Protein - The Basics and Everything Else

Written by  BodyActive Technical Panel
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Science has long told us it that only 20 percent of your daily calorie intake comes from proteins. However, there may be some good reasons for increasing your protein intake while decreasing fat and carbohydrates.

Protein is a macro nutrient composed of upto 21 amino acids and is the only macro source of nitrogen in the diet. Amino acids consist of an amino group, a carboxyl group, a hydrogen atom, and a distinctive R-group, all bonded to a carbon atom. Many amino acids join together by peptide bonds to form a polypeptide chain.

In 1953 Frederick Sanger determined the amino acid sequence of insulin, a protein hormone. This was a landmark discovery because it showed for the first time that a protein has a precisely defined sequence which determines its function. Each protein has a unique, precisely defined amino acid sequence.

The human body can make the majority of the amino acids however 9 of these are impossible to synthesise and so have to be taken in through the diet and are thus termed essential amino acids. Without them you would degenerate and die, it is as simple as that.

Over 50% of the dry weight of your body is protein and all bodily functions are controlled by enzymes which are also proteins. Protein is therefore undoubtedly a key nutrient for the human body.

Over 98% of the molecules that make up the human body are completely replaced each year. The body you have today is built almost entirely from what you have eaten over the past six months. The well-known saying "you are what you eat" is founded on the fact that the body is in a constant state of change at the chemical level. Protein is the primary building material for the human body, remove the water from the muscle and nearly everything that is left is protein. Consequently, eating the correct levels of protein is essential. The quality of the protein that you eat is also important, if you eat poor quality protein then all of the structures of your body synthesised from that protein will be poor quality.

There are two key questions to be answered here:

-How much protein do you need to take in?

-What is good quality protein?

The amount of protein required in a diet varies dramatically between sedentary individuals and athletes. This is because protein is used for energy providing 5-10% of the total energy supply during intense training. Also, protein is lost from the body in sweat and hemolysis (death of red blood cells) which increase substantially during exercise.

So, how much protein is needed for athletes?
A very high protein intake will maintain a highly positive nitrogen balance which is necessary for the building of muscle. However, it is not simply the protein that you eat that controls the use of nitrogen for muscle building. Such use is controlled by the processes in the liver that holds the available store of amino acids at precisely the level required to meet bodily demands. Any excess protein is simply broken down into carbohydrates and urea. It is therefore bodily demand that dictates how the protein you eat will be used, not the amount of protein taken in itself. If you take in masses of protein in the hope that it will build muscle you will see little in the way of results as any protein ingested in excess of what your body currently believes it needs, will simply be passed out of the body in the urea. Muscle growth is caused by the trauma of intense exercise. Following intense training your body will recognize that it is in need of more protein than it previously required and so any extra protein ingested will be utilised as opposed to expelled. Any use of anabolic growth agents such as steroids causes a rapid buildup of nitrogen balance and protein within the cells and your demands fro dietary protein dramatically increase.

The trick is therefore to match your protein intake to your training program.

Protein does nothing to stimulate growth, it simply provides the necessary materials for growth which is stimulated by the trauma placed on muscles during training. Preceeding growth, it only makes sense that there must be some form of stimulation for growth to occur.

Proteins play crucial roles in virtually all biological processes.

Enzymatic Catalysts
Nearly all chemical reactions in biological systems are catalysed by specific macromolecules called enzymes -nearly all enzymes are proteins, therefore proteins are central to determining the pattern of chemical transformations in biological systems such as the human body.

Transport and Storage
- Myoglobin (a protein) transports oxygen in muscles.
- Coordinated Motion
- Proteins are the major component of muscle and muscle contraction occurs by the sliding motion of two kinds of protein filaments.

Mechanical Support
The high tensile strength of skin and bone is due to collagen, a fibrous protein.

Immune Protection
Antibodies are highly specific proteins that recognise and combine with foreign substances and are therefore vital in distinguishing between self and non-self.

Generation and Transmission of Nerve Impulses
- The response of nerve endings to certain stimuli is controlled by specific receptor proteins.
- The remarkable range of functions mediated by proteins results from the diversity and versatility of the amino acids which are the building blocks of protein.


Protein is made up of Amino Acids which are considered to be the building blocks of life. There are nine essential amino acids which must be obtained in the diet. In addition there are a further 13 amino acids present in protein which are considered non-essential as they can be synthesised by the body. There are also many other amino acids but they do not form parts of protein.

