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How We Make A Better Protein Powder

Phil Connolly, CNP Professional

When we set out to formulate the world's best protein powders, we knew that we had to come up with some new twists if we were truly going to develop a protein powder that was better than everyone else's protein. There were already some pretty good proteins on the market. So how could we make better proteins? The answer seemed obvious, if you want to make the world's best protein powders, use the best raw material proteins available and make sure that the body uses them better.

Micellar Casein

We already had access to the finest casein component - natural structure, micellar casein. This is casein as you would find it in milk. This is casein in the structure that nature intended. This is casein that one can use for building a stronger, healthier body. Micellar casein is in just the right conformation that our bodies can efficiently digest the protein to yield metabolically bioactive peptides. These bioactive peptides, when detected, stimulate a whole cascade of anabolic hormonal production in the body. In addition, micellar casein will provide a sustained release of amino acids into the bloodstream over extended periods of time. The body cannot manufacture or repair muscle tissue unless amino acids are in ready supply in the blood (and it's a good idea to always have plenty available). In addition, the casein micelle structure contains bound calcium and phosphorous in large quantities that are efficiently absorbed into the blood to help build strong bones. In fact, the calcium and phosphorous, in the complex chelated form as they exist in the casein micelle, are excellent for strengthening bones compared to other forms of supplemental calcium and phosphorous. That is why dairy product marketers are allowed to claim that milk is good for your bones. Every dedicated athlete understands that as muscle mass is increased, it is necessary to increase skeletal density (bone strength) to support the extra muscle mass. A common mistake for weekend warriors is not to consume enough calcium and phosphorous for skeletal support. Consuming true micellar casein remedies that problem. All of the above mentioned properties contribute to the anabolic nature of micellar casein. Regular casein or caseinates have not been shown to produce the same high level of bioactivity or sustained time release and, therefore, are not considered as anabolic.

Whey Protein - The Debate of Undenatured vs Denatured

Now, we needed to find the right whey protein. We weren't, however, interested in just any old whey protein. We wanted to incorporate the healthiest, most anabolic whey protein available. Anytime you see a magazine article or an advertisement detailing the health / anabolic benefits of whey protein, the majority of the claims made in support of the health benefits of whey protein are derived from the definitive authority on which they all rely - a scientific paper that was published in 1991 in Clinical Investigative Medicine (Volume 14, pages 296-309), written by Gustavo Bounous and Phil Gold (You have probably seen this often quoted paper many times referred to as Bounous et. al.). This scientific paper is considered to be the bible for whey protein marketing. Gustavo Bounous is a Doctor of Medicine and he wanted to study the effects of whey protein on the human immune system. He enlisted the assistance of Phil Gold, a professor of Chemistry at a nearby University. Bounous had been studying whey proteins and their immunoenhancing (ability to support the immune system) properties. In the midst of his studies, he received a new shipment of whey protein (from the same supplier). In the 1991 paper, Bounous admits that "a recent observation has revealed to us that the described biological activity of whey protein concentrate ... is actually dependent on the undenatured conformation of the ingested proteins".. He then goes on to describe how the "discovery was made accidentally".. He had been using a certain commercial brand of whey protein in his studies. When he received a new shipment of the whey protein, he found that the new shipment of whey protein "failed to exhibit the immunoenhancing effect previously described while exhibiting the same nutritional efficiency".. Both Bounous and Gold theorized that the structural conformation of whey protein would determine its bioactivity. They designed a study to "define the effect of changes in molecular conformation of whey protein concentrate on the immune response and glutathione formation of the host".. Just so that we're all clear on the meaning of their study - when they talk about changes in molecular conformation of whey protein concentrate, they are talking about denaturation of whey protein concentrate. Webster's Dictionary defines denaturation as:

To modify the molecular structure of (as a protein or DNA) especially by heat, acid, alkali, or ultraviolet radiation so as to destroy or diminish some of the original properties and especially the specific biological activity.

In Chemistry, denaturing a protein is defined as changing its molecular conformation (structure) by heat, acid, alkali, or radiation. So, we can confidently say that when Bounous and Gold designed an experiment to study "the effects of changes in molecular conformation of whey protein concentrate on the immune response and glutathione formation", they were designing an experiment to study the effects of whey protein concentrate denaturation on the bioactivity of whey protein.

