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Critical Proteins PART I:

April 27, 2004 03:21 PM

It has long been suggested that proteins are different in their ability to promote growth. Most methods that measure protein quality are related to the efficacy with which food protein can satisfy amino acid requirements. However, as impressive as protein-evaluating systems appear to be (with numbers that suggest higher or lower protein scores), they could at times be quite misleading. As you may soon realize, most current conventional methods of protein evaluation, including the Biological Value (BV) system, often fail to truly estimate protein capacity to promote growth.

Why Protein BV May Be Misleading
The BV of proteins has been measured via nitrogen balance. A positive nitrogen balance generally indicates high BV and vice-versa. There are however some serious concerns regarding the accuracy of this evaluation system. BV tests are based on studies that measured protein utilization in a tightly controlled feeding environment, that doesn't resemble real life situations. Furthermore, these tests were conducted primarily on proteins in their raw state, overlooking the fact that most protein foods are habitually consumed in a processed or cooked form.

Processing and cooking significantly change the amino score and BV of raw protein foods. To make the matter even more confusing, protein BV studies were based on small servings (100 to 200mg per kilogram of body weight). In such a small servings, even inferior proteins are almost fully utilized with a relatively high BV score. Unfortunately, these high scores dramatically decline when protein is consumed in normal or large amounts, such as with athletes or bodybuilders, a fact that must be calculated when designing a nutritional program.
The most efficient conventional method to evaluate protein quality is the so-called PDCAAS (Protein Digestibility Corrected Amino Acid Score) developed by the Food and Agriculture Organization (FAO).

The PDCAAS system measures both amino acid content and digestibility. However, even this evaluation system fails to notice that protein quality and utilization can change according to additional variables such as the amount of calories, methods of cooking, level of pH, naturally occurring enzyme inhibitors, storage time, temperature and rate of degradation. Moreover, through millions of years of evolution, different populations have adapted to different foods. Assimilation of nutrients including protein, predominantly depends on genetic pre-disposition, individual needs and overall nutritional composition of meals. All these variables significantly affect protein BV and utilization.

Bodybuilders and athletes, though not an ethnic population, are in fact a unique group of people (a "freaky" population) that may be characterized by increased metabolic requirement for certain amino acids. For instance, the amino acids tryptophan, tyrosine, methionine-sAME or lysine-carnitine, serve as building blocks for stress hormones and energy compounds, these amino acids are often required in extra amounts due to high-energy demand and the need to perform under extreme mental and physical stress. In other words, bodybuilders and athletes often need to satisfy their protein intake requirement with extra essential as well as conditionally essential amino acids, and therefore can't rely on the BV system alone as a sole paradigm for practical applications.

The purpose of this article is to correct some common mistakes regarding protein evaluation and present alternative ways to enhance food protein quality for improved utilization and enhanced growth.

Protein Deficiencies' Effect on Growth
Proteins are made up of 22 amino acids, out of which nine are essential, and therefore must be obtained from an outside source. There are also conditionally essential amino acids, which play major roles in performance, recovery and reactions to stress. Dietary proteins are divided into two kinds of proteins: complete proteins, which include all essential aminos and incomplete proteins, which are deficient in one or more essential amino acids.

It has been established that consumption of incomplete protein would likely suppress growth. This assumption is based on the fact that protein synthesis for anabolic purposes requires all essential amino acids in the right proportions. A deficiency of even one essential amino may suppress critical metabolic functions, which are necessary for the repair and buildup of tissues including muscles. Moreover, it has been assumed that a deficiency of essential amino acids would limit protein synthesis (and growth) proportionally to the extent of deficiency. Indeed, protein-scoring systems which are based on the above assumptions, claim to evaluate protein scores according to the extent of protein deficiency and thereby assumably help improve dietary protein choices. However, the evaluation of protein quality according to their amino score raises some questions regarding the practical applications of this system.

The Skinny on Protein Scores
Current protein scoring systems are based on measuring the most deficient essential amino acid in the protein matrix (i.e., "the weakest link"). This most deficient essential amino, also known as the limiting amino acid, would finally determine the protein value. For instance, if a protein is deficient in the amino acid lysine (such as most grains), by about 50 percent compared to standard egg protein, its score would be 50.

However, this protein-scoring system has some serious limitations. It ignores the occurrence of conditionally essential amino deficiencies. It also overlooks the fact that the body can often correct amino deficiencies via a special adaptation mechanism by which the body recycles endogenous proteins (from damaged and old tissues) for anabolic purposes.

To understand fully what the best growth-promoting protein sources are, much more research and clinical studies may be needed. Nevertheless, based upon current data, and for the purpose of practical applications, it is important to understand the factors that influence protein capacity to be fully utilized for growth.
Factors That Effect Protein Utilization for Growth
It has been established that protein utilization is a key to growth. It is commonly believed that increased consumption of proteins would likely increase protein utilization. It has also been assumed that only animal proteins with a high BV can effectively promote muscle gain. Plant foods are generally regarded as inferior sources of proteins and as such are consumed as a shear source of vitamins, minerals and fiber, and not as a viable source of amino acids. However, as you may soon realize, all the above presumptions are only partly true and therefore may often lead to wrong conclusions.