Research over recent years has shown that the human body has evolved to best utilise amino acids which are in dipeptide and tripeptide form (these are most commonly found in hydrolysates, ion exchanges and cross flow prepared whey proteins) which simply means two or three amino acids have been joined together. These are better absorbed, and retained, than both whole food proteins and free form amino acids.

There are a group of amino acids called Branched Chain Amino Acids (BCAA) which play an important role during exercise. They are the main amino acids to be sacrificed from muscle tissue during muscle catabolism. BCAA consist of three amino acids; leucine, Isoleucine, and Valine. The cause of this breakdown is that during exercise large amounts of the non-essential amino acids alanine and glutamine are used, in fact more than the body stores, and the deficit is made up by the body converting BCAA's into these two aminos.

To prevent this breakdown it has become common to try to raise blood levels of BCAA prior to exercise to reduce muscle breakdown. Supplementing with Glutamine directly after training then further reduces post exercise catabolism.

Glucogenic Amino Acids is a term used to describe the three amino acids threonine, glutamine and arginine. This term means that they lend themselves to glucose production, which is used for energy during exercise. Ample levels of these aminos may help prevent muscle breakdown, and has also been shown to increase feed efficiency in animals (ie grow more from the same amount of food).

Protein technologies have identified a group of amino acids called the Critical Cluster Amino Acids which play a big part in muscle sparing during dieting or intense exercise. This cluster consists of the three BCAA's along with Glutamine and Arginine which are two 'conditionally essential' amino acids. Around 45% of whey protein consists of the critical cluster aminos, with milk (casein) and soy protein isolate next in line at around 36%.


This is a basic amino acid due to its aromatic nitrogen-heterocyclic imidazole side chain. It is biochemically metabolised into the neurotransmitter histimine.

This amino acid has no other significant biological role than incorporation into proteins and enzymes where main purpose is to help dictate tertiary structure of macromolecules.

This is a hydrophobic amino acid found as a structural element on the interior of proteins. It is the second most common amino acid found in proteins

This amino acid is commonly found at the surface of proteins and is present in meat, fish, poultry and dairy.

This amino acid helps to initiate translation of RNA by being the first amino acid incorporated into the N-terminal position of all proteins.

Plays a key role in the biosynthesis of amino acids and neurotransmitters.

Plays an important role in Porphyrin metabolism.

Is the biosynthetic precursor to the important neurotransmitter serotonin.

Determines the 3D structure of proteins due to its hydrophobic nature. Sources include soy flour, cottage cheese, fish, meat and vegetables.


Involved in the metabolism of tryptophan. One of the simplest amino acids most widely used in protein construction. It has little therapeutic role in humans however has been shown to have a cholesterol reducing effect in rats.

A complex amino acid often found at the active catalytic site in proteins and enzymes. Is actually an essential amino acid during the juvenile period in humans. Natural sources include brown rice, nuts, raisins, and whole wheat.

A derivative of Aspartic Acid. Has an important role in the biosynthesis of proteins.

Aspartic Acid
This amino has a paramount role in metabolism during construction of other amino acids and biochemical's in the citric acid cycle.

Often involved in the three dimensional stability of proteins and critical to the metabolism of coenzyme A, biotin, lipoic acid, & glutathione.

Glutamic Acid
Negatively charged and therefore very polar and usually found on the outside of proteins where it is free to interact with intracellular surroundings.

Has an important role in cellular metabolism of animals and is the only amino acid with the ability to easily cross the barrier between blood and brain. It also has a central role in the regulation of bodily ammonia levels.

This is the simplest amino acid and is essential for the biosynthesis of nucleic acids as well as bile acids & creatine phosphate. It is the second most common amino acid found in proteins which has the ability to inhibit neurotransmitter signals in the central nervous system.

This is a major component of the protein collagen, the connective tissue that binds and supports other tissues.

This amino has a major role in a variety of biosynthetic pathways including those involving pyrimidines, purines, & creatine.

Determines the three dimensional structure of proteins due to its hydrophobic nature. Sources include soy flour, cottage cheese, fish, meat and vegetables.



Nitrogen balance is one of the phrases you will hear batted around all of the time when you begin looking into the realm of exercise training and nutrition. But what exactly is nitrogen balance and why is it so important?

Nitrogen is provided by all proteins. Exercise causes the body to use proteins at a much faster rate than at rest. Now, a positive nitrogen balance means that the body is obtaining sufficient proteins from the diet that you are supplying. Whenever your body slips into a negative nitrogen balance this is the state where your body has insufficient input of protein and is therefore cannibalising muscle and other protein structures to provide its daily needs. You don't need to be a rocket scientist to understand that this means that all of that time and effort you spent building that muscle up is being flushed down the toilet, as your body literally eats its own muscle to provide the proteins it requires.