As part of the experimental design, they studied commercially available whey protein concentrates and isolates from Europe, New Zealand, Canada, and the USA. These whey proteins all had one thing in common - they were manufactured from cheese whey. Bounous and Gold then had a near perfect whey protein specially made for them in a laboratory in Quebec. They called this near perfect whey protein, Product X. It was their experimental design to compare the commercially available whey proteins, made from cheese whey, to a near perfect whey protein, Product X for bioactivity. As a control for the experiment, they also compared everything to casein (because casein is reputed to have little immune supporting bioactivity).

The results of their study showed that whey protein does indeed possess bioactive properties that are anabolic - but only Product X, their specially manufactured whey protein displayed significant bioactivity. They stated that "immune response ... is highest in mice fed Product X".. Results of the experiment also showed that Liver and Heart glutathione content was significantly higher in the Product X group than other groups. In fact, the casein group had the same heart glutathione content as did the cheese whey protein groups (not very good for cheese whey, huh?). The authors concluded:

"The current findings indicate that the previously described biological activity of dietary whey protein is restricted to the UNDENATURED form of the protein and it is not related to its nutritional efficiency."

Translation so that we can all understand it: The results of the experiment showed that the much desired biological activity of whey protein is limited to a totally undenatured whey protein - Product X. The cheese whey proteins did not exhibit the desired biological activity.

and

"Indeed specific thermolabile proteins, crucial to biological activity of the protein mixture, may be involved. In addition, partial unfolding of some molecules, UNDETECTED BY SOLUBILITY CHANGES, could initiate further unfolding and/or other biologically significant alterations during the process of digestion in the gastrointestinal tract." Thermolabile means those proteins that are easily denatured by heat.

Translation so that we can all understand it: Those proteins that are easily denatured by heat are the most crucial to whey protein's biological activity. In spite of the fact that a whey protein may seem water soluble (hence, the false claims of"undenatured"), some of the proteins will be partially unfolded (not enough to affect water solubility but enough to cause a change in molecular structure - denaturation). This will decrease biological activity significantly.

and

Our Product X whey protein concentrate was prepared in the most lineant (sic) way compatible with accepted standards of safety with regard to bacterial contamination." They then go on to discuss the commercially available cheese whey proteins. "Although the proteins contained in the concentrates from other sources examined were MOSTLY in undenatured form, as indicated by the relatively high solubility of the concentrates, the content of serum albmin and immunoglobulins in these mixtures is below the level apparently necessary to produce a biological activity. These very thermolabile proteins are denatured, hence, precipitated and partially lost from whey when high pasteurization temperatures are utilized. Conversely, the relatively high concentrations of the thermosensitive serum albumin and immunoglobulins resulting from low pasteurization of milk in Product X, may reflect more closely the pattern of raw milk.

Translation so that we can all understand it: Product X was prepared using legally acceptable, low temperature pasteurization (63^o C for 30 minutes) to kill harmful bacteria. Even though the cheese whey protein concentrates appeared to be MOSTLY in undenatured form (as measured by water solubility), they were missing important bioactive fractions of protein - serum albumin and immunoglobulins. What happened to them? How could they be denatured and yet the whey protein still seems water soluble? They were denatured by heat and acid - the heat of normal legally required pasteurization techniques (72^o C for at least 15 seconds). Not only were these valuable proteins denatured by the heat, but they were partially lost from the commercially available whey protein powders through precipitation during production. In contrast, Product X contained higher levels of the bioactive serum albumin and immunoglobulin fractions because of the lower pasteurization temperatures employed and it more closely matched the protein pattern of raw milk.

And their final conclusion:

"In conclusion, our data lend support to the concept that the concentration of serum albumin and possibly immunoglobulins, as well as the undenatured conformation of the molecules are crucial factors in determining the biological activity of dietary whey protein concentrate."

Translation so that we can all understand it: Our results show that if a whey protein has been denatured, even just a small part, it will not have good biological activity.

To summarize: Bounous and Gold proved that only a totally undenatured whey protein (better termed a "native" whey protein because it would be in its natural, raw milk-like state) would provide the bioactive properties of immune system support and glutathione production that people advertise today. They even proved that whey proteins made from cheese whey did not display the desirable effects because they are actually missing large amounts of the valuable, bioactive whey protein fractions - even though they have excellent solubility in water.

