20121007

ERYTHROPOIETIN (EPO)

ERYTHROPOIETIN (EPO) is a naturally occurring hormone that stimulates the production of red blood cells (RBC). EPO levels up to 48% safely improve performance in males, however beyond this level, the risk of compromised health increases.


Erythropoietin (EPO) is most commonly known as the cytokine secreted by the kidneys that stimulates red blood cell production and is used as a drug for the treatment of anemias. Epo is also secreted in the brain in response to hypoxia, such as ischemic stroke. Epo production in the brain is stimulated by the hypoxia-inducible transcription factor HIF-1 (see HIF pathway). Administration of Epo to the brain in rodents before hypoxic stress or other neuronal stresses is neuroprotective, preventing neuronal apoptosis. The erythropoietin receptor (EpoR) is known to associate with JAK kinases that phosphorylate and activate the STAT family of transcription factors (See Epo pathway). The neuroprotection by Epo involves cross-talk between Epo receptor and anti-apoptotic pathways through activation of NF-kB by the JAK2 kinase (see NF-kB pathway). Epo stimulates JAK2 phosphorylation of I-kB, releasing NF-kB to translocate into the nucleus and activate transcription of neuroprotective genes. Neuroprotective genes activated by NF-kB include the anti-oxidant enzyme manganese superoxide dismutase and calbindin-D(28k). The erythropoietin receptor is also essential for proper brain development in mice. The absence of EpoR causes high levels of neuronal apoptosis in the developing mouse brain, further confirming the important role of Epo as a neuroprotective agent.

What nutritional protocol safely increases natural production of EPO?

Erythropoietin is a glycoprotein hormone produced in the kidneys containing a 165-amino acids structure. Most erythropoietin is produced by the kidney's renal cortex. But some is also produced in the liver (mainly in the fetus), the brain and uterus. Erythropoietin production is stimulated by low oxygen levels in interstitial cells of the peritubular capillaries in the kidneys. Following its production in the kidneys, EPO travels to the bone marrow where it stimulates production of red blood cells.[2] In the absence of erythropoietin, only a few RBC's are formed by the bone marrow. EPO increases the blood-oxygen carrying capacity but only up to a point, but beyond, it may compromise health and hinder blood flow dynamics with performance-limiting implications.


EXCESS EPO CAN BE LETHAL

The margin between effective and lethal quantities of EPO is very narrow. EPO use can be LETHAL (many athletes seeking to derive its performance-enhancing effects have died from incorrectly-administered EPO. Inappropriate use of exogenous Erythropoietin can cause elevated Hematocrit levels (i.e. thickened blood is difficult to pump). Elevated EPO increases the risk of heart attack (due to the increase in hematocrit). Exogenous EPO is totally cleared from the urine within 48 hours of its administration and is cleared from the blood within 72 hours of its administration (although its physiological effects prevail for several months).[3]

ERYTHROPOIETIN (EPO) LEVELS INCREASE DURING HYPOXIC EXERCISE AND PLASMA VOLUME DEPLETION

Roberts et al. examined exercise-induced hypoxemia (EIH) and plasma volume contraction as modulators of serum Erythropoietin (EPO) production. Five athletes cycled for 3 min at supra-maximal power outputs, at each of two different elevations (1,000 and 2,100 meters). Five subjects were exposed to normobaric hypoxia (F(I)O(2)=0.159), seven subjects underwent plasmapheresis[7] to reduce plasma volume and eight subjects were time controls for EPO levels. Oxyhemoglobin saturation was significantly reduced during exercise and during normobaric hypoxia. The time period of haemoglobin oxygen saturation <91% was 24+/-29 s (mean+/-S.D., n=5) for exercise at 1000 m, 136+/-77 s (mean+/-S.D., n=5) for exercise at 2100 m and 178+/-255 s (mean+/-S.D., n=5) with resting hypoxic exposure. However, significantly increased serum EPO levels were observed only following exercise (21-27% at 1,000 m and 31-41% at 2,100 m). Volume contraction also resulted in increased serum EPO 29-41% in spite of a significant rise in hematocrit of +2.2%. Despite similar degrees of arterial desaturation, only the hypoxemia induced by exercise was associated with an increase in serum EPO. This finding indicates that other factors, in addition to hypoxemia, are important in modulating the production of EPO in response to exercise. Volume depletion in the absence of exercise resulted in increases in EPO levels that were comparable with those observed in response to exercise. The paradoxical responses of increased hematocrit and increase in EPO in subjects undergoing plasmapheresis suggests that plasma volume may also modulate the production of EPO.[8]

does exercise intensity increase erythropoietin?

Roberts & Smith measured the effects of exercise-induced hypoxia on the physiological production of erythropoietin. Twenty athletes exercised for 3 min at 106-112% maximal oxygen consumption. Estimated oxyhemoglobin saturation was measured by reflective probe pulse oximetry (Nellcor N200) and was validated against arterial oxyhemoglobin saturation by CO-oximetry in eight athletes. Serum erythropoietin concentrations-as measured using the INCSTAR Epo-Trac radioimmunoassay-increased significantly by 19-37% at 24 h post-exercise in 11 participants, who also had an arterial oxyhemoglobin saturation < or = 91%. Decreased ferritin levels and increased reticulocyte counts were observed at 96 h post-exercise. However, no significant changes in erythropoietin levels were observed in nine non-desaturating athletes and eight non-exercise controls. Good agreement was shown between arterial oxyhemoglobin saturation and percent estimated oxyhaemoglobin saturation (limits of agreement = -3.9 to 3.7. They concluded that a short 3 minutes supramaximal exercise period could induce both hypoxemia and increased erythropoietin levels in well-trained individuals. The decline of arterial hypoxemia levels below 91% during exercise appears to be necessary for the exercise-induced elevation of serum erythropoietin levels. Furthermore, reflective probe pulse oximetry was found to be a valid predictor of percent arterial oxyhemoglobin saturation during supramaximal exercise when percent estimated oxyhemoglobin saturation > or = 86%.[9]

Fitness of these athletes provides a physiological environment for increasing EPO naturally from short 3-minute all-out intervals.

DIETARY INTERVENTIONS REDUCE ANEMIA AND INCREASE OXYGEN CARRYING CAPACITY

COMMON CAUSES OF ANEMIA

Red blood cells carry iron-rich hemoglobin for up to 120-days, then they die. Unless there is a continual supply of Iron, Vitamin B-12, Vitamin C and Folacin, anemia and reduced oxygen carrying capacity appear in two forms:

1.      Low red blood cell count

2.      Malformed red blood cells.

Iron deficiency anemia is the most common form of anemia. Approximately 20% of women, 50% of pregnant women, and 3% of men are iron deficient. Iron is an essential component of hemoglobin, the oxygen carrying pigment in the blood. Iron is normally obtained through the food in the diet and by the recycling of iron from dying "retired" red blood cells. The causes of iron deficiency are iron-poor food, lead poisoning, chemotherapy, dehydration, poor absorption of iron from food or supplements, and blood loss. Anemia develops slowly, after the normal stores of iron from the body tissues and bone marrow are reduced to low levels. Women, in general, have smaller stores of iron than men and experience increased blood loss through menstruation, placing them at higher risk for anemia than men. Runners are also reported to lose more blood during heel strike during gait motion than cyclists, whose impact riding is noticeably less than running. In men and postmenopausal women, anemia is usually due to gastrointestinal blood loss associated with ulcers, nonsteroidal anti-inflammatory medications (NSAIDS), or colon cancer.