A study performed by Gontzea at the institute of medicine in Bucharest (1974) shows us that athletes instructed to stop exercising and remain sedentary for 2 weeks, and were given a daily intake of 1 gram of protein per kg of bodyweight (this being 33% above the RDA). Now so long as these athletes remained sedentary they maintained a positive nitrogen balance. When these subjects were returned to their two hour daily workouts, within two days, nitrogen balanced dropped into a negative state. This means they began breaking down their own muscle tissue as opposed to building it up as you would hope for from regular intense training.

Dr Peter Lemon et al, at the Kent State University Ohio (1989) repeated the above Gontzea study and found that endurance athletes in regular training required 1.14 - 1.39 grams/kg of bodyweight daily to remain in a positive state of nitrogen balance.

There is absolutely no doubt that a very high protein diet of around 3.0grams per kg of bodyweight per day maintains a highly positive nitrogen balance. But the use of nitrogen for building muscle is not controlled by the protein that you eat, it is controlled by the liver that holds the available store at precisely the level required to meet daily demands, and all excess protein is simply broken down as it is not needed.

So theoretically there are no additional benefits to consuming an intake of protein above and beyond what your body is in demand for, with the exception of dietary manipulation in order to achieve certain specific health or fat loss goals.

It is also worthwhile to note that excess protein fills your blood with more than the amino acids that make it up. And excess amino acids are converted into highly toxic ammonia.

One thing that you should bear in mind when it comes to choosing the quality of your proteins is that a deficiency in just one amino acid results in a negative nitrogen balance - more protein is degraded than is synthesised and so more nitrogen is excreted.


The Glycaemic Index was developed in 1981 by Dr. David Jenkins, a Professor of nutrition at the University of Toronto as a tool to better understand how the body responds to carbohydrates. It is essentially a ranking of a catalogue of foods from 0 - 100 that tells us whether a food will raise blood sugar levels dramatically, moderately, or a little.

Foods with a score of 60 or less are considered to have a low GI, whilst foods with a score over 60 are considered to have a high GI.

Refined dietary sugars almost always turn into fats and starches can also turn into saturated fats. This is the process by which carbohydrates enter the bloodstream as sugar. This sugar is energy for your brain and body. If it is not used up absolutely immediately it cannot just hang around in your blood stream doing nothing. What does your body do? It secretes the storage hormone insulin in response to your carbohydrate intake. This insulin then stores glucose in the muscle and liver as stored glycogen, ready for immediately energy use. There is a limit to how much glycogen that you can store within your muscle - obviously limited by the size of your skeletal muscle tissue. Glycogen storage for a 150lb athlete is radically different than a 300 lb Mr Olympia competitor - who definitely can store much more. Of course once your muscle glycogen and liver are full up to the maximum, the glucose must be converted into energy to be able to stored for a later date. So what happens within the body is that your glucose is converted into fat and the insulin itself, that was used as the hormone, is converted into triglyceride and stored in your fat cells for use as energy of a later date.

When you eat a carbohydrate rich meal your body responds by secreting the hormone insulin form the pancreas. Insulin signals the fed-state and stimulates the storage of fuels such as glucose. The greater the rise in blood-sugar, the more insulin produced. Glucose is stored as Glycogen in the liver and the muscles. This storage facility however has a limited capacity, any excess glucose that cannot be stored as glycogen enters the adipose (fat) cells of the body and stimulates the production of triacylglycerides. Consequently, if an individual's blood-sugar constantly fluctuates above the maximum storage capacity the excess glucose that they ingest will be stored as fat. Foods with a high GI factor raise blood-sugar levels very high very rapidly and are therefore likely to push glucose levels above that that can be stored by the body as glycogen. High GI foods are therefore likely to promote the storage of fat. Foods with a low GI factor raise blood-sugar levels slowly and steadily, just enough to keep supplies of glycogen topped up without stimulating fat synthesis.

This is generally well known and accepted. Now, when you digest proteins, they are themselves a different chemical structure than carbohydrates. Proteins are not directly, nor initially, broken down into carbohydrate, although they can be through another process. Proteins are digested and assimilated into their amino acid components. This does not appear to raise blood glucose levels much at all, and so you will probably not find many protein foods on the glycaemic index rating or ranking. Although, this does not mean that protein does not stimulate the release of insulin, because it does. Insulin is a storage hormone and amino acids require storing. When you consume proteins with carbohydrate, you generally have an overall lowering of the GI factor - a slightly slowed release of sugar into the blood stream.


