by Mike Arnold
From the beginning, vegetarianism has been the red-headed step child of performance-based nutrition; oft maligned and generally portrayed as inferior to the meat heavy diets which characterize modern bodybuilding. It’s not so much the foods themselves that detractors have a problem with, but rather, the lack of animal products within the diet—the claim being that animal proteins are essential for meeting the nutritional requirements of those engaged in the various strength and physique sports.
It’s no secret that the main gripe against vegetarianism has always been centered around protein. More specifically, it is both the quality and quantity of protein within the diet that critics take issue with. At the time this belief originated it was not without merit, but one should understand that the issues surrounding the vegan lifestyle were unique to the era in which they arose, as we did not yet possess the technology required to overcome them. However, it didn’t take long for supplement companies to step up to the plate and render these issues obsolete.
No doubt, protein is the single most important macronutrient within the bodybuilding diet, thereby making the type of protein consumed a necessary consideration. When it comes to determining a protein’s quality, there are 3 primary factors we need to concern ourselves with. First and foremost is whether or not the protein is a complete or incomplete protein; complete proteins being those which contain the 9 essential amino acids (EAA’s) required for muscle growth and in complete proteins being those that don’t. While all animal proteins contain these 9 EAA’s, many plant-based proteins do not, making some of them incapable of promoting growth on their own.
The 2nd factor is a protein’s PDCAA score. The PDCAA (protein digestibility and corrected amino acid score) score is a method of determining protein quality based on the amino acid requirements of humans, as well as their ability to digest it. During the muscle building process, the body utilizes the 9 EAA’s in a specific ratio. The closer a protein’s amino acid ratio is to that of human muscle tissue, the higher its PDCAA score (biological value is an older term used to describe the same thing). A protein like whey is considered to be very high quality for this reason, as the amino acids within it are present in a ratio which allows the majority of them to be used muscle growth.
On the other hand, the amino acid ratio within pea protein is comparatively poor (as are many plant-based proteins), so the percentage of available amino acids which can be used for growth is lower. Basically, a higher PDCAA score means the body in able to use a larger percentage of the protein for muscle growth, so we don’t need to eat as much in order to experience maximum results. Keep in mind that a protein’s PDCAA score is not a reflection of the quality of the amino acids themselves (an amino acid is an amino acid), but only the ratio of aminos within that protein.
The 3rd and final determinant of protein quality is its leucine content. As stated above, there are 9 EAA’s involved in the muscle building process, one of which is leucine. However, leucine is unique in that it has a dual role, acting as both a building block and the sole activator of protein synthesis via mTOR signaling. The degree to which leucine activates protein synthesis is dose-dependent, with larger amounts of this amino increasing protein synthesis to a greater degree and smaller amounts having the opposite effect. Therefore, maximizing muscle growth not only requires enough building blocks, but it also requires adequate leucine, so that those building blocks can be put to good use.
When explaining the role of EAA’s and leucine in the muscle building process, I often like to use the following analogy. Imagine your muscles as a construction site, with EAA’s being your common laborers and leucine acting as foremen. As anyone in the construction business knows, erecting a building requires a certain number of common workers in order to complete the project, without which construction will stop prematurely. However, before construction can even begin, the workers must first receive the green light from their foremen, who provide instruction regarding their individual duties. Otherwise, they will just sit around doing nothing. It is also important that a sufficient number of foremen remain on the job. If not, efficiently directing the workers becomes an impossibility, causing construction to slow.
So it is with leucine and EAA’s. EAA’s are used to construct new muscle fiber, but it is leucine which signals the body to use those aminos for growth. If the body lacks either one of these, muscle growth will be hindered or discontinued altogether. This is why vegetable proteins have been shown to result in less protein synthesis per gram—because the lower leucine levels result in a weaker signal.
Knowing all this, is there anything we can do to correct these flaws? Absolutely, and it is not nearly as difficult as one might think. Although most vegetable-based proteins have a lower PDCAA score, this shortcoming is easily eliminated in one of four ways. The first is simply to eat larger quantities of protein, which helps make up for the less than optimal amino acid ratio. Another and more efficient way is to combine two complimentary protein sources (ex. rice & beans), thereby obtaining a better balance of aminos and improving the meal’s overall PDCAA score. This allows us to create an amino acid profile similar to what is found in animal proteins, such as beef, eggs, or milk. We can also add improve a protein’s amino acid profile by supplementing with the individual amino acids that the protein lacks.
Although all of these methods allow us to improve protein quality, they fail to solve the following problem, which is that vegetable proteins contain a lower percentage of protein by weight in comparison to animal proteins. Because of this, vegetarian bodybuilders need to eat a larger quantity of protein foods in order to meet their daily protein requirements. This was a big problem in generations past, as even meat-eating bodybuilders are already forced to eat a large volume of food in order to build and maintain maximum muscle mass. Having to eat even more food just makes things more difficult.
Fortunately, modern technology has largely eliminated this problem through supplementation, providing bodybuilders with a number of high quality vegetable protein isolates. This makes taking in adequate protein a breeze. One can also use an EAA supplement, which contains all 9 EAA’s in the proper ratio (ex. ALRI’s Humapro). Due to these advancements, there really isn’t any reason for a vegetarian bodybuilder to struggle with protein intake in this day and age.
Having addressed the issues of protein quality and quantity, we are now left with only one other obstacle to overcome—that of leucine deficiency. Most vegetable proteins contain relatively low amounts of leucine, making it impossible for them to activate protein synthesis to the same degree as animal proteins when consumed in equal quantities. But vegetarian bodybuilders need not worry, as free-form and even peptide-bonded leucine is now widely on the sports nutrition market, allowing us to close the gap between vegetable and animal proteins.