High-risk groups include:

1.      Women of child-bearing age who have blood loss through menstruation

2.      Pregnant or lactating women who have an increased requirement for iron

3.      Infants, children, and adolescents in rapid growth phases

4.      People with poor dietary intake of iron through little or no eggs, meat for several years.

5.      Blood loss from peptic ulcer disease, long term aspirin/NSAIDS, colon cancer

6.      Cancer-related drug therapy & chemotherapy

7.      Athletes whose sport requires running

WHAT IS THE EFFECT OF EXERCISE ON EPO (HEMATOCRIT)?

The paradox of hematocrit in exercise physiology is that artificially increasing it by autotransfusion or erythropoietin doping improves VO2 max and performance, while in normal conditions there is a strong negative correlation between hematocrit and fitness, due to a training-induced "Autohemodilution". Brun et al. reported that in professional soccer footballers:

        Physiological values of hematocrit in athletes were comprised between 36 and 48%

        Low hematocrit (<40%) was associated with a higher aerobic capacity

        Subjects with the higher hematocrits (>44.6%) were frequently overtrained and/or iron-deficient, and their blood viscosity (and red cell disaggregability) tended to be increased.[10]

Over the past 9 years several endurance athletes have complained of low hematocrit levels. In 6 elite endurance athletes ranging from 31-67 years age, hair lab analysis showed iron deficiency, in spite of a calorie-sufficient dietary iron intake. Proper nutrition permits the body to set optimal natural (EPO) hematocrit levels. The diet should contain specific blood-iron building blocks, first from whole foods, second from supplements. However, an athlete should not take supplemental iron unless prescribed and monitored by a physician.

SYMPTOM-SPECIFIC EPO DEFICIENCY

The rate hematocrit increases varying specific to the individual but it may be improved applying dietary interventions with hypoxic interval sessions. The same dietary intervention that relieves Anemia is the protocol for increasing blood oxygen capacity of any endurance athlete. The most common cause is iron-deficiency anemia in red blood cells, smaller than usual and pale in color due to improper amounts of hemoglobin (the molecule in red blood cells that binds to oxygen and carries it in the blood).


Lack of iron for hemoglobin

CAUSES:

1.      Loss of iron from the body due to blood loss

2.      Poor absorption of iron from one's diet

3.      Lack of dietary iron

4.      Radiotherapy or Chemotherapy

5.      Anti-cancer drugs

6.      Certain types of viral infections

7.      Genetic reasons

8.      A result of malaria

9.      AIDS

10.  A deficiency of Vitamin B-12

11.  A deficiency of folic acid

12.  An imbalanced ratio of B-12:Folate

SYMPTOMS OF ANEMIA

  • Tiredness and weakness
  • Lethargy
  • Dizziness, shortness of breath, and palpitations(rapid heart rate)
  • Headaches
  • Pale complexion
  • Brittle nails (due to lack of iron)
  • Irritability
  • Sore tongue
  • Unusual food cravings (called pica)
  • Decreased appetite
  • Headache - frontal
  • Blue tinge to sclerae (whites of eyes)
  • There may be no symptoms if anemia is mild.

NUTRITION BUILDING BLOCKS INCREASE EPO

Protein adequacy is a factor in erythropoietin (EPO) production. Inadequate protein nutrition can reduce the EPO produced. The erythroid response to Erythropoietin (EPO) is highly dependent on dietary protein adequacy and quality. The mouse spleen is an erythropoietic organ, which contains an EPO-responsive cell population that can be easily amplified by administration of the hormone. Researchers determined the effect of a protein-free diet offered freely to mice up to two days after injection of r-Hu EPO (1000mU/200 ul) on the response of the above population. Splenic cell suspensions from control and experimental mice were prepared in microwells containing 400 mU r-Hu EPO and appropriate medium. The response to EPO was evaluated in terms of 3H-thymidine uptake. The results obtained indicate that acutely induced protein restriction suppressed the response of the EPO-responsive splenic cell population to EPO when it was imposed on mice immediately after hormone injection, and suggest the appearance of deficient rates of differentiation of erythropoietic units by protein restriction.[11]

Adequate dietary protein intake is 1.4-1.7 grams/kilogram body weight per day for an endurance athlete.


Inadequate dietary iron; Food sources of iron are red meat, liver, and egg yolks. Most flour, bread, and cereals are iron-fortified. If the diet continues to be iron-deficient, only a physician should prescribe and supervise iron supplementation.

Calorie inadequacy is a secondary factor in EPO production including red blood cell quality and quantity. In order to test the hypothesis that the early cessation of erythropoietin (Ep) production during hypobaric hypoxia is induced by lowered food intake, researchers compared the plasma Ep titer of rats after exposure to continuous hypoxia (42.6 kPa = 7000 m altitude) for 4 days with that in fed or fasted rats after exposure to discontinuous hypoxia. They found that plasma Ep was rather low after 4 days of continuous hypoxia. However, the Ep titer significantly rose again, when rats were maintained normoxic for 18 h and then exposed to repeated hypoxia for 6 h. Because this was also found in rats, which were deprived of food during the normoxic interval and the second hypoxic period, they concluded that the fall of the Ep titer during continuous hypoxia is not primarily due to reduced food intake. In addition, these findings show that fasting per se lowers the EPO-response to hypoxia in normal rats but not exhypoxic rats.[12] Calorie sufficiency (in spite of exercise expense) is required for optimal EPO-release. If training is causing weight loss, then EPO loss may be occurring.

HORMONE & GLUCOSE IMPACT EPO LEVELS

IRON ABSORPTION RATE EFFECTS ERYTHROPOIETIN RELEASED

Dietary interventions significantly advance nonheme iron absorption rate during EPO production. It is very important to include foods to enhance nonheme iron absorption, especially when an exercise-induced iron loss is high or when no heme iron is consumed, such as in a vegetarian diet. Absorption of heme iron is very efficient; the presence of red meat increases absorption of non-heme iron +400%. Only 1-7% of the nonheme iron in vegetable staples in rice, maize, black beans, soybeans, and wheat are absorbed consumed alone. Vitamin C improves the rate of absorption of nonheme iron from red meats. Diets that include a minimum of 5 servings of fruits and vegetables daily provide adequate vitamin C to boost nonheme iron absorption. Calcium, polyphenols, tannins from tea, and phytates (a component of plant foods), rice, and grains inhibit the absorption of nonheme iron. Some of the protein found in soybeans inhibits nonheme iron absorption. Most healthy individuals maintain normal iron stores when the diet provides a wide variety of foods. However, if the diet contains large amounts of oxalates and phytates from dark green leafy vegetables and whole cereal grains the absorption of iron decreases due to binding with iron in the gut. High absorption of heme iron is further advanced by foods containing vitamin C in an acid environment found of the stomach. The recommended for daily iron intake is between 10-18 milligrams for adult males and postmenopausal females. Most endurance athletes consume too much iron. Iron is added to breads, cereals, and most packaged foods.