Insulin is probably the single most important hormone that will make a particular dramatic change to your physique and your health and life span. So what is insulin and how is it affected by the proteins that you consume in your diet? Well, Insulin is a hormone released into the blood by an internal organ called the pancreas. Insulin functions in many ways as an anabolic, or a storage hormone; in fact it's been called the most anabolic hormone. When insulin is released into the bloodstream, it acts to shuttle glucose [carbohydrates], amino acids, and blood fats into the cells of the body. It is actually proteins and carbohydrates that both affect your insulin production. Fat does not stimulate the production of insulin at all as it is digested and absorbed by the human body by a different mechanism. Now, the insulin index actually measures insulin response to a food. So rather than just making the assumption that insulin response is indeed correlated with carbohydrate absorption (such as predicted by the GI scale), researchers decided to go ahead and measure it. And their results were eye opening!

Insulin is very much misunderstood. It is of course a storage hormone. It shuttles nutrients (proteins as amino acids and carbohydrates as glycogen) into places like skeletal muscle tissue. Insulin can be as much an ally as an enemy, when it comes to building muscle and burning bodyfat.

Used together, the GI and II indices can help you plan meals according to your needs (i.e. high or low insulin release). Why would you want high or low insulin release and what affect does protein have on insulin release. For instance, if you're trying to get lean you'll want to keep insulin at bay most of the day except immediately after training when you want to spike it through the roof to shuttle glycogen and protein back into your starved muscles. Maintaining steady and stable, low insulin levels allows the process of fat burning to take place. As soon as insulin levels rise, fat burning grinds to a halt.

What you need to know is that not only do carbohydrate stimulate insulin, so do proteins. And certain proteins can spike insulin through the roof. Whey hydrolysates and specific amino acid combinations are being used in many post workout drink formula's, as when they are mixed with a high insulin carbohydrate blend, they cause a synergistic high insulin response - perfect for shuttling nutrients back into muscle cells for repair and growth.

In terms of fat loss - In this scenario you'd eat a combination of low GI and II foods throughout the day. If, on the other hand, you're trying to bulk up and gain quality muscle, you'll no doubt want to spike insulin several times throughout the day along with a generous helping of protein. Shuttling amino acids into muscle cells. Protein being used as the source of amino acids and nitrogen for muscle growth and the assistance in releasing more insulin.

One of the goals of eating to grow should be to maximize the muscle gain to fat gain ratio. Basically, if you want to pack on the most muscle with the least amount of fat gain. To do this you need to understand which meal combinations to pursue and which to avoid. The foundations of the recommendations in this area are based on the avoidance of a nasty scenario. The worst case scenario for someone trying to pack on muscle while minimizing fat gain is to have high blood levels of carbs, fat, and insulin at the same time. This is deleterious, not only to ones appearance, but to ones health. If you eat carbs, fat and protein all together in a traditional westernised meal, you will of course shuttle some nutrients and amino acids to muscles but generally just cause a rapid release of insulin leading to great fat storage.

Before you make a rash decision and try to eliminate insulin, you must know that insulin is very anabolic. Insulin can be utilised as apposed to abused, and can become one of your most powerful hormones in the endeavour to create a superior athletic physique. Insulin itself is responsible for carb and amino acid delivery to the muscles for recovery and growth. This is why your body is primed to release insulin whenever you digest protein. Bottom line - you need insulin, but you need to control it. And when you eat to promote insulin surges, you've got to be sure that you have the ideal profile of macronutrients in your blood to ensure that this insulin surge leads to muscle gain and not fat gain. This is where meal combinations come into play.

It's well known in the research world that eating carbs and protein together also creates a synergistic insulin release, as discussed above. In the scenario of post workout nutrition and the attempt to harness the anabolic properties of this hormone, that insulin release is just what you want. By having a few meals per day that cause high blood levels of insulin, carbs, and amino acids (as long you don't have chronic high blood levels of insulin all day long), the body tends to become very anabolic, taking up all those carbs and amino acids into the muscle cells for protein and glycogen synthesis. And since there's no excess fat for the fat cells, fat gain is minimized.

