducing lectins (and cooking reduces them further).


White rice (the sole grain that requires no elaborate processing).

Read more: http://www.marksdailyapple.com/soaked-sprouted-fermented-grains/#ixzz2HEWimPzQ


*Leptin
is a hormone that monitors how much energy an organism takes in. It surveys and maintains the energy balance in the body, and it is secreted by fat cells to regulate hunger by counteracting the effects of neuropeptides that are feeding stimulants secreted by the hypothalamus and specific gut cells (neuroppetide & and anandamide (the bliss hormone)) and promotes the production an appetite suppressant (a-MSH). Leptin signals that the body has adequate adipose tissue (energy) stores and that the body has had enough to eat. Both are supposed to result in the reduction in appetite. It is also important for fertility, libido, immunity, and even puberty. If insufficient energy is available to the body, the body down-regulates all the “extra” stuff, like reproduction, sex drive, puberty, and immunity, while the presence of leptin indicates sufficient energy, enough to spend on other bodily functions and physiological processes. That might explain why heavier kids reach puberty earlier than leaner kids. The loss of menstrual cycles in women and reduced sex drive in both men and women who reach extremely low body fat levels might also be explained by low leptin levels.

Leptin also responds to short-term energy balance. It’s the hunger hormone. Overfeeding temporarily boosts leptin, reducing hunger.

If leptin is absent, feeding is uncontrolled and relentless.

In normally healthy people, if leptin is present and receptors in the hypothalamus are sensitive, feeding is inhibited. More body fat means less food is required, and so leptin is secreted to inhibit feeding and the accumulation of excess adipose tissue.

In overweight people, there is a high level of circulating leptin. Even though overweight have a high level of circulating leptin, they are less receptive to it, and there is a disruption of the leptin pathway.

In leaner people, there is a lower leptin level. A severe caloric deficit will result in reduced leptin secretion – this is your body’s way of getting you to eat when you need energy.

Signs seem to point to leptin resistance and leptin sensitivity as being dependent on the dietary environment we provide. As long as they do not stray far from their evolutionary diets, wild animals do not have damaged metabolisms, and the leptin pathway is preserved. Most modern humans, having strayed far from their evolutionary diets, are metabolically deranged, with misguided or disrupted leptin pathways.

If hunger is a challenge to you, how to maintain adequate levels of leptin without growing resistant to its effects:

Watch Your Fructose Intake
In rats, fructose feeding inhibits leptin receptors. Rats on the fructose diet gained even more weight when switched to a high-fat diet.
Fructose appears to affect the leptin pathway in two ways: fructose directly renders the hypothalamus resistant to leptin and high blood triglycerides – brought on by a high fructose intake – block the passage of leptin to the brain. High triglycerides actually physically prevent leptin from passing through the blood-brain barrier, and the leptin that does get through elicits a poor response from leptin receptors.

A high-fat, low-carb, low-fructose diet generally decreases serum triglycerides and increases satiety; perhaps the lower triglycerides are allowing more leptin to pass through and inhibit hunger. The fructose found in reasonable amounts of fruit shouldn’t affect leptin sensitivity.

Avoid Lectins
Lectins, specifically those from cereal grains, may be direct causes of leptin resistance. Wheat germ agglutinin, or WGA, (a lectin present in wheat, barley, and rye) actually binds directly with the leptin receptor and prevents leptin binding.

Get Good Sleep
We know that getting adequate sleep is an important primal law, and inadequate sleep can lead to excessive levels of cortisol, which can induce insulin resistance and (especially in the belly) weight gain, but we also know that sleep deprivation has been linked to lowered serum leptin.

Get eight-ish hours a night and try avoiding late night electronic usage, which can disrupt sleep patterns.

Avoid Severe Calorie Restriction
Too much dieting inhibits leptin secretion. In fact, drastic reductions in caloric intake reduce leptin levels, faster than could be explained by body fat losses (the same goes for overfeeding, which increase leptin levels faster than can be explained by body fat gain). This can make getting really lean really difficult – the leaner you get and the less you eat, the lower your leptin gets and the more your appetite increases. Anyone who’s dieted knows that sheer intellectual willpower cannot win out against the hormonal urge to eat. Hormones always win.
Read more: http://www.marksdailyapple.com/leptin/#ixzz2HEYWYQDR