This information is critical to all professional bodybuilder, pro bodybuilding wannabes or just average Joes or Janes.
The question of whether large quantities of dietary protein are necessary to optimize protein synthesis and enhance muscular hypertrophy and strength has been debated for more than 100 years, a debate that’s fueled by extravagant claims and the many different proprietary brands of protein products available. To add fuel to the fire, when you hit the local gym, health club or health food store, you can’t get any straight answers. If you look beyond the hype and in some cases the scientific jargon, the mystery surrounding protein supplementation and how to choose the products that are the most effective may be easier to solve. You just need to be armed with a little more information.
Proteins are the basic building blocks of life, the body’s main structural components. The proteins in food are too large to be absorbed through your intestines, so they’re broken down during digestion into smaller components called amino acids. The smaller agents are able to penetrate the intestinal wall and are absorbed into the bloodstream after they’re reassembled and used to build and maintain the body’s structure. Amino acids not used for that purpose are used for energy. Presently, there are 22 known amino acids, with eight that are considered essential, meaning that the body can’t make them and so they must be supplied through the diet. The other 14, known as nonessential amino acids, are made in your body. The accompanying chart lists all the amino acids.
When you look into the mirror, you’re viewing protein in action. Your hair, eyes, skin, bones, heart, veins and muscles and the genes that carry your individual blueprint are made of protein. While other food factors are important, it’s protein that actually builds your muscles. Only protein gives your muscles the nitrogen necessary for growth, recovery and repair. Nothing gives you more nitrogen than protein, not carbs, anticatabolic substances-things that slow muscle protein breakdown-fats or even creatine and HMB.
Although there’s a clear distinction between essential and nonessential amino acids, the term nonessential is something of a misnomer because you need all of them for superior growth. In fact, when any proteins are constructed, all of the necessary amino acids must be present at the same time.
Current studies suggest that proper meal planning is important and that by consuming frequent meals-at least six per day-athletes can limit muscle protein breakdown. When studying nitrogen retention and amino acid absorption into the bloodstream, scientists have found that your body lives and breathes to maintain what’s called a free amino acid pool, which can be described as a small tank of amino acids that help repair and rebuild muscle tissue. When you don’t take in adequate amounts of protein, however, the amino acids in the tank begin to be used up. The body starts looking for some way to refill the tank, and it breaks down existing muscle tissue to sustain the right ratios.
The real problem is that the free amino acid pool must be totally replaced about six times a day. In fact, about 75 percent of the amino acids in the normal human adult are metabolized for the purpose of creating tissue proteins, enzymes and
protein hormones. The new proteins are needed because of the constant destruction of body proteins. Most of the amino acids that aren’t used to create proteins are converted to essential nonprotein nitrogenous tissue constituents. In fact, protein itself is composed of 15 percent nitrogen. Your body constantly gives off nitrogen through waste, as well as through hair, skin and nails. Without ample supplies and retention you’re at risk for nitrogen deficiency.
Protein Principle 1:
Since protein provides the nitrogen to ensure growth, it’s imperative that you maintain adequate supplies throughout the day.
Given the importance of getting enough protein, the burning question for the past 100 years has been, how much is enough? The current recommendation is 0.8 grams of protein per kilometer of bodyweight a day. For example, a 130-pound woman would need 47 grams of protein. To arrive at that amount, you convert the pounds into kilograms by using a conversion factor of 2.2, follows:
130 pounds ÷ 2.2 = 59 kilograms
59 x 0.8 grams = 47 grams
Many researchers contend that the above requirements are based on normal growth and repair and are insufficient for bodybuilding purposes. In recent years research has confirmed that people who perform heavy resistance training require more protein than the above recommendation to maintain nitrogen balance and stimulate muscle development. Current data suggest that 1.7 to 1.8 grams of protein per kilogram of bodyweight is a more realistic figure, as illustrated in the following example. The example involves a 220-pound man who engages in strength and resistance training and eats six meals per day. Plug in your own weight to determine your daily intake range.
