Here’s part 2 of Arthur Baker’s article.
Enjoy, Roger Haeske
Raw Fresh Produce vs. Cooked Food – Part 2
by Arthur M. Baker, MA, MHE
Author of Awakening Our Self-Healing Body
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: ï‚· 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 denaturat-ion 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. ï‚· The changes that accom-pany 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.
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 acknowledgement 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.
World Copyrights reserved 2000 Arthur M. Baker MA, NHE Self-Health Care Systems