Many people will argue that elevation of insulin levels this high is going to prevent the breakdown of fats (lipolysis) even if it does minimise fat storage. This is indeed true. But what people must also understand is that most meals (unless they are of very certain types of protein only) are going to raise insulin levels so that lipolysis is prevented anyway. So protein and carbs raise your insulin past this level, and you should be consuming protein every few hours. A vital lesson.

Taking a step back, the purpose of protein plus fat meals is to provide energy and amino acids without causing large, lipolysis-preventing insulin spikes. In addition, after fatty meals that contain no carbs, the body oxidizes less carbs (more carbs are stored and retained in the muscle as glycogen) and burns more fat for energy. So basically you'll be burning fat for energy and storing carbs in the muscle after such meals.

So in terms of respecting your insulin levels to build muscle and burn fat you should be combining protein and carbs with no fat, especially after training and maybe occassionally throughout the early portion of the day, and eating solely protein and fats at all other times to maintain steady and slow streams of amino acids to be shuttled by moderate insulin release to your muscle cells.


Lets face it, we are surrounded by protein rich foods everyday. From dairy proteins, to meat, to vegetable sourced proteins such as nuts and seeds and pulses and grains. Are they all equal in quality to each other for building muscle tissue. Well, the answer is of course, no. One of the key questions with regard to the quality of proteins is whether the quality of vegetable proteins are as high as that from meats and dairy foods.

Using the old method of Protein Equivalency Ratios (PER) vegetable proteins do not score very high. But, it is now known that the PER standard bears little relation to human needs for amino acids or to the bioavailability of proteins. A new method of measuring protein quality is therefore now used, known as the Protein Digestibility Corrected Amino Acid Score (PDCAAS).

With the PDCAAS, the quality of food protein is assessed by its content of essential amino acids, the ratios of these amino acids to each other and their bioavailabilty. For example, best quality soy protein is given a PDCAAS of 1.0 which means it is a high quality protein complete in all the essential amino acids.

So what does all of this mean? Well basically, human muscle tissue is not the same as tuna fish muscle, or baboon muscle tissue. This is what makes each animal different in it's dietary requirements for proteins. It was discovered years ago that amino acids are different in quantity to each other and in respect to each other. The structure of amino acids and order of them varies so much from protein to protein. This means that tuna fish protein is an excellent choice for tuna fish to eat to build tuna fish muscle. And so logically speaking, human muscle tissue is ideal for building human muscle tissue with. The amino acids are in the perfect ratio and quantity. Of course we cannot eat masses of human muscle tissue for our needs and so we must assess the quality and availability of existing proteins and their uses for us.

This makes any of those animal and rat studies on proteins virtually irrelevant when it comes to measuring the quality of proteins for humans.

Whey and Casein And Their Biological Value's
All proteins are made up from different ratios of amino acids, the make-up of which determine the proteins Biological Value. This is the measurement of protein quality expressing the rate of efficiency with which protein is used for growth.

Of the whole foods, Egg contains the highest quality food protein known. It is so nearly perfect, in fact, that egg protein is often the standard by which all other proteins are judged. Based on the essential amino acids it provides, egg protein is second only to mother's milk for human nutrition.

On a scale with 100 representing top efficiency, these are the biological values of proteins in several foods:
Protein Ratings

Eggs (whole) 100
Eggs (whites) 88
Chicken / Turkey 79
Fish 70
Lean Beef 69
Cow's Milk 60
Unpolished Rice 59
Brown Rice 57
White Rice 56
Peanuts 55
Peas 55

As far as sources of protein created in the lab are concerned, here is a short list of some protein sources you can find in supplements common today. See how they compare to the natural sources listed above:

Whey Protein Isolate 159
Whey Protein Concentrate 104
Casein 77
Soy 74

As you see, the BV of whey is very very high, but this is wasted if it cannot be absorbed and used by the body in the short period it is in your system. Now take a look at the BV value of casein which is lower than that of Whey. What is unique about casein protein however is the slow digestion rate. Studies that compare whey and casein administered in the workout period inevitably find that whey protein exerts a far stronger anabolic response in this case. However, when casein is administered at other periods the strength gains are twice of those seen with whey. This is because while whey stimulates protein synthesis much more than casein in the short term, casein causes a sustained release of amino acids, preventing muscle breakdown for a more extended period of time . This makes whey the protein of choice for the workout period, with casein preferably added at other times, especially before periods of fasting (such as sleep).

A Word On Soya
Men should avoid soya protein at all costs. This is because there are elements of soya protein, soy isoflavones, that are estrogenic. This lowers your testosterone levels to a point where it can even influence sperm production and efficiency. This can also lead to accumulations of bodyfat and estrogenic side effects in sensitive individuals.