Amazingly, when the paper was published (and still to this day), every marketer of whey protein in sports nutrition began to advertise their whey protein as having the bioactive properties of Product X. They quoted the Bounous and Gold paper (and still do). They did this in spite of the fact that every one of them purchased whey protein that came from cheese manufacture. Most of them were probably using the very whey proteins that Bounous and Gold had concluded did not contain bioactivity. Now, let's get real! Either they didn't understand what they were reading (that's a scary thought when one considers that they are "scientifically" formulating protein powders) or they didn't care and intended to misrepresent a scientific paper, thereby pulling a fast one on the consumer. Today we have certain whey protein marketers claiming that their whey protein doesn't come from cheese whey (at least they get the message) - it comes from acid casein production. They claim that their process is "gentle". If cheese whey is bad, then acid casein whey is worse! In acid casein manufacture the pasteurization temperatures are the same as for cheese whey and the pH changes are greater. More of the valuable bioactive whey protein fractions are lost in acid casein whey than are lost in cheese whey.

Being a biochemist, when I read the Bounous and Gold paper, I recognized the causes of denaturation of the whey proteins that Bounous and Gold couldn't. Remember? Denaturation of a protein is defined as a change in the molecular structure by heat, addition of acid or alkali, or by radiation. Cheese whey receives every damaging treatment except for radiation. Cheese whey is heat pasteurized twice at 72^o C for at least 15 seconds - and - it is exposed to significant acid - and it is also exposed to alkali.

Let's start with pasteurizing temperatures. Why is 72^o C so different from the lower, yet still legal, pasteurizing temperature of 63^o C for 30 minutes? For the simple reason that the "thermolabile" (heat sensitive bioactive proteins) whey proteins that concerned Bounous and Gold start to denature at 64^o C. We can stay below the denaturation temperatures of the most heat sensitive fractions of whey protein by pasteurizing at 63^o C for 30 minutes. When milk or whey is pasteurized at 72^o C for at least 15 seconds, those heat sensitive fractions of whey protein start to unfold (change molecular shape) and, therefore, lose their desired bioactivity. There are those in the dairy industry who will claim that pasteurizing at 72^o C for 15 seconds has been shown to cause minimal denaturation. That may be true - but what does "minimal" damage mean? Do the heat sensitive proteins survive intact? What happens if whey proteins are exposed to two of these heat treatments in a row? Data collected thus far shows at least partial damage (some denaturation) to the heat sensitive whey protein fractions from one 72^o C pasteurization treatment.

Bounous and Gold found significant damage (significant denaturation) in the whey proteins from cheese whey that they studied. Why? Because cheese whey proteins have been heat pasteurized twice (exposed twice to damaging heat) and they have also been exposed to damaging acid and alkali. You see, when manufacturing cheese, you must start with sterile milk. You can't have unwanted bacteria in the milk because they may cause off flavours in the cheese. Therefore, pasteurization of the milk prior to cheese manufacture is required. This would be the first heat treatment. To manufacture cheese, specific bacteria are then added to the sterile milk and allowed to multiply and grow. As they grow and multiply, these bacteria produce significant amounts of acid (significant enough to cause a change in molecular structure of other bioactive whey proteins such as lactoferrin - denaturation). Once the milk becomes sufficiently acid in pH, an enzyme is added to the milk and a cheese curd precipitates out, leaving a foul smelling, yellow-green colored liquid that we call "whey". This liquid whey contains about 6% to 7% solids of which only 11% is protein (about 0.7% of the liquid whey). To make a whey protein concentrate or isolate from this liquid whey, it is necessary to ultrafilter, and/or microfilter, and/or nanofilter the whey. All three are filtering processes - the difference is in the size of the microscopic holes used. If the holes are sized correctly, the proteins (large molecules) can't fit through the filter holes, while all of the smaller molecules (undesirable lactose, mineral ash, etc) pass through the holes and are separated from the protein. Simple right? It would seem so, but there are a few obstacles to overcome to make the microscopic filtering proceed smoothly. First, the liquid cheese whey is loaded with the bacteria that were allowed to grow and multiply so that the cheese could be manufactured. These bacteria are at least as large as the protein molecules and even larger. If liquid cheese whey is filtered with these bacteria present, the resultant whey protein would contain as much, or more, bacteria as it does whey protein. The cheese bacteria have to be destroyed before whey protein can be filtered. How are the bacteria destroyed? With another heat pasteurization step at 72^o C (the second, damaging heat treatment step). Now the cheese whey is sterile but it does contain some insoluble particles (probably partially denatured protein, some tiny cheese curds, and even insoluble milk minerals such as calcium phosphate). These insoluble particles will "blind" (plug) the microscopic holes in the filters, thereby rendering the filtering process useless. It is, therefore, necessary to remove all insoluble particles from the liquid whey prior to filtering. This is accomplished by adding alkali (denaturation) in most cases and adjusting the pH of the whey to a level that would cause most of the insoluble calcium phosphate to become soluble. The liquid whey is then passed through high speed centrifuges (known as clarifiers) to remove any remaining insoluble particles (this would include any whey proteins that were denatured by the two heat treatments, the acid, and/or the alkali). No wonder, the whey proteins that we see from cheese whey are water soluble! They have been centrifuged during processing to ensure maximum water solubility. What was removed during centrifugation? According to Bounous and Gold: significant portions of the bioactive whey proteins.