From a computer-generated dietary analysis on 16 endurance athletes and 9 non-athletes, iron intake from their reported food intake was assessed. The results of this data collect follows:

GROUP

PERCENT DAILY IRON (RDI/RDA)

MALE ENDURANCE ATHLETE

279%

FEMALE ENDURANCE ATHLETE

193%

MALE SEDENTARY

158%

FEMALE SEDENTARY

115%








FOOD COMBINATIONS THAT INFLUENCE IRON ABSORPTION

Diet then likely provides enough iron, but how foods are combined may affect iron absorption rate. Excess iron overdose is unhealthy and should be avoided. Common side effects of acute iron overload are gastro-intestinal pain, constipation, nausea, and heartburn. Excess iron levels may generate a continuous low-grade infection. Foods are the best source of iron. The best food source of iron is liver and red meats. These foods contain heme iron, which is better absorbed than non-heme iron. Non-heme iron can be found in dark green, leafy vegetables (spinach, chard and kale) and whole cereal grains (bran and whole wheat bread). Include dark green, leafy vegetables and whole cereal grains in the daily diet. Oxalates and phytates found in dark green leafy vegetables and whole cereal grains decrease the absorption of iron because they bind with iron in the gastrointestinal tract. Iron fortified cereals increase iron from the diet. Anemia may develop on a meat-free diet and/or if the iron store or intake is low.


Red meat contains arachidonic acid, an EPO-precursor nutrient, but it also contains high levels of saturated fats and cholesterol suggesting a little (now and then) is good but too much will harmfully compromise cardiovascular lipid levels. Adding iron to the diet in supplemental form is not recommended except under the supervision of a physician who is monitoring blood serum levels for a specific outcome. It has been shown that eating red meat 1-2 per week may contribute to providing substrates known to regenerate EPO as shown in animal research. The ability of Arachidonic Acid (AA), the bisenoic prostaglandin precursor to stimulate erythropoiesis and Erythropoietin (EP) Production in exhypoxic polycythemic mice and the programmed isolated perfused canine kidney was found to stimulate erythropoiesis when administered to exhypoxic polycythemic mice in the lowest dose tested (50 microgram/kg i.p.). Endogenously synthesized prostaglandins, their intermediates and/or other products of AA metabolism, such as prostacyclin and prostaglandins play an important role in the control EPO production.[14] Hematocrit levels are restored through the supplying dietary or supplemental specific substrates to support the body's natural EPO-producing mechanisms during endurance exercise stress.

SUBSTRATES ASSIST ERYTHROPOIETIN [EPO] METABOLISM[15]

  1. Acidophilus - 15-30 Billion Count Probiotics
  2. Coenzyme Q10 - 150-300 mg daily
  3. Garlic - 2 cloves or 2 capsules up to 3 x day
  4. Kelp - 100-225 micrograms
  5. Vitamin B6 - 50-100 mg
  6. Vitamin B12 - 200-1,000 mcg
  7. Folic Acid - 800 mcg
  8. Proteolytic enzymes - Bromelain & Papain
  9. Selenium - 200 mcg
  10. Vitamin A - 15,000 IU daily or Beta Carotene - 25,000 IU daily
  11. Vitamin B Complex - 50-100 mg
  12. Vitamin C plus Bioflavonoids - 1-3 grams (divided dose)
  13. Vitamin E - 400 IU daily
  14. Copper - 2 mg
  15. Zinc 40 mg daily ---->(Do not take zinc in amounts over 40 mg daily as it may interfere with metabolism of iron and copper)

DIETARY RECOMMENDATIONS

There is a method to improve iron uptake in the absence of oxalate or phytate rich foods previously mentioned above If hematocrit, hemoglobin, or ferritin blood lab measures are low, the athlete may add 1-gram vitamin C to a 3-4 ounce lean cut of red meat cooked in an iron skillet 1-2 each week.. A complete dietary protocol for cancer patients going through chemotherapy and radiation was published and is applicable to over trained endurance athletes who present low hematocrit levels.[16]

CONCLUSIONS

Nutritional imbalance from caloric restriction (or exercise related expense), dehydration, fluid intoxication, excess calcium, excess inositol, excess oxalates foods[17], excess phytic acid from cereal grains[18], or a lack of hypoxic (interval training) are factors that inhibit the natural production of Erythropoietin (EPO).

Manipulating diet for protein and total calorie adequacy, monitoring hydration, supplements, timing food combinations, adding weekly hypoxic exercise followed by easy or rest days increases the release of natural EPO for healthy maximal oxygen carrying capacity. When individual hematocrit exceeds 48%, the risk of insulin resistance syndrome and stroke exponentially increase. Men with hematocrits above 48 percent have a 400% increased risk of non-insulin-dependent-diabetes mellitus. This research followed over 7,000 middle-aged men for more than 12 years, and discovered that the risk of diabetes increases proportionate to hematocrit increase.[19] [20] The upper recommended levels for a female is slightly lower at 45%.

This nutritional intervention parallels exercise intensity s effect for increasing EPO. Nutritional and training interventions for resolving low EPO levels during iron supplementation (only prescribed by a physician who should monitored progress) should not be permitted above a reference range of 48% in males and 45% in females. Similar research confirms this report.[21] [22] [23]

Source 1,

Raw Fresh Produce vs. Cooked Food


Eighty million species on earth (about 700,000 of which are animals) thrive on raw food. Only humans apply heat to what they eat. Humans on average as a race, die at or below half their potential life span of chronic illness that is largely diet and lifestyle related. Domesticated pets also are fed cooked, processed, packaged food that likewise is denatured by heat. As a consequence, they suffer human-like chronic ailments including cancer, arthritis and other degenerative diseases.
The typical species in its natural pristine environment lives seven times past its age of maturity. Humans normally mature in their late teens to early twenties. Our average potential life span in robust wellness is actually in the range of 120-140 years. This is never actualized due to the effects of heating food and not learning to skillfully handle psychological stress through self-mastery (see Essentials of Health). Humans have been on earth for millions of years. Prior to mastering fire perhaps less than 10,000 years ago, humans thrived on a diet of nothing but fresh, live, unfired foods as furnished by nature in their whole unadulterated state.
Presently, humans apply heat to the bulk of their food day in and day out prior to consumption. Like eating ash from the fireplace, microscopic burnt nutrients are toxic. Slowly and silently as the decades pass, the harmful effects of consuming these toxins accumulate. Humans are biologically adapted to raw fresh produce (see: Biological Adaptations: Diet is Species Specific). Eating raw fresh produce as a staple rather than cooked food keeps your body vibrantly healthy at nearly any age.
Scientific Research Proves Raw Food Protects Against Cancer and Heart Disease
Scientific evidence shows that raw vegan diets decrease toxic products in the colon (From: J Nutr 1992 Apr;122(4):924-30). Shifting from a conventional diet to an uncooked vegan diet reversibly alters fecal hydrolytic activities in humans, according to researchers, Ling WH, and Hanninen O, of the Department of Physiology, University of Kuopio, Finland. Results suggest a raw food uncooked extreme vegan diet causes a decrease in bacterial enzymes and certain toxic products that have been implicated in colon cancer risk.
Researchers have also found that a diet rich in raw vegetables lowers your risk of breast cancer, and eating lots of fruit reduces your risk for colon cancer, according to a study published in the May 1998 issue of the journal Epidemiology. Including fresh fruit as part of your daily diet has been associated with fewer deaths from heart attacks and related problems, by as much as 24%, according to a study published in the September 1996 issue of the British Medical Journal.