In fact, clinical studies have revealed that when leucine is added to vegetable protein in sufficient quantities, we can surpass the protein synthesis rates achieved with animal proteins. According to research, protein synthesis is maximized with a 4.5 gram dose of leucine, with greater amounts having no additional effect. This research clearly demonstrates that leucine is the primary regulator of protein synthesis, and that protein type has no bearing on protein synthesis rates in the face of identical leucine concentrations. With modern supplementation having taken away the main advantage of animal protein, the playing field has been leveled, placing vegetarian bodybuilders on equal footing with their meat-eating counterparts.
One seldom mentioned benefit of animal proteins is that many of them contain growth and immune system boosting factors that are not present in vegetable proteins. This is not surprising given that many animal proteins, such as milk and eggs, have been specifically created to provide all the sustenance an animal needs to grow to full maturity. To what degree these growth factors might affect muscle growth, it is impossible to determine with any accuracy, as science has not yet provided a way of measuring their muscle building value relative to the variables mentioned above. Still, it is not unreasonable to assume that they supply some benefit in terms of muscle hypertrophy.
However, many of the animal proteins available in stores have been severely damaged, rendering many of their natural growth factors inert. For example, raw milk is loaded with these substances, but the homogenization and pasteurization processes, which all regular store-bought milk is subjected too, destroys them, making it a mere shadow of the nutritional powerhouse it once was, but let’s not stop there. Most milk is also derived from corn-fed cows rather than grass-fed, which alters the milk’s nutritional profile so severely that it is changed from a health fortifying food to a potentially health damaging one. In short, regular store bought milk is junk while raw, grass-fed milk is a bodybuilder’s best friend.
Meat products aren’t any better. Let’s use cows as an example. Like with milk, most cows raised for slaughter are fed corn (and sometimes much worse), which changes the nutritional content of the meat in the same way as cow’s milk. On top of that, the cows are pumped full of drugs, including steroids, growth hormone, and antibiotics, all of which result in the presence of active, unwanted drug metabolites in the meat. Furthermore, the cows live an unhealthy life, being locked away from sunlight, and confined within such small spaces that they cannot even turn around, let alone get some exercise, all while living in their own shit and piss. Many of these cows become sick and diseased (hence the need for antibiotics) and these same animals are sold as food. I won’t even get into the manufacturing of the meat.
Chickens? The state of affairs is no better, and their eggs are just as nutritionally damaged as cow’s milk. How about fish? Certainly, that must be good for us, right? Not really. Most of the fish sold in supermarkets today is farm-raised, which means they are born and raised within man-made ponds, while their feeding is closely regulated. Let’s use salmon as an example. Normally, salmon live in the wild, eating their natural sources of food. This results in an animal brimming with nutrition and free of disease.
On the other hand, farm-raised salmon are fed pellets which contain chicken feces, corn meal, soy, canola oil, and other fish. The effects of this practice are so dire that farm-raised salmon literally becomes a different food from what is seen in the wild. Farm-raised salmon are 7X higher in PCB’s, have 30x as many sea lice, and are administered more antibiotics than any other kind of live stock (to prevent them from contracting life-threatening illnesses in their disease-ridden environment). If that doesn’t make you think twice about farm-raised fish, the following should.
Whenever we think of salmon, most of us think of a fish with brightly colored orange flesh. This is normal and what salmon is supposed to look like. Not so with farm-raised salmon. Their flesh is actually a grey, rotten-looking color. Salmon farmers have to purchase coloring agents and subsequently dye the fish’s flesh orange so consumers don’t vomit at the check-out line. Of course, in addition to all the harmful contaminants, its nutritional profile has been drastically altered, turning this animal protein from a health-bolstering food into a potentially health damaging one.
This is only the tip of the iceberg. If you think chicken, beef, dairy, and egg products are the only animal proteins subjected to these health-damaging practices, think again. Nearly all commercially raised and prepared animal proteins have been just as polluted and nutritionally raped as these. Once you become aware of the true state of the food industry, particularly the sector which oversees livestock, the consumption of regular, store-bought animal products becomes increasingly difficult to justify.
The good news is that there are much better options available, such as grass-fed beef, raw-grass-fed milk, free-range-grass-fed chicken, wild-caught fish (preferably from less polluted areas, such as those harvested from Alaskan waters), and all sorts of wild game like venison, pheasant, etc. These foods supply significant health and muscle building benefits. Unfortunately, most bodybuilders cannot afford to eat them with any regularity, especially in the quantities typically consumed by bodybuilders. Of course, if they are included they should be properly balanced with organic, non-GMO whole-grains, fruits, vegetables, nuts, seeds, and raw/virgin oils (examples of healthy oils include raw red palm fruit oil, raw avocado oil, extra virgin olive oil, raw coconut oil, macadamia nut oil, etc).
In addition to avoiding the health-threatening effects of tainted animal products, vegetarianism provides many other benefits, such as reduced systemic inflammation, improvements in metabolic health, enhanced immune system function, improved digestive health, and overall disease prevention. All of these benefits are either directly or indirectly connected to some aspect of the muscle building process, thereby assisting the individual with both his health and bodybuilding progress.
Regardless of which dietary lifestyle you choose to embrace, one thing you can be sure of is that vegetarianism, when properly understood and combined with modern supplementation, is not the muscle building death-blow we once thought it was. While there is still some merit to the arguments which support the inclusion of (healthy) animal proteins within the bodybuilding diet, supplementation is capable of providing many of the benefits that were previously only available to meat eaters, particularly those related to protein quality, the ability to meet protein requirements, and protein synthesis.