As another, more empirical method, for proving the heat denaturation of whey proteins made from cheese whey, we can offer the following example:

When you fry an egg, what happens? You start with breaking an eggshell and dropping the contents into a frying pan. Initially, the egg white (a 12% protein solution) isn't actually white - it's clear isn't it? This is the egg albumen (protein) in undenatured form. As heat is added, the clear egg white turns an opaque white - the protein denatures. A sulfur smell develops (because the metabolically valuable amino acid, cysteine, contains sulfur and as the cysteine is being heat degraded it releases sulfur). Any time you detect a sulfur smell in a protein factory, you can be sure that cysteine is being degraded (a sure sign of protein denaturation). Walk into any cheese factory in the world and visit the whey processing area. You will smell a strong sulfur smell. When you smell sulfur in a cheese factory, you can be sure that the high cysteine whey proteins (serum albumin and immunoglobulins - the bioactive ones) have been denatured because they are releasing sulfur. This is just more practical evidence that whey proteins manufactured from cheese whey have been heat damaged.

What makes Product X of Bounous and Gold so different? That's what we wanted to know. After a long search, we found an obscure paper written by Phil Gold in which he described the process used to manufacture Product X. Product X was manufactured directly from skim milk - not from whey as the starting material. The process utilized a low temperature, long hold pasteurization treatment (63^o C for 30 minutes), to keep the heat treatment below the denaturation temperature of the heat sensitive bioactive proteins, and no acid or alkali had been added to the milk at any point in the process. They had avoided denaturation of the proteins as much as was humanly possible. Looking at the process they used to make Product X, we thought that it would be possible to find a factory somewhere in the world that would be willing to manufacture a whey protein by the process. You would think that a large number of factories would be willing to manufacture by the process, but it is the low temperature, long hold pasteurization that stops them. To hold milk for 30 minutes during pasteurization slows a dairy factory down to a crawl. They have all been designed and constructed to pasteurize milk for 15 seconds at 72 ^o C. They cannot work out how to pasteurize for 30 minutes. We sought the assistance of a friend who had knowledge of every whey protein manufacturing factory in the world. We asked him to find a factory that would manufacture a whey protein concentrate by the process as outlined by Phil Gold (a copy of Product X of the paper by Bounous and Gold). He found one factory - only one - that was willing to manufacture by the process.

Our whey protein comes from that factory. It is as close as anyone can get to Product X in a large scale commercial ultrafiltration factory. Sure, we have to pay more for it because the factory runs slower and we don't start with a waste product (like cheese whey), but Bounous and Gold have already shown that is it significantly superior in bioactive properties to any whey protein made from cheese whey for the reasons outlined above. And now, you should understand that, the next time you see an advertisement for whey protein, it doesn't matter how much they want to talk about the excellent water solubility of their whey protein - IF IT COMES FROM CHEESE WHEY IT HAS UNDERGONE DENATURATION. It can have excellent water solubility, an excellent amino acid profile, and yet, no bioactivity. Sure, we all consume protein for an excellent amino acid profile so that we can make lean tissue gains. It is the bioactivity of a protein, however, that will provide the extra, winner's edge for greater gains in health and lean tissue by stimulating a cascade of anabolic processes.