Excessive Heat Denatures Nutrients
Burn your finger and skin tissue dies. Overly apply heat to food and nutrients are progressively destroyed. Fresh food prior to wilting or rotting sustains life to a high degree of wellness. Harvested food from field and orchard provides raw materials to replenish your cells and tissues. Overly cooking food destroys live plant and animal tissue whose nutrients no longer bear any relationship to your living body. A diet containing an abundance of raw, unfired food maximizes well being.
The chemical changes that take place to individual nutrients, as excessive heat is applied will now be examined. It is well understood and recognized in scientific literature that heat breaks down vitamins, amino acids and produces undesirable cross-linkages in proteins, particularly in meat. When food is cooked above 117 degrees F for three minutes or longer, the following deleterious changes begin, and progressively cause increased nutritional damage as higher temperatures are applied over prolonged periods of time: proteins coagulate, high temperatures denature protein molecular structure, leading to deficiency of some essential amino acids, carbohydrates caramelize, overly heated fats generate numerous carcinogens including acrolein, nitrosamines, hydrocarbons, and benzopyrene (one of the most potent cancer-causing agents known), natural fibers break down, cellulose is completely changed from its natural condition: it loses its ability to sweep the alimentary canal clean 30% to 50% of vitamins and minerals are destroyed, 100% of enzymes are damaged, the body’s enzyme potential is depleted which drains energy needed to maintain and repair tissue and organ systems, thereby shortening our life span,  pesticides are restructured into even more toxic compounds, valuable oxygen is lost, free radicals are produced, cooked food pathogens enervate the immune system, heat degenerates nucleic acids and chlorophyll, cooking causes inorganic mineral elements to enter the blood and circulate through the system, which settle in the arteries and veins, causing arteries to lose their pliability, the body prematurely ages as this inorganic matter is deposited in various joints or accumulates within internal organs, including the heart valves.
As temperature rises, each of these damaging events reduces the availability of individual nutrients. Modern food processing not only strips away natural anti-cancer agents, but searing heat forms potent cancer-producing chemicals in the process. Alien food substances are created that the body cannot metabolize.
For example, according to research performed by cancerologist Dr. Bruce Ames, professor of Biochemistry and Molecular Biology at University of California, Berkeley various groups of chemicals from cooked food causes tumors: Nitrosamines are created from fish, poultry or meat cooked in gas ovens and barbecues, as nitrogen oxides within gas flames interact with fat residues; Hetrocyclic amines form from heating proteins and amino acids; Polycyclic hydrocarbons are created by charring meat; Mucoid plaque, a thick tar-like substance builds up in the intestines on a diet of cooked foods. Mucoid plaque is caused by uneliminated, partically digested, putrefying cooked fatty and starch foods eaten in association with protein flesh foods; Lipofuscin is another toxin: an accumulation of waste materials throughout the body and within cells of the skin, manifesting as spots in the liver as liver and in the nervous system including the brain, possibly contributing to ossification of gray matter and senility.

From the book Diet, Nutrition and Cancer published by the Nutritional Research Council of the American Academy of Sciences (1982) and the FDA (Food and Drug Administration) Office of Toxicological Sciences, additional carcinogens in heated foods include: Hydroperoxide, alkoxy, endoperoxides and epoxides from heated meat, eggs, fish and pasteurized milk; Ally aldehyde (acrolein), butyric acid, nitropyrene, nitrobenzene and nitrosamines from heated fats and oils; Methyglyoxal and chlorogenic atractyosides in coffee; Indole, skatole, nitropyrene, ptomatropine, ptomaines, leukomaines, ammonia, hydrogen sulfide, cadaverine, muscarine, putecine, nervine, and mercaptins in cheese.
It is no coincidence since 1950 as processed food proliferated that cancer rates in the United States have steadily increased and are now at the highest point in history. The effect from consuming overly cooked food is minimal nutrition. The body is forced to raid its dwindling supply of nutrient reserves and remains hungry for quality nutrients after a typical meal on the SAD diet (Standard American Diet). This leads to further hunger even though the stomach is full. The result is chronic overeating and rampant obesity seen nationwide.
Scientific Research: Denaturation: What Cooking Does to Protein
Cooking denatures protein. According to Encyclopedia Britannica, denaturation is a modification of the molecular structure of protein by heat or by an acid, an alkali, or ultraviolet radiation that destroys or diminishes its original properties and biological activity.
Denaturation alters protein and makes it unusable or less usable. According to Britannica, protein molecules are readily altered by heat: Unlike simple organic molecules, the physical and chemical properties of protein are markedly altered when the substance is boiled in water. Further: All of the agents able to cause denaturation are able to break the secondary bonds that hold the chains in place. Once these weak bonds are broken, the molecule falls into a disorganized tangle devoid of biological function.
According to Britannica the most significant effect of protein denaturation is the loss of the its biological function. For example, enzymes lose their catalytic powers and hemoglobin loses its capacity to carry oxygen. The changes that accompany denaturation have been shown to result from destruction of the specific pattern in which the amino acid chains are folded in the native protein.
This is why the term dead food, referring to cooked food, is often stated. A result of denaturation is lowered solubility. In the case of egg white, a gel or coagulum is formed when heat is applied, thereby forming enzyme resistant linkages that inhibit the separation of constituent amino acids.
Proteins Coagulate
You can see coagulation of protein take place on a macroscopic level when you fry an egg. The clear protein gel surrounding the yolk whitens, thickens, and coagulates into a glue-like consistency. Digestive enzymes (peptones and proteases) cannot readily break down coagulated protein molecules once they fuse together. Not only are heated proteins unavailable to your body, worse yet: the indigestible, coagulated protein molecules tend to putrefy as bacteria in the body feed upon this dead organic matter. Bacterial enzymatic by-products are carcinogenic. Coagulation occurs on a microscopic level in all cooked protein molecules whether witnessed or not.

In Britannica is the acknowledgment that cooking destroys protein to make it practically useless. Utilize raw fruits, vegetables, nuts and seeds as your source of protein (amino acids). By eating The Fresh Produce Diet, you are assured of maximum biological value of protein and other consumed nutrients. (For further detail, see: The Truth About Protein and The China Project: Avoid Animal Protein).
As you consume more fresh produce as a staple, the body progressively requires less food. As you eat more nutrient rich raw food, the body steadily becomes healthier, and its metabolic efficiency increases. So does its ability to absorb and assimilate more nutriment. Only about one-half the amount of protein if eaten raw from protein plant food is necessary (via nuts and seeds) rather than from cooked animal protein.
The Difference Between Heat from Cooking and Digestive Chemistry
Physiologists claim that cooking and human digestion are virtually the same: that cooking is a form of predigestion where heat is used to hydrolyze nutrients that would otherwise be hydrolyzed at body temperature through digestion.
There are two ways to denature the proteins: chemically using digestive enzymes, or through the use of heat. Via heat, the body does not have the recombinant ability to utilize damaged denatured protein components (amino acids) and rebuild them once again into viable protein molecules.
This due to the enormous heat exposure during cooking, that denatures the protein molecule past a point of being bioactive, whereas body heat is too low to effect the protein molecule so adversely. The body does not require heat to reduce proteins to amino acids. It does a fine job of this chemically through enzymes. Chemically digested protein can be reused, whereas most of the heat denatured protein molecules cannot.
Raw Plant Protein Is Best
The Fresh Produce Diet includes protein predominantly in raw form. Fruits, vegetables, nuts, seeds and sprouts do not require cooking to increase their palatability or digestibility. When proteins are subjected to high heat during cooking, enzyme resistant linkages are formed between the amino acid chains. The body cannot separate these amino acids. What the body cannot use, it must eliminate. Cooked proteins become a source of toxicity: dead organic waste material acted upon and elaborated by bacterial flora.
When wholesome protein foods are eaten raw, the body makes maximum use of all amino acids without the accompanying toxins of cooked food. Some high-protein plant foods such as soybeans and lima beans contain naturally occurring toxins thought to be neutralized by heat. It is best not to eat these at all, since cooking does not totally remove the toxic effect of these foods.
Further Scientific Research on Detrimental Effects of Thermal Energy on Nutrients
(Warning: this next section is rather tedious)