Women should actually seek to increase the levels of soya protein in their diet as it has a very beneficial effect on hormones, recovery rate and bodyfat.

The main sources of protein are meats, fish, milk, eggs, beans, and grains. Egg whites, tuna, turkey, trout, and chicken are among the best.



Milk contains two protein sources, casein and whey. In cows milk, these are in the ratio of 80% casein and 20% whey, whereas in human maternal milk, these ratios are reversed, with most of the protein coming from whey. The ratios are actually about 60:40 whey to casein in human maternal milk. We are going to look in depth at both whey proteins and the various forms that this appears in and the ever increasing in popularity, casein protein, in particular micellar casein.

So what is whey protein and how can it benefit me?

Whey is a component of milk. Whey proteins have nutritional properties that extend well beyond protein quality as measured by amino acid composition. As far back as the 17th century, it was recognised that, those who consumed whey, generally fared better than those who did not during this era of disease and infestation. Recent research gives new hope to those suffering from conditions such as burns, injury-induced muscular wasting and various catabolic states. So we know from whey research that it is good to heal damaged and repairing muscles. Then the benefits for creating and building stronger healthier bodies is guaranteed.

However, the medical world has nothing new to concede about whey's immunity benefits - the existing scientific research has made this a well-documented fact. Without a doubt, our future health lies with preventative medicine and materials such as whey and colostrum are likely to play a key role.

The importance of using the correct processing method cannot be overstated, for without this most of the properties may be rendered completely inert. There are a number of methods used to manufacture whey, and you may see these advertised on the side of protein powders; eg. Ion-exchange, cross flow microfiltration, hydrolysis etc. These are, however, no longer valid descriptions for labeling supplements.

UK labeling laws require that the whey content in protein powders be classed as either whey concentrate or whey isolate. Concentrates will contain protein solids from 30-80%, whilst isolate will be around 90%.

In short, the biological activity of whey depends on the level of denaturation suffered during its production process and it is entirely unrelated to its nutritional quality. So be sure to stick with reputable manufacturers and never buy your whey because it's going cheap - if that's the case then corners have probably been cut. The immuno-supportive activity can include the following:

Increased resistance to carcinogens
Increased longevity
Increased immunity
So we know that whey protein is good for the human body. Whey protein is a highly nutritional, immune supporting protein source. You can learn more about the immune supporting effects of whey protein below. Scoring systems that compare textbook profiles of protein sources consistently score whey protein very high. However, it is important to keep in mind that most commercially available whey proteins fall well short of the textbook profiles that score so high. You have heard it before, Not All Whey Proteins Are created Equal! Why is this? Well, essentially the manufacturing process from which your whey protein is derived from differs greatly. Below is a brief summary of how whey is extracted from each of the manufacturing methods. Generally the processes all have a common start, that is from sweet dairy whey.

Manufacturing Whey Protein
Milk is treated with an enzyme called rennet, which causes the milk to curdle. The surface is skimmed off and when processed, becomes cheese. Whats left behind is called sweet dairy whey and is a 30% concentrate whey protein. At this point it is high in fat and high in lactose (a simple sugar present in milk that causes an allergic reaction in a large percentage of the adult population).

The most bioactive (anabolic) parts of whey proteins are also the most easily destroyed during whey protein manufacture. Almost every commercially available whey protein (including those in your favorite supplement powder) has been heavily processed, including heat treatments and pH changes.

Both heat and pH adjustments will destroy the fragile, bioactive components of whey protein as well as degrade some of the more important amino acids that are claimed in support of whey proteins. Immunoglobulins and BSA start to denature (degrade) at temperatures as low as 140 degrees F. Most commercial whey proteins have been pasteurized at 170 degrees F. Now you can start to see why some whey is cheap and some whey is highly expensive.

The standard whey protein has undergone much denaturation (degradation) and does not compare to the textbook profiles or scores for whey protein. Don’t be fooled by whey protein supplement labels that claim specific protein fraction or amino acid compositions! The truth is that whey protein processing destroys portions of these protein fractions and amino acids! A standard whey protein can vary by as much as 15% in amino acid content from production batch to production batch and the protein fraction composition varies widely throughout the industry, depending on the manufacturing technique employed during production.