Fast versus Slow Digesting Protein - Which One Is Better?

There are very few "facts" in sports nutrition that people won't argue. One of the accepted facts, however, is that casein is a"slow" digesting protein and whey proteins are "fast" digesting. There are those who would like to convince the world that whey protein is the perfect protein for athletes. The main reason they make the claim is that "whey protein is fast digesting and fast absorbed". Are there scientific studies that show fast digesting / absorbing proteins to be more anabolic? Is a slow digesting protein of any advantage for athletes? The argument raged until a study was published in December 1997 in the Proceedings of the National Academy of Science USA. The scientific study, performed by Yves Boirie and others, was entitled: Slow and Fast Dietary Proteins Differently Modulate Postprandial Protein Accretion. A fancy title that simply means slow digesting and fast digesting proteins are absorbed differently and utilized differently by the body after they are eaten. The authors of the paper designed a study wherein they started with healthy adults and fed one group a truly undenatured whey protein (manufactured specifically for the study in a laboratory) while another group was fed micellar casein. Both proteins were obtained from the same cows' milk. The cows had been fed radiolabeled amino acids so that both the casein and the whey protein from their milk contained radiolabeled amino acids. The authors followed the digestion, absorption, and metabolic fate of each protein by keeping track of the radiolabeled amino acids.

Boirie and his associates found that whey protein "induced a dramatic but short increase of plasma amino acids."Casein, on the other hand, "induced a prolonged plateau of moderate hyperaminoacidemia (elevated amino acid levels in the blood), probably because of a slow gastric emptying." To translate, they found that after eating whey protein, there is a short window of time (from about 45 minutes after consumption to perhaps 2 hours after consumption) where amino acid levels are significantly elevated in the blood. On the other hand, after consumption of casein, the amino acids remain at a somewhat lower elevated level in the blood but for a window of more than 7 hours after consumption. Why are elevated amino acids in the blood important? You can't build new muscle or repair damaged muscle if you don't have the building blocks readily available. Amino acids are the building blocks of muscle tissue and they are only available for muscle repair / construction when in the blood at elevated levels. Casein consumption maintains elevated amino acids in the blood for more than 7 hours after consumption while whey protein amino acid levels fall to near baseline levels after 2 hours.

The authors also found that "protein synthesis was stimulated by 68%" with whey protein and "to a lesser extent (31%)" with casein. Whey protein appears to be better at stimulating protein synthesis. Why is this important? "Protein synthesis" can be translated to mean the manufacture and/or repair of muscle tissue. A strong word of caution is needed here: this result, as analyzed and stated, does not mean that whey protein is more than twice as effective (or as so many of the "math geniuses" in sports nutrition have stated in their marketing ads - 219% more effective) as casein at stimulating protein synthesis. The authors themselves stated that total protein synthesis "was stimulated by 68% and 31% (average from 40 to 140 min) with WP and CAS respectively, the difference between the two diets being NOT SIGNIFICANT although there was a trend for higher protein synthesis with WP." Because of the experimental design, the seemingly widely varying result was not considered by the authors as demonstrating a significant difference between whey protein and casein concerning protein synthesis - but the whey protein did show a tendency to stimulate protein synthesis better than casein. This cannot be interpreted to mean "twice as effective" or "219% more effective." It signifies basically what the authors say - the data showed that there was a TREND for higher protein synthesis with whey protein.

What was the fate of the two proteins after they were consumed by the test subjects? A much higher percentage of the whey protein amino acids were oxidized by the liver for energy rather than utilized to make muscle tissue, when compared to casein. Because casein digested slower and released amino acids into the bloodstream at a slower rate and over a longer period of time, significantly fewer amino acids from casein ingestions were oxidized for energy by the liver. Perhaps the most important finding from the study was that "an index of protein breakdown did not significantly change after the WP (whey protein) meal. It was progressively and durably inhibited from 120 minutes to 420 minutes with CAS (casein)." In other words, casein is anti-catabolic (prevents muscle tissue from being broken down) while whey protein showed no anti-catabolic properties.

Finally, the authors concluded that "CAS (casein) promotes postprandial protein deposition." Simply put, it means that more amino acids are stored in the body for future use after casein consumption than after whey protein consumption. In other words, you get your money's worth when you eat casein.