According to the textbook Nutritional Value of Food Processing, 3rd Edition, (by Karmas, Harris, published by Van Nostrand Reinhold) which is written for food chemists in the industrial processed food industry, changes that occur during processing either result in nutrient loss or destruction. Heat processing has a detrimental effect on nutri-ents since thermal degradation of nutrients can and does occur. Reduction in nutrient content depends on the severity of the thermal processing.
    Effect of Temperature on Rate of Destruction of Various Food Components
    Component minutes at 250 degrees F Ea(kcal/mol)
Vitamins 100 to 1000 20-30 Quality factors 5 to 500 10-30 (texture, color, flavor) Enzyme inactivation 1 to 10 10-100 Vegetative cell inactivation 0.001 to 0.01 80-200 Spore inactivation 0.1 to 5 50-200 At 121 degrees C (249.8 F) the nutritional components decreased by 90%
At relatively low thermal processing temperatures, the destruction of enzymes is greater than that for microorganisms. The temperature range where the destruction rate of enzymes equals that for microorganisms is generally 270-290 degrees F. The fact that application of thermal energy to foods reduces the nutritive value of some components cannot be contested.
Degradation of Protein, Amino Acids and Carbohydrates: The Maillard Reaction
Various heat-utilizing techniques are employed in the commercial processing of food. Destruction of one or more nutrients often occurs during baking. This adverse effect on nutrients is more intense in the crust portions since the interior (crumb) of most baked foods rarely approaches oven temperature. While the heat of baking denatures protein, the quality of protein is adversely affected by nonenzymatic (chemical type) browning: the Maillard reaction.
It is ironic that the desired dark crust on bread is a result of the Maillard browning reaction that is known to reduce the nutritional value of bread. Maillard reaction products appear to have no nutritional value for the mammalian system. In fact, they may be of toxicological concern, as studies have also shown them to raise cholesterol. The Maillard reaction primarily affects the basic amino acids of which lysine is particularly significant. Maillard reactions are complex and are responsible for the odors and flavors of freshly baked products.
Specific Limiting Amino Acids
The first nutritionally limiting amino acid for humans in cereal grains is lysine. Methionine is the first limiting amino acid in legumes and has received particular attention in fortification of soy-based foods. Methionine presents potentially serious odor and flavor problems in fortification projects. It may not be used in infant foods or foods containing added nitrates or nitrites.
Lysine, the most limiting amino acid in grain products, is not the only amino acid destroyed during the Maillard reaction; almost all amino acids are adversely affected. In breads made with flour, significant losses of all essen-tial amino acids except tryptophan occurs. The loss of essential amino acids such as lysine and methionine during extrusion processes is of interest because of potential impact on protein quality.
A study of Maillard reactions on the loss of reactive lysine during extrusion was conducted by using soy protein enriched wheat flour. Lysine loss increased rapidly with increasing temperatures. Free amino acid loss has also been reported in the extrusion of dried potato flakes.
At 1600 degrees C, all amino acids measured were reduced extensively, with the average destruction rate being 89%. At extrusion temperatures less than 1300 degrees C, isoleucine, leucine, phenylalanine, tyrosine, and serine were lost to a surprisingly high degree. Clearly, the elevated temperatures lead to a substantial loss of availability of amino acids during the ex-trusion process. Lysine became less available nutritionally with conventional baking than with either microwave baking or steaming.

The physiological effect of a diminished lysine value after toasting of bread has been studied in weight gain in rats, and protein efficiency ratio (PER) of breads toasted to varying degrees of brownness. The toasted breads fed to the rats had a significant effect on growing rats. Weight gain was especially low with diets consisting of dark-toasted bread.
In toasting bread, the greater surface area exposed to toasting heat allows a greater proportion of the product to become browned and lysine destruction is greater. For example, thickly sliced bread would be less susceptible to nutritional loss than thinly sliced bread since less surface area is exposed.
Vitamins
In addition to amino acids, the effect of baking on vitamins has also been widely investigated. Vitamins are heat-labile, with thiamin and vitamin C being the most susceptible to baking losses. When the pH of the baked product rises above 6, nearly all of the thiamin is destroyed. Such conditions exist in a variety of chemically leavened baked goods including cookies and crackers. In high-protein cookies, calculations revealed thiamin losses exceeding 90%.
In addition to baking, vitamin B6 and pantothenic losses could be as high as 91% in canned food. The recommended -daily allowance (RDA) for these two nutrients probably can not be obtained from a menu of refined, processed, and canned foods. When we treat foods with heat, we lose up to 97% of the water-soluble vitamins (Vitamins B and C) and up to 40% of the lipid soluble vitamins (Vitamins A, D, E and K).
Minerals
Heat treat-ment also profoundly affects the absorption / utilization of certain minerals primarily through cleavage of complexes that renders these minerals less absorbable. Phytate, fiber, proteins, and certain minerals are particularly suspect as components of these complexes.
[Vitamins and minerals need to be consumed in an organic colloidal and naturally chelated molecular form to be absorbed, assimilated and utilized by cells and tissues during metabolic processes. Heat deranges the molecular arrangement of vitamins and minerals, thereby liberating its carbon. They are returned to an inorganic, ash-like form as found in soil. Inorganic nutrients are treated as toxins by your body. (For detail, see: No Need for Supplements).]
Fats and Carbohydrates
The Maillard reaction adversely affects the available carbohydrate and fatty acid content of baked products. At extreme baking conditions, linoleic acid and possibly other fatty acids are converted to unstable hydroperoxides, which affects both the lipid and vitamin nutritive quality of the product.
Fats Are Rendered Carcinogenic:
Heating also changes the lipids. These changed fats are incorporated into the cell wall and interfere with the respiration of the cell, causing an increase in cancer and heart disease. Acrolein, nitrosamines, hydrocarbons and benzopyrene are generated when fats are heated. Each are carcinogenic, cancer causing substances.
Deep-fried foods are the worse such as fried chicken, french fries, onion rings, potato chips, corn chips, cooked beef, chicken and just about all cooked meats due to their high fat content. Cancer is the number one killer of children in the United States and this is one significant reason why.
Oils tend toward rancidity especially when heated. Consume these in very small amounts, if at all. Paul Addis, professor of food science and nutrition at the University of Minnesota, says ”Rancid oils are one of the factors that are important in heart disease. Oils turn rancid when the fats are broken down in cooking, and, unarguable, these fats are toxic.”
High heat applied to oils during frying turns them into hydrocarbons that can cause cancer. Typical frying temperature is about 400 degrees F and can reach up to 600-700 degrees F. When fats / oils are heated to such temperatures the CIS fatty acids are converted to TRANS fatty acids. The unsaturated fats then begin to behave like saturated fats.
When heated, they raise rather than lower serum cholesterol levels (about 50% of the cholesterol increasing effect of saturated fat) and can raise LDL cholesterol by nearly as much as saturated fat. Besides the extra fat consumed, this is another reason why fried foods contribute to hardening of the arteries.
When oil is reheated to frying temperatures (as in deep fryers), the fat is more likely to develop the cancer producing agents acrolein and benzopyrene. Very hot temperatures also destroy vitamins and alter major proteins. Temperatures up to 1000 degrees F especially when one re-uses cooking oil (as in fast-food restaurants), breaks down the polyunsaturated molecule and free radicals then form. These are fragments that have combined with oxygen to produce poisonous peroxides. They are toxic due to their strong oxidizing (rusting) capacity, as they damage and destroy cells.