Most commercially available whey proteins are significantly different from whey protein textbook descriptions in important nutritional properties. Given the differences between textbook compositions and real world whey proteins, it is not valid science to make claims for real world whey proteins based on textbook studies. It is also important to keep in mind that while whey proteins have been shown to be anabolic, due to their immuno-supportive, bactericidal, and antiviral functions, a recent study concluded that whey proteins have no effect on protein breakdown in the body (no anti-catabolic function). While anabolic performance is important, you need your protein diet to have some anti-catabolic function for maximum lean tissue growth.

So what are the manufacturing methods?

Ion-exchange whey is manufactured by adding the sweet dairy whey to an electrically charged resin bath. The negatively charged protein fractions are attracted to the positively charged resin particles whilst the water, fats and lactose are left behind. A weak solution of hydrochloric acid (similar to the levels found in the stomach) is added to the resin and protein to dissolve the bond. A sodium or potassium salt is added at this point to get rid of the bitter taste caused by the acid. The whey protein solution is then dried using a cold spray dry technique, so as not to damage the protein. Typically the whey is 80-90% concentrate at this point.

Cross Flow Microfiltration can be used to manufacture whey both from whole milk or sweet dairy whey. Typically, milk is spun at high speeds in large vats to cause the milk to curdle. The fat is removed, leaving skimmed milk. A weak acid is then added to cause the casein to curdle. Once this is removed you are left with a low percentage protein whey liquid. A series of filters are used (each filter allowing through different sized particles) to firstly remove the majority of the lactose and then to remove minerals and finally the last of the fat and lactose. Finally the liquid is then dried using a cold spray dry technique, leaving a high quality whey of around 90% protein content.

Whey Hydrolysis is a method used on a whey isolate to deliver a protein containing only di-peptides and tri-peptides. The whey is treated with an enzyme that breaks down the whey proteins into di, tr and poli-peptides. The solution is then filtered to remove the poli-peptides (the larger protein molecules) and then treated to remove the acidic taste. Hydrolysis never leaves a pleasant tasting protein, and is generally only added to protein mixes to increase the overall quality of the product.

Each of these processes have pros and cons beyond the basic levels of protein. Within milk protein there are five protein fractions. Whey concentrate, because it retains more of the fat, is often higher than whey concentrate in some of these fractions, whilst CFM is often higher in protein percentage wise, is usually lower in Beta-Lactoglobulin than an ion-exchange whey (BLG is an important growth factor).

So What Are Growth Factors and What Do They Mean To Me?
When looking at the growth-promoting effects of whey, scientists identified its growth factors as being the primary agents responsible for this action. Research has shown that these growth factors also form an integral part of the powerful immuno-supportive properties of whey. It is known that growth factors such as IGF-1 help control infection and stimulate healing and production of immune cells. However, there are other constituents of whey that also contribute to its impressive list of benefits, its bioactive fractions (peptides). These fractions have multiple functions to perform within an organism after ingestion.

Beta-lactoglobulin - the most predominant component in bovine milk, this is the cause of many allergic reactions experienced in humans. A component that does not occur in human maternal milk, it may account for up to 75 per cent of the components present in ion-exchange whey products. This high percentage content would indicate that more important fractions have been replaced by its respective processing technique.

Alpha-lactalbumin - the main component in human milk, it is therefore considered by some to be the most nutritive and easily digestible fraction for humans. Bovine milk has a low percentage content of this and this has presented a long-standing problem for the infant formula market. Some companies have now turned their attention to the development of an alpha-lactalbumin based formula, thereby avoiding many of the deleterious side effects caused by beta-lactoglobulin in some infants.

Lactoperoxidase - this is another highly bioactive component that has also been demonstrated to boost immune function. It has been used in dental formulas to inhibit cavities.

Glycomacropeptides (GMPs) - these are a good example of the finely balanced synergy that is unique to the maternal milk formulas of each species. GMPs are known to modulate digestion by initiating the release of the hormone cholecsystokinin (CKK) after the ingestion of fat or protein. This then aids the passage of bioactive fractions such as lactoferrin and lactoperoxidase into those areas of the intestinal tract where they can impart most benefit. This action may be kept in check by the opiate-like peptides known as casomorphins, found in the micellar casein of portion of maternal milk. Basically, their job is to slow things down where necessary, making sure that nutrients do not pass through the system unabsorbed. Both lactoferrin and GMPs offer further protection by promoting the growth of protective probiotic bacteria in the large intestine.

Immunoglobulins - asantibodies, they have quite a wide range of immuno-supportive functions. IgG is perhaps the most specific to human immune function, along with IgA, it helps to neutralise toxins and other unwanted invaders in the circulatory and lymphatic system. IgD and IgE are highly antiviral. IgM is known to fight bacteria.