Here was a scientific study that showed that whey protein will stimulate protein synthesis better than casein and that casein was anti-catabolic while whey protein had no anti-catabolic properties. The study also proved that more amino acids are retained in the body for use in manufacturing new and stronger muscle fiber after consumption of casein. Should we then formulate our protein powder with more casein than whey protein? Why not use more whey protein than casein - isn't protein synthesis more important? We found our answer in human maternal milk. You see, every mammal produces milk for its baby's nourishment. The milk each mammal produces is custom tailored to fit the requirements of that species' digestion / metabolism. Cow's milk, for instance, is roughly 82% casein and 18% whey protein - the perfect ratio for a calf. On the other extreme, a cheetah's milk is 67% whey proteins and 33% casein - a ratio that is tailored for a baby cheetah. Human maternal milk is approximately 50% whey protein and 50% casein (it has sometimes been analyzed as high as 60% whey protein and 40% casein). That makes perfect sense in light of the Boirie et. al. study. Our bodies will use whey protein to stimulate protein synthesis and then follow up with longer lasting casein to continue muscle repair / growth as well as prevent muscle destruction. Both proteins are, evidently, necessary for a growing human body and both seem to possess equal metabolic importance. If the creator of the universe felt that both were equally important for us humans, who are we to argue? We decided to set our ratio of casein and whey proteins to match the ratio found in human milk.

Egg White

We also add some egg albumen (egg white) to the protein blend. Why? Because egg albumen, like the best bioactive fractions of whey protein, contains high quantities of the sulfur containing amino acid, cysteine. Cysteine is an essential building block for the body to manufacture glutathione, the body's natural defense against unhealthful and harmful oxidation reactions (the body's antioxidant and anti-inflammatory). Studies have also shown that higher intracellular muscle tissue glutathione contents are directly related to increased muscle size and strength. Increased glutathione levels have also been shown to be directly linked to good health by strengthening the immune system. Good health means fewer down days and more training days.

Glutamine

Glutamine is the most abundant amino acid in the human body. It is also the most abundant amino acid circulating in the blood. 60% of the free amino acids in muscle tissue are Glutamine. As you can see, Glutamine is a very important amino acid for humans. It is not, however, an essential amino acid - because our body can synthesize Glutamine from numerous other amino acids in the mitochondria (the power generating factories of our cells). Glutamine improves intestinal health by maintaining healthy intestinal lining, plays a major role in protein synthesis, aids in replenishing muscle glycogen stores (glycogen stores increase muscle volume), has been shown to stimulate and strengthen the immune system, will apparently help to stimulate growth hormone production, and can be the starting point of the Krebs energy cycle in the mitochondria (Glutamine can be converted to pyruvate and alanine - pyruvate is converted to alpha-ketoglutarate, the starting point of the Krebs Energy Cycle. Alanine is converted by the liver to glucose, supplying extra fuel to muscles during prolonged exercise.). Glutamine is also another building block of the body's own antioxidant / anti-inflammatory compound, glutathione. Glutathione is comprised of three amino acids (a tripeptide) - Glutamine, cysteine, and glycine. Glycine is a common food amino acid, but it's most important to feed the body the other two - cysteine and Glutamine. Between our undenatured whey protein and the egg white that we add to our protein powders, they contain plenty of cysteine. We needed to add extra Glutamine. When designing a supplement for athletes, it's always a good idea to include additional Glutamine quantities anyway. Would you be surprised to learn that numerous governments around the world have recommended that a person who is under stress should supplement their normal diet with 20 grams of Glutamine per day? The definition for a person under stress is someone suffering from a chronic, debilitating illness (such as cancer or AIDS) or a hard training athlete. That's right! A hard training athlete is as depleted of Glutamine as a person who is in a battle for their very life. A person suffering from a chronic illness loses large quantities of Glutamine daily as the body uses Glutamine as a precursor for rapidly dividing immune cells. Athletes lose Glutamine every time they exercise because as exercise intensifies, the demand for energy increases. Glutamine will be used as the starting compound of the metabolic cycle when other supplies are depleted. Intense exercise can quickly deplete the supply of Glutamine in muscle cells by up to 40%. Unless the depleted Glutamine is replaced in a timely fashion, muscle tissue will be broken down (catabolized) to liberate glycogen (which is stored in muscle tissue). Supplementation with 3 to 4 grams doses of Glutamine 4 to 5 times per day has been shown to slow down muscle breakdown (catabolism) by providing sufficient starting material for the energy cycle without the need to steal Glutamine from muscle tissue.