Carbohydrates Carmelize
Bake some yams or sweet potatoes. Notice the sweet sticky goo oozing from the skin that partially turns to ash from the excessive heat. You’re witnessing sugar molecules (carbohydrates) carmelizing, fusing together like sticky molasses. Similar to protein coagulation, carmelization also occurs on a microscopic level when all foods are sufficiently heated, whether or not it is witnessed.
When complex carbohydrate sugar molecules are carmelized or fused together, amylases (digestive enzymes) cannot cleave them into constituent simple sugars for use as an energy source. Not only are they unavailable, but the heat turns them into an ash-like toxin.
Amino Acids Deaminize
Protein molecules under ideal eating and digestive conditions are broken down into amino acids by gastric enzymes. Every protein molecule in your body is synthesized from these amino acids. Protein you consume IS NOT used as protein: it is first recycled or broken down into its constituent amino acids AND THEN used to build protein molecules the body needs.
There are 23 different amino acids. They link together in different combinations in extremely long chains to create protein molecules, like individual rail cars form a train. The amino group gives each amino acid its specific identifying characteristic that differentiates it from the others. Excessive heat sloughs off or decapitates the amino group. Without this amino group, the amino acid is rendered useless and is toxic.
Heating Food Past 117 Degrees Deranges Enzyme Molecules
When food is heated past 117 degrees, enzymes are destroyed. This is not a very high temperature. Consider the instructions on frozen food items that are sitting in your kitchen freezer at home. Pre-heat oven to 350-400 degrees. When cooking, the higher the temperature the worse the damage to your food.
Enzymes are specialized protein molecules that perform numerous catalytic physiological functions including breaking down food during digestion. Expose food enzymes to heat and nearly all are inactivated. The body then must utilize energy to generate more of its own digestive enzymes. Heat of less than 117 degrees does not denature the food enzymes, however. Using food dehydrators that blow hot air on food until it cooks at low, safe temperatures allows for delicious, creative recipes such as using uncooked dehydrated garbanzo beans to make raw falafel, and dehydrated live crackers of various flavors.
Live Enzymes?
Most physiologists cringe at the raw food enzyme theory. They claim that digestion depends on enzymes that the body generates, and not food enzymes. Enzymes in unripened fruit however, slowly break down its nutrients. As the fruit ripens, starches are reduced to sugars, fats are reduced to fatty acids, and proteins are reduced to amino acids.
But it’s not the food enzymes doing the work, says registered dietitian Roxanne Moore, spokeswoman for the American Dietetic Association. Fiber and antioxidants of which fruits and vegetables are prime sources, make the difference. Overall, the less cooked the fruit or vegetable, the more nutrients and fiber it retains. Moore says. If you don’t want to eat raw vegetables, how you cook them determines how much of the nutrients survive, she says. A few tips: use shorter cooking times, steam and microwave instead of boiling. Rely on fresh produce, which has more nutrients than processed or canned varieties.
Theory aside, eating raw food is a smart step toward good health. Consuming more fruits and vegetables gives your body a noticeable energy boost without harmful stimulants. (See: Stimulants and Supplements: Literally A Waste of Energy---Understanding Compensatory vs. Non-Compensatory Stimulation).
When Cooking Is Better?
Some nutritionists and biochemists erroneously claim that raw isn’’t always best. Sometimes cooked food gives more nutrients for the buck, say Rutgers University and Taiwanese researchers at the 1999 annual American Chemical Society meeting in San Francisco. They found that the body more easily absorbs iron from 37 of 48 vegetables tested when boiled, stir-fried, steamed, or grilled. Absorbable iron in cabbage jumped from 6.7% to 27% with cooking. Iron in broccoli flowerets rose from 6% to 30%. What the researchers were apparently unaware of, is the potential harm of high inorganic iron absorption.
NOTE: There are numerous instances when cooking releases a nutrient here or there - like lycopene in tomatoes, or when cooking breaks down toxins in something you couldn’t eat raw. However, what they forget to say it that if you eat primarily raw foods, you wan’t have a prostate problem so won’t bee needing any extra lycopene...and you won’t be needing to eat anything that would otherwise be toxic anyway. - Robert, ed.
The Danger of Increased Inorganic Iron Absorption
The reason for iron becoming more absorbable with cooking is that heat breaks down cell structure more completely than chewing alone. The ferrous iron (plant form) is changed to a more elemental inorganic form that is more easily absorbable in the intestine. But the more elemental iron begins to overload the system since it is relatively difficult for the body to eliminate.
The iron in cooked food is altered by heat. Iron absorbed from cooked food is detrimental compared to raw. There are several forms of iron, and the body alters them to suit its needs. Elemental iron is inorganic. After cooking, the structures and bonds have been radically altered. Excess inorganic iron can be a problem. It is associated with: increased infection, the generation of heart disease, predisposition to formation of free radicals, and free radical damage has extensive implications including the promotion of atherosclerosis, premature aging and cancer.
If you chew raw carrots well, you get as much iron as if you ate cooked mushy carrots. Thoroughness in mastication is just one factor governing the ultimate utilization of any nutrient. The health of the entire gastrointestinal tract has to be considered, as does the vitality of the individual (see: Nerve Energy), their blood purity, and the presence of all symbiotic factors involved in the absorption and utilization of iron.