Step 1. Change pounds to kilograms:
pounds ÷ 2.2 = 100 kilograms
Step 2. Multiply the weight in kilograms by 1.7 and 1.8:
100 x 1.7 = 170 grams of protein per day
100 x 1.8 = 180 grams of protein per day
Step 3. Calculate how much protein to consume throughout the day, in this case over six meals:
170 ÷ 6 = 28.3 grams of protein per meal
There are conflicting reports that protein intake at the above levels poses some risks. Health officials contend that excessive amounts of proteins and/or amino acids unaccompanied by proper electrolyte balance, meaning dissolved minerals in the bloodstream, saturate the body with harmful waste products, a situation caused by the incomplete conversion of protein to amino acids. As a result, the body creates uric acid, a poisonous by product, instead of new tissue. It may be wise to incorporate a liquid colloidal mineral formula into your regimen as well as drinking plenty of water.
If you don’t have the essential amino acids constantly entering your body, the rate of new protein formation will slow down. The amount of amino acids that actually enter the bloodstream is primarily determined by the digestibility of the protein source. That’s due to the fact that if digestive enzymes are unable to go to the protein, the undigested portions will pass through your system without being absorbed and used by the body. What’s more, with the natural daily fluctuations of amino acid levels in your bloodstream, the content of your meals can have a major impact on how well those powerful substances get to target sites, namely muscle cells.
Protein Principle 2:
There’s mounting evidence that confirms the need to include some carbohydrates at postworkout feedings, which helps to accelerate the rate at which amino acids are shuttled into the muscle cell. Current data indicates that 200 calories of carbohydrates will raise your insulin levels just enough to facilitate the transport of amino acids into muscle cells.
The last part of the puzzle has to do with your choice of a protein that has high biological activity, meaning that it will yield the greatest amount of nitrogen. Researchers have come up with a formula that determines the protein quality of foods, in which the active biological value, or BV according to what’s called the protein digestibility corrected amino acid score, or PDCAAS.
If a food’s amino acid availability completely matched your body’s requirement, its level of protein usability would be 100 percent. Biological value, then, refers to the percentage of a food’s protein usability. Proteins are also classified according to their source, such as an animal, plant or dairy source. The old method of determining protein quality and nitrogen-retaining capabilities, which was known as protein efficiency ratio, or PER, has been replaced with PDCAAS.
The PER method involved a carefully controlled animal feeding test, which calculated the amount of weight gained in grams for each gram of protein consumed. Casein, a milk protein, was used as a standard. PDCAAS, which is the method currently recognized by the Food and Drug Administration, is based on a food’s content of essential amino acids and the ratio of those aminos to each other. Scientists now have the technology to eliminate the uncertainty in determining a particular protein’s ability to deposit nitrogen into muscles. While the old method measured growth in relation to protein intake by rats, biological value involves the measurement of nitrogen from the dietary protein and the output of nitrogen in human feces and urine. Thus, this method focuses on how well nitrogen is retained after you eat a particular protein source.
Here are the current biological values of a number of proteins popularly eaten by bodybuilders:
- Whey protein isolate- 159
- Whey protein concentrate- 104
- Egg white – 88
- Chicken – 79
- Casein- 77
Protein Principle 3:
The biological value and the digestibility of a protein are critical factors in its relationship to absorption, nitrogen deposition, retention and any subsequent muscle growth.
The next time you buy protein products, use the following guidelines to make sure you don’t get a poorly formulated product, even though the source of protein is considered to have a high BV. Read the fine print, and keep an eye out for the following key words.
1) Acid hydrolysis.
These proteins are broken down but treated with acid-on-base solutions instead of enzymes. They often have sodium contents and so cause water retention.
2) Cross-filtered ion exchange (CFIF).
This protein produces superior results to that of protein processed through the ion-exchange method alone. CFJF removes 98 percent of denatured protein as opposed to 90.8 percent via ion exchange.
3) Cross-filtered ionized, or microflow, techniques.
In this process no heat is required to process the protein, which preserves glutamine, the most abundant amino acid in skeletal tissue. In fact, glutamine makes up about 61 percent of the amino acid in skeletal tissue.
This occurs when protein is exposed to high temperatures, typically above 60 degrees Celsius or to chemical agents that disrupt the bonds on which certain protein structures are based. When that occurs, the protein can no longer perform its biological function. Look for undenatured types of protein.
5) Enzymatic hydrolysis.
This creates predigested proteins, which involves breaking them down into smaller peptides, such as di-, tri- or oligo peptides. The peptides don’t attract water into the intestine, which causes diarrhea, as single amino acids often do.
6) Intact proteins.
These are in their original natural form and require complete digestion.
7) Isolated amino acids.
These individual amino acids require no digestion and contain no animal by-products.
These are smaller protein fragments, the same as predigested proteins.
9) Pure crystalline aminos.
These require no digestion.