Bovine Serum Albumin (BSA) a glutathione precursor, BSA has powerful antioxidant and tumour prevention properties.
Lysozyme - this is known to destroy bacteria and viruses.Aside from the growth factors and fractions found in whey, there are several other ingredients that are known to have some effect on immune function. These include the following:
Interleukins - reduce inflammation and boost immune function.
Leukocytes - stimulate production of interferon.
Cytokines - stimulate and regulate immune response, communications and tumour regression.
Sulphur amino acids - regulate body cell mass and provide antioxidant properties.
Orotic acid - supports red cell integrity.
Hydrogenperoxide producing enzymes - attack bacteria.
Proline-Rich Polypeptide (PRP) - boosts the under active immune system and restores thymus gland function (produces T-cells that fight viruses and antigens).PRP can help balance overactive immune systems, present with autoimmune diseases, where the body actually attacks itself. This means that undenatured whey may be helpful with conditions such as:

Rheumatoid arthritis
Multiple sclerosis
Chronic fatigue syndrome
All forms of whey protein will spike your insulin levels and in particular hydrolysates.

Caseins and Micellar Casein
Casein is the other constituent of milk, as apposed to whey protein. Casein is generally considered milk protein, because in cows milk the casein portion takes up a good 80% of the formula.

Casein is hardly a poor quality protein. For many years, casein has been considered the standard reference protein by which all other protein qualities are measured and compared. It is now known that caseing has had a bad wrap. And there is more than just ignorance behind this thinking. When it comes to money, there is much mis-information leaked into the world. In order to sell 100% whey protein powders, some unscrupulous companies have tried to convince consumers that casein is of poor quality … even going so far as to hint that casein may be dangerous. This is of course unfounded and indeed, wrong.

Casein is GRAS (generally regarded as safe) listed by the US FDA and is one of the few food components to achieve that status. This is a fundamental point that you need to consider at all times. Casein contains many bioactive peptide sequences that provide important benefits for the body. In fact, the highly regarded peptide, glycomacropeptide (described above), which many people believe to be a whey protein, is, in reality, a peptide chain from casein that finds its way into cheese whey protein as a byproduct of cheese manufacture. So casein has a very important factor that is ideal for your muscle building desires.

As it has been stated above and you can work out for yourself, human maternal milk contains 40% to 55% casein. There is of course a reason behind this in nature.

Micellar Casein
Micellar casein differs from "caseinate" in that micellar casein is not denatured and is the naturally occurring form of casein. A recent study involving 16 healthy, well fed individuals compared the effects of whey protein to micellar casein on whole body protein utilization.

So we know how good whey protein is as an anabolic protein and immune supporting health boosting choice. So why don't we consume whey protein the whole time. Well, there are a number of problems with this. One of the major points that you need to get a grasp of when it comes to protein, is that we don't need to focus on only anabolic (muscle growth) effects, but rather both anabolic and anti-catabolic (preventing muscle wastage and breakdown) actions of our diet. And that is where Micellar Casein rules supreme.

Several studies have demonstrated that whey protein is a fast dietary protein as discussed. With a fast dietary protein, all that happens is that every time it is consumed, the amino acids are released quickly into the bloodstream in a large grouping. It is the fast, excessive release of amino acids that causes the body to send a significant portion of the aminos to the liver for oxidation. In other words they are wasted and useless. This also causes aging effects upon the body through oxidative damage.

These same studies have shown that as each new batch of amino acids is released into the bloodstream in a large group so often, a lower percentage is used for lean tissue growth support and a higher percentage is oxidized in the liver. Even worse, these percentages become more skewed on each successive protein ingestion, resulting in a reduction in the efficiency of protein utilization. Why waste your money consuming whey protein more often when the benefits would be doubtful at best?

Secondly, the groundbreaking study comparing micellar casein to whey protein concluded that micellar casein significantly inhibited protein breakdown and that whey protein had no effect on protein breakdown. It did not say that whey protein had a slight effect or somewhat of an effect on protein breakdown.

The study concluded that whey protein had absolutely zero effect on protein breakdown. In other words, you can eat all of the whey protein you want as often as you desire, but it will not have an anti-catabolic effect. There are initially high anabolic properties, but these rapidly diminish if you consume whey all of the time. And there are absolutely no anti-wasting effects of the protein. This means whey is ideal and perfect for scenarios when you need to