Glutamine supplemented diets have also been linked to improved intestinal health. ƒÆ’ †â€™ ƒÂ¢ ‚¬ …¡ ƒÆ’ €š ƒâ€š   Studies have shown that glutamine enriched diets lead to improved gut barrier function (transport of food nutrients across the intestinal wall and into the blood for use by the body), intestinal cell proliferation and differentiation, as well as reducing septic morbidity and symptoms of Irritable Bowel Syndrome. Much of glutamine's function in the gut is to maintain a healthy intestinal lining. The human intestine replaces its lining every 72 hours. Large amounts of Glutamine are required for lining replacement. If the body has uses for Glutamine elsewhere, repair of the intestinal lining is of lower priority. As we stated before, in the body of a hard training athlete, Glutamine is in high demand. As a consequence of Glutamine shortage, the intestinal lining can be poorly maintained. Poor lining function translates to poor absorption of food nutrients. The body won't efficiently absorb nutrients from the diet. Athletic performance will start to suffer. Supplementation of the diet with additional Glutamine serves to provide sufficient quantities of Glutamine to avoid muscle catabolism (breakdown) as well as maintain the intestinal lining. Food nutrients are absorbed better and performance increases.

Most companies add L-glutamine (a Free form amino acid) to their products. We don't. We use peptide bonded Glutamine (glutamine that is linked by the standard amino acid linkage to other amino acids). The reason we use peptide bonded Glutamine rather than free form L-glutamine is that numerous studies have shown that free form amino acids are only absorbed efficiently when consumed in small doses and on an empty stomach. When free form amino acids are combined with other food nutrients, even fat or carbohydrates, they are not absorbed into the bloodstream from the intestines efficiently. You see, they have to compete with a number of other nutrients in the intestines to be transported across the gut barrier and into the blood. To understand this, picture a large skyscraper in your mind. The ground floor lobby of the skyscraper is the inside of the intestine. There are 20 elevator (lift) doors in the lobby. Only 2 of those doors provide access for a free amino acid and other food nutrients to be taken up to the top for entrance to the bloodstream. It's rush hour. All of the nutrients in the food you just ate are in the lobby. They are all waiting for those 2 doors to open so that they can be taken up. Every time the doors open, they all push for entrance. Only a certain percentage makes it inside. At the same time, at the far end of the lobby, there are security people pushing everyone out of the lobby towards the exit doors. They push and push, constantly moving everyone towards the exit (this is what happens in the intestines - they constantly undulate, moving digested food through the intestinal labyrinth until it is expelled.). How many chances does a nutrient get to make it into the elevator (lift) before it is pushed beyond the uptake site and out of the lobby? Not many. Only a small percentage actually make it into the uptake system and into the blood by the very competitive system that free amino acids must endure in the intestines.

What about the other 18 elevator (lift) doors in the lobby? They are express elevators. They are available only for amino acids that are peptide bonded to one or two other amino acids. These peptide bound amino acids easily gain admittance to the uptake system and make it into the bloodstream. This is the way that the human intestinal uptake system was designed. We consume a protein. The protein begins to be digested in the stomach. Smaller pieces (peptides) break off and make their way into the intestines. They are broken down further into even smaller pieces (peptides) as they travel through the upper intestine. Eventually, they are broken down to di- or tri-peptides (two amino acid pieces or 3 amino acid pieces). This is the peptide length that our intestines were designed to efficiently absorb. There is not competition from other food nutrients for those uptake sites and there are plenty of them. The peptides are efficiently absorbed into the blood.

A study released in 2003 proved that supplemental Glutamine, in the form of peptide bonded Glutamine, is more efficiently absorbed and utilized by the body than free form L-glutamine. The main difference between the two forms of supplementation? In the intestines! Basically, the study showed that peptide bonded Glutamine increased intestinal Glutamine content while free form L-glutamine supplementation did not increase intestinal Glutamine concentration. The study indicates that supplementation with free form L-glutamine does not provide sufficient Glutamine to serve all of the required metabolic functions (because the intestines weren't getting sufficient quantities). Supplementation with peptide bonded Glutamine, on the other hand, provides enough Glutamine to power muscles during intense exercise as well as improve intestinal health. Improved intestinal health means better, more efficient absorption of nutrients that we eat. We waste less money from our food budget and we make healthier bodies.