Keep in mind the reasoning and trust, that Nature has provided the perfect balance of available nutrients in fresh plant foods which we are designed for (see: Biological Adaptations: Diet is Species Specific). By the application of heat we upset that balance.
Food, Nutrients, Digestive Activity, and the Effects of Cooking Food supplies the following nutrients:
NUTRIENT DIGESTION DIGESTIVE USED BY OVERLY COOKING CREATES ENZYMES BODY FOR CAUSES
  • protein amino acids hydrochloric acid body structure deaminization pepsin, pepteoses enzymes, blood coagulation ACID environment steroids numerous toxins
  • carbohydrates simple sugars salivary amylase energy carmelization (complex) pancreatic amylase dextrinization ALKALINE environment
  • fats fatty acids bile cell structure numerous carcinogens: hormones, energy acrolein, nitrosamines
  • vitamins (no change) - - - - - - metabolism returns to an (organic) inorganic state
  • minerals (no change) - - - - --- metabolism returns to an (organic) inorganic state
  • phytochemicals (no change) - - - - - - wards of reduced to an (natural cancer fighting chemicals) free radicals ash-like state
  • fiber (no change) - - - - --- keep colon healthy loses fibrous nature regular elimination becomes saturated
  • water H2O - - - - - - plasma / blood - - - - - - - - - - (body removes inorganic minerals) medium for all metabolic reactions
Practical Considerations: Living in Society
Cooking DOES NOT increase digestibility of foods. The more a food needs cooking, the further it compromises health: a prime indicator it is NOT one that you are biologically adapted to. This means you should not be consuming it as a major component of your diet. Our society however, is centered round a cooked food lifestyle. You can still enjoy cooked foods and be healthy to some degree. If you eat cooked foods, practice proper food combining.
Food combining allows your digestion to operate smoothly, without food fermenting or putrefying in your digestive tract. Aim for a minimum of 85% raw food of mostly fresh produce. Use transitional cooked food recipes. Enjoy your food, including your cooked food. But don’t kid yourself. You will NOT achieve optimal wellness unless you consume a Clean--Burning Fresh Produce Diet;.
Cooked vs. Raw Food and Pottenger’s Cats
Dr. Francis M. Pottenger Jr. MD wrote about his experiments with 900 cats over a period of ten years. Pottenger fed raw meat to a portion of his test cats, and fed cooked meat to the other test cats. Pottenger wrote, Cooked meat fed cats were irritable. The females were dangerous to handle, occasionally biting the keeper.
Cooked meat and a pasteurized milk diet led to progressive degeneration of the animals. He compared healthy cats on raw foods with those on heated diets with mention of parallel findings among humans in Dr. Weston A. Price’s worldwide studies. Behavioral characteristics, arthritis, sterility, skeletal deformities and allergies are some of the problems that were associated with the consumption of all-cooked foods.
The cooked meat fed cats suffered with pneumonia, empyema, diarrhea, osteomyelitis, cardiac lesions, hyperopia and myopia (eye diseases), thyroid diseases, nephritis, orchitis, oophoritis (ovarian inflammation) and many other degenerative diseases. No cooked food is benign. Cooked foods act malignantly by exhausting energy, inhibiting healing, and decreasing alertness, efficiency and productivity.
Pinpointing the Pathogenic Nature of Cooked Foods: Leukocytosis
An increase in white corpuscles in the bloodstream is indicative of pathology. White corpuscles are the body’s first line of defense against toxic or harmful substances. The typical white corpuscle count is about 6,000 per cubic millimeter. When this count doubles, triples or increases four or five fold it is evidence of a diseased condition even if outward appearance does not reflect it.
Dr. Kouchakoff of Switzerland conducted over 300 detailed experiments, which pinpointed the pathogenic nature of cooked and processed foods. Food heated to temperatures of just 120 to 190 degrees F (a range usually relegated to warming rather than cooking which, nevertheless destroys all enzymes), causes leukocytosis. Leukocytosis is a term applied to an abnormally high white corpuscle count.
On Raw Food, Leukocytosis Does Not Occur
Within a short time after eating food cooked at these low temperatures, white corpuscle counts tripled in the participants of Dr. Kouchakoff experiments. When raw foods were added to the meal, foods cooked in this low temperature range did not cause leukocytosis. At cooked temperatures higher than 190 degrees, no amount of raw food offset the pathological effects of heating, and leukocytosis always occurred.
There is no proliferation of white corpuscles when uncooked, raw fresh produce food is eaten. On the contrary, the constant daily fight against the toxic effects of cooked food eventually exhausts the immune system, causing age-related illness and premature death.
NOTE: This research was done in the 1930’s, as I recall, and has never been confirmed. Nobody it seems has done the same experiment to disprove it either - in almost 80 years. Hmmm? Meanwhile, cooked food proponents will always remind you that this research hasn’t been verified, and was also poorly designed. Nonetheless, it is indicative of something, and they still teach in medical schools that digestive leukocytosis is normal after eating. Is it? - Robert, ed.
White Blood Cells and the Immune System
A spontaneous multiplication of white corpuscles takes place in normal blood immediately after the introduction of any virulent infection or poison since white corpuscles are the fighting organisms of the blood. The human body contains hundreds of defensive mechanisms including leukocytes, lymphocytes, plasma cells, monocytes, basophils, neutrophils, eosinophils, and granulocytes to clear the circulation of toxic materials. These serve to protect and continuously purify the body against the ravages of poisons.
White blood cells patrol your circulatory system and defend against alien potentially harmful substances that have been absorbed or injected into the body. White cells are sanitation engineers maintaining the purity of tissues, lymph, and body fluids. If poisons, bacteria, fungi (yeast), metabolic wastes, cooked food debris, or other foreign substances enter the blood, they are engulfed by white blood cells. White cells tolerate nothing abnormal in the circulatory system. Some of what is apprehended is recycled as food, especially organic materials. High concentrations however, overwhelm your immune system.
When pharmaceutical or recreational drugs, medicinal herbs, nutritional supplements, inorganic nutrients and cooked foods are consumed, leukocytosis occurs. An abnormal proliferation of leukocytes are released into your bloodstream from lymph glands and bone marrow where they are normally held in reserve until needed, to apprehend harmful alien substances before they disrupt and chemically unite with a significant number of cells and tissues.
In the process, white cells go on a suicide mission sacrificing themselves while protecting the greater good of the organism. In the aftermath of eating cooked food or taking drugs, the white cell count rises to between 12,000-20,000 per cubic millimeter of blood. After clearing the bloodstream of toxic debris your white cell count decreases back to normal, about 4,300-7,000 per cubic millimeter of blood.
Healthfully Normal White Blood Cell Counts vs. Ordinary WBC Counts in the Typically Toxic
Although ordinary, this pathological average WBC count of 4,300-7,000 is exceedingly high and is based on the general populace who routinely consume junk food, cooked foods, condiments, soft drinks, teas, coffee, tobacco, and fermented foods: all of which cause abnormal proliferation of white cells. This phenomenon repeated each meal, each day, each week, each year for decades slowly lowers resistance to disease and hideously drains your immune defensive response.
On the contrary, those who consume a clean-burning diet of predominantly raw fruits, vegetables, nuts and seeds have white cell counts well below 4,300: and are mistakenly regarded as immunodeficient! The truth is: those who are REALLY suffering immunodeficiency diseases (as in AIDS) have destroyed their capacity to generate white blood cells, from constantly ingesting drugs or massive transfusions.
The healthy body is parsimonious, harvesting its resources strictly according to need. Your system is very economical in that it does not maintain faculties beyond what it requires. Healthy individuals whose blood streams are pure have lower white cell counts in circulation. The remainder is held in reserve within bone marrow, capillaries, and lymph nodes for times of emergency.
Raw fresh produce foods strengthen your immune system, alleviating the need to deplete its reserves. Overtime however, an enervating typical lifestyle routine gradually drains the body’s tremendous capacity to throw-off toxins. The average American is self- poisoned 20-40 times DAILY. Each bout lowers body vitality as chronic disease slowly develops.