Factors That Promote or Suppress Protein BV
The variables that influence protein BV and utilization may appear as contradictory and somewhat confusing. Nonetheless, to put some order to this madness, here is a list of protein BVs most enhancing vs. most suppressing factors. Note that real life protein BV would likely indicate how much of it could be utilized for actual growth.

Real-Life Protein BV is enhanced by:
  • Small servings of proteins
  • High calorie intake
  • Food combinations
  • Fasting and undereating
  • Raw (unprocessed) state of food
  • Free-form amino acid supplementation
  • Probiotics and enzymes
Protein BV is suppressed by:
  • Large servings of proteins
  • Low calorie intake
  • Mono diets (based on one source of food)
  • Food processing
  • Protein exposure to high heat
  • Stress
  • Indigestion
  • Excessive intake of dietary fiber
  • Vitamin and mineral deficiencies

Note: protein BV marks only the rate and efficacy upon which food proteins may be utilized.

Next issue: We will apply all this information in practical terms; we'll go deeper into the matter and review the most viable methods to maximize food protein BV and its capacity to be utilized and promote growth.

EFA - Can Heal or Kill!
What is the optimum daily intake of Essential Fatty Acids (EFAs)?
The issue of EFA intake remains controversial. EFAs are polyunsaturated long chain fat molecules which are building blocks for cellular membranes and prostaglandins that regulate numerous critical metabolic functions. It has been established that certain EFAs, in particular Omega 3 oils, are most beneficial in virtue of being anti-inflammatory, anti-cancerous, insulin sensitizers and brain neuroprotective. Some health experts recommend to increase EFA consumption, in particular Omega 3 oils. When it comes to EFAs, the idea that more is better is currently quite popular.

Fat guru Udo Erasmus recommends active individuals to increase consumption of essential oils and even use them as fuel for energy. According to Erasmus, EFAs are the most efficient fuel among all food compounds.

With all due respect, I'm quite concerned with the idea of high consumption of EFAs and for that matter, of any long chain fatty acid. Diets rich in polyunsaturated fats have been shown to deplete Vitamin E from the body. These long chain fat molecules possess highly reactive double bonds that have a high affinity to react with oxygen and thereby increase levels of free radicals. Reactive free radicals destroy tissues while increasing cross linkage of proteins. Cross linkage of proteins is an uncontrolled metabolic process that binds protein in a way that compromises their natural configuration and thus causes dysfunctional or damaged tissue. Cross linkage of proteins is associated with aging of tissues. The leathery appearance of old skin or the sagginess of old muscle tissues is partly due to an advanced cross linkage process.

Evidently, the body isn't well equipped to utilize polyunsaturated fats as fuel for energy. As politically incorrect as it may appear to be, the body is more efficient in converting saturated fats to energy (such as palmitic acid) than polyunsaturated fats. In order to be able to handle long chain EFA molecules, the body must utilize them in certain compounds known as peroxisomes. There, EFAs are broken down to hydrogen peroxide and water. However, this peroxisomal process does not yield energy. Therefore, EFAs should never be considered as a good source of energy! Quite the opposite, all long chain fats are primarily poor fuel.

Saying all that, it has been suggested that the body can be trained to gradually increase its capacity to utilize fat fuel. When that adaptation to fat fueling occurs (via special high fat dietary cycles), the body would likely improve its capacity to utilize long chain fats including EFAs via a process that involved activation of certain genes that regulate fat metabolism. The activation of fat regulating genes is controlled by certain gene activator compounds known as PPARs (peroxisome proliferator activated receptors). This super family of gene activators regulates the number of peroxisome bodies in the cell. Interestingly enough, some of these gene activators can effectively promote massive fat burning. We'll discuss this in another issue. For now, let's just say that EFA consumption should be optimized instead of maximized.

A 1-4 tablespoon/day of quality EFA (such as Udo oil) for a 160-200 pound person is sufficient. Note that certain polyunsaturated fatty acids derived from Omega 6 oils are shown to increase the risk of cancer, arteriosclerosis and premature aging. It's most important than to keep a ratio of 2 : 1 omega3 to omega6, respectively.

Just to be on the safe side, take extra Vitamin E. Vitamin E destroys free radicals that cause cross linkage and aging. It also protects EFAs from getting rancid. Recommended daily amount of Vitamin E is 800iu.

Keep your EFA in cold temperature. Smell it and taste it before using it. If it has a funky smell or taste, throw it away.

Finally, train your body to gradually increase its capacity to utilize fat fuel. Cycle between days of high fat (low carbs), based mostly on raw nuts and light protein during the evening meal followed by days of moderate to high carbs. That way, your body will gradually adapt to effectively turn fat fuel to energy while increasing its capacity to fully utilize EFAs for other critical metabolic functions with minimum risk of adverse reactions of free radicals.

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