Probiotic (Good) Organisms

In keeping with the idea of promoting healthier intestines and better digestion / absorption of food nutrients, we also add live, viable probiotic (good for you) organisms to our powders. We accomplish this by"culturing" (allowing probiotic organisms to grow and multiply) the micellar casein with bifidus, acidophilus, and yogurt organisms. These organisms were carefully selected. Would you be surprised to learn that the average human adult carries around about 4 pounds (almost 2 kg) of organisms in their intestines? Obviously, these organisms become a major factor in our overall health, good or bad, depending upon what type are present. Bifidus is the organism that is native to our intestines. We have large amounts of bifidus in our intestines when we are born. Bifidus helps in food digestion and produces Vitamin K as a byproduct for use by our bodies. Bifidus, however, is fragile and is easily destroyed by other, less healthful types of organisms - like yeast and mold. By the time we reach adulthood, the average human being plays host to about 70% harmful organisms (2.8 pounds) and 30% probiotic organisms (1.2 pounds). Numerous studies over the past 30 years have shown that changing the balance from mostly bad organisms to mostly probiotic organisms in the intestines can significantly improve health - less colds, less flu, etc.

Within the last 6 years, new studies have shown that the type of organisms in your intestines also have a significant effect on how you digest, absorb, and utilize food nutrients. Dr. Jeffrey Gordon of Washington University has performed numerous studies on the balance of good versus bad organisms in the intestines. He and his group have found that obese people possess higher amounts of bad organisms in their intestines than do lean people. He has also shown that obese people will lose body fat if they can increase the level of good (probiotic) organisms in their intestines. Here's a scary thought, by decreasing the level of good organisms in the intestines of healthy, lean people, he has shown that they will gain body fat. The theory is that the bad type of organisms (including yeast and mold) are most efficient at harvesting fat from the food we eat (compared to probiotic type organisms). The bad organisms also appear to have the effect of stimulating fat uptake into the bloodstream and stimulating fat storage by the body. It appears that probiotic organisms are more efficient at harvesting protein from the food we eat and stimulating the uptake of amino acids into the bloodstream.

How can we change the balance of organisms in our intestines? Because Bifidus is so fragile, we need to consume live, viable bifidus organisms every day to replenish the supply. We also need to "make room" for the bifidus in the intestines. Yeast and mold organisms are very hardy and they do quite well in our intestines. They grow easily and "choke out" bifidus. Acidophilus organisms grow fast and easily in our intestines - just the right environment. Acidophilus will grow and multiply so fast that these organisms will "choke out" mold, thereby decreasing mold organisms counts and allowing bifidus the space to grow and multiply. Likewise, yogurt organisms have been used for centuries as a folk remedy to cure yeast infections. Yogurt organisms are very effective at killing yeast cells. We include acidophilus and yogurt organisms in our micellar casein culture because we want to lower intestinal levels of the bad organisms, yeast and mold, thereby allowing bifidus to grow and thrive. Yogurt and acidophilus organisms also help maintain a healthy environment for bifidus organisms to thrive once the intestinal balance has been shifted. It doesn't do much good to consume active bifidus organisms every day unless one is also "cleaning up" the intestines by getting rid of those organisms that would choke out the bifidus organisms.

Conclusion

There you have it! A thorough explanation of why our protein powders are so effective at promoting anabolism (the positive part of our metabolism).

• Micellar Casein - Bioactivity, extended amino acid release, and skeletal support. Longer retention of amino acids in the body than from whey protein.
• Undenatured Whey Protein - Not made from cheese whey or casein whey. Scientifically proven to be significantly more bioactive than whey protein manufactured from cheese whey. Stimulates protein synthesis.
• Fast and Slow Digesting Proteins - In a ratio that fits human beings.
• Egg White - An excellent source of cysteine, the sulfurous amino acid that is a required precursor for the body to manufacture glutathione.
• Peptide Bonded Glutamine - Scientifically proven to be more efficiently utilized by the body than free form L-glutamine.
• Probiotic Organisms - to assist improved health, digestion, and absorption of food nutrients as well as stimulate better usage of food nutrients for an athlete.

Don't let anyone try to confuse you. Our products are based on real science.