Raw foods are easily digested, requiring only 24-36 hours for transit time through the digestive tract, compared to 40-100 hours for cooked foods. Eating overly heated nutrients increases the threat of putrefaction and disease. As you consume cooked carbohydrates, proteins and fats, you are eating numerous carcinogenic products generated by heat.
Bacteria Decompose Dead Organic Matter (Cooked Food) In the Body
Overly cooked foods literally wreck our body. They deny needed nutrients to the system since heat alters foodstuffs such that they are partially or wholly damaged. Nutrients are coagulated, deaminized, caramelized and rendered inorganic and become pathogenic. Virulent bacteria find soil in dead food substances whereas they cannot exist on living cells.
Cooked food spoils rapidly, both inside and outside our body, whereas living foods are slow to lose their vital qualities and do not as readily become soil for bacterial decay. Bacteria decompose the trash in our digestive system just as they do in soil. Bacterial action renders usable some waste materials that would ordinarily be expelled. Bacteria are essential to live and without them our existence would not be possible.
Yogurt Requires Dead, Cooked Pasteurized Milk
After eating cooked food, bacterial populations multiply exponentially. Consider what happens to milk while yogurt is made. If you start with raw milk and add a culture of bacillus bulgaricus the culture dies before it sours the milk.
But if first pasteurized or boiled, the milk is no longer fresh and is rendered lifeless. In making yogurt, it is then cooled to 100 to 110 degrees F and the bacterial culture is added. Bacteria then spoils (ferments) the milk by feeding on dead organic molecules, thereby producing yogurt in 6 to 8 hours. Note that the bacterial culture could not act on raw fresh milk whereas in a dead state, the milk readily became decomposing soil for bacterial proliferation.
Cooked food is dead organic matter that bacteria feast on. As a result, typical meals of protein, starches and sugars quickly ferment and putrefy. The metabolic by-products of bacterial activity include acid excreta, vinegars, alcohols, indole, skatole, nitropyrene, ptomatropine, ptomaines, leukomaines, hydrogen sulfide, cadaverine, muscarine, putecine, nervine, mercaptins and ammonias.
Our stomach becomes a cesspool of fermenting starches, sugars and putrefying proteins especially when eaten in incompatible food combina-tions as is typical in society. Indigestion occurs, and bacteria feed upon most of the food rather than your body. Digestive juices are no longer secreted when the digestive tract is vitiated. Under this condition, the digestive canal seeks to divest instead of digest.
Healthful Changes that Occur When Adopting a Raw Food Diet
Three important changes immediately occur when you adopt a raw food diet. First is the improved quality of nutrients taken into your system. Raw fresh produce is nutrient dense, largely pre-digested nutriment that is easily absorbed into your blood. Heated nutrients are denatured and of inferior quality, which are among the reasons why people commonly overeat cooked food. While their stomach feels full, their physiology craves nutrients and remains nutritionally starved.
The second important change that occurs on raw food cuisine involves what you STOP eating. No longer introduced into your system are devitalized, refined, heat-damaged toxic nutrient remnants. Energy is no longer wasted that previously was devoted to flushing these nutrient antagonists away from cells and tissues or quarantining them into fat cells, cysts, warts or tumors and abnormal growths. Instead, this energy is now redirected to enhance internal cleansing and further maximize the unfoldment of wellness.
The third major change on a fresh produce diet is the cessation of overeating. Overeating saturates the body with degenerated unnatural foodstuffs that constipate or clog the bloodstream’s nutrient delivery and sewage cleansing system. The blood delivers nutrients and oxygen to living cells, and carries away their toxic metabolites generated during ordinary cellular metabolism. This is why obesity is a serious condition. With too much food, the body is overburdened with inferior nutritionless empty calories.
High fiber, high water content fresh produce abolishes constipation of the bowels, cells and circulatory system. Obstructions are cleared and blood flow increases to each and every cell in the body. Enhanced blood flow is significant for two reasons: as mentioned above, blood delivers nutrients and oxygen to living cells, and carries away their toxic metabolites.
Raw Food and Athletes
Superb athletic performance on a raw food diet are not unheard of. Dr. Douglas Graham has been a 100% raw fooder for 17 years. He coaches professional athletes and consults with trainers from around the world. As a college gymnast he coached the springboard diving team. A national level competitor himself, Dr. Graham went on to train a trampoline team. After only three years under his tutelage, all seven members of the team won age group National Championships. Dr. Graham has trained professional athletes from many fields, including tennis legend Martina Navratilova and NBA pro basketball player Ronnie Grandison. He has advised Olympic athletes from four continents in a wide variety of sports.
Dr. Karl Elmer experimented with top athletes in Germany, producing improvement in their performance by changing to a purely raw food diet. Raw food provides you with more strength, energy and stamina. On raw food, the mind, memory and power of concentration is more focussed. Raw food leaves you energized rather than the typical tired feeling after meals. The tendency toward sleepiness after cooked meals is forsaken. Raw fooders require less sleep and achieve a more restful sleep.
Raw materials that the body needs to build wellness are not cooked materials. Nutrient values expressed as Percent of Recommended Dietary Allowance [RDA] per Calorie on nutrition charts are highest for raw foods. Potato, brown rice, winter wheat, pasta, and bread don’t even make it to the Recommended Dietary Allowance.
Just Eat
Don’t get bogged down with figuring out yet another diet or baffled over how to cook (or not cook) your veggies or fruits. What’s most important is that you actually eat them. The U.S. Department of Agriculture recommends 3 to 5 servings of vegetables, and 2 to 4 servings of fruit every day, which is satisfied each meal on The Fresh Produce Diet. This amount is a far cry from the 3.6 servings of fruits and vegetables combined, that Americans are now eating, which includes junk food such as french fries, potato chips, ice berg lettuce and ketchup on a burger.
On raw food: energy levels will increase, less money is spent at the grocery store (processed snacks are alarmingly expensive), sugar and fat cravings slowly subside since the sweet tooth is satisfied with sugar in fruit, and nutrient dense fat is obtained from raw nuts, seeds and avocado weight also normalizes: it’s almost impossible to overeat fresh produce plus its colorful, and delicious. No matter how you slice it, making room for raw does only good.
Raw food is also good for plants. When grasses are separately covered with fertilizers that are both raw and cooked, the grass grown with the raw fertilizer grows 400% more tonnage, over that grown with the same amount per acre of cooked food fertilizer.
The World’s Scriptures
According to Dr. Bernarr Zovluck, if you consult ancient scriptures and sacred writings, in Eden people did not eat cooked food with burning fire. Chinese, Egyptian, Indian and Hebrew accounts indicate that people were expelled from Paradise for using fire to cook food. Methuselah because he ate only raw foods, lived to an old age.
The Bhagavad Gita says, Pious men eat what the brilliant forces of nature leave over them after the offering. But those ungodly, cooking good food, sin as they eat. They’re speaking of illness caused by fire-cooked food.
In the Essene Gospel of Peace, a third century Aramaic Essene manuscript, Jesus is described as saying, Cook not your food with the fire of death, which is the fire that blazed outside you, that is hotter than your blood. Cook only with the fire of life, that is the natural heat of the day.

Professor Edmund Szekeley wrote concerning the Essene scrolls, Eat nothing, therefore, which a stronger fire than the fire of life has killed. Cook not, lest your bowels become as steaming bogs.
Review
  • Maximize your well-being and strengthen your immune system by consuming an abundance of unfired raw fresh produce at each meal.
  • Heat destroys nutrients, wholesale. Not only are heated nutrients unavailable to your body, the heated food debris becomes TOXIC which overwhelms your immune system.
  • Stop saturating your body with toxins and undermining your immune system. Avoid an abundance of cooked food and junk food.
  • If you cook, heat food conservatively. The lower the heat for the shortest duration, the better.
  • Use transitional recipes, proper food combining, and organic food sources to achieve at least an 85% raw food diet.
Do It for the Health of It!
Arthur M. Baker

------------------------------------------------------ कोई भी मूल्य एवं संस्कृति तब तक जीवित नहीं रह सकती जब तक वह आचरण में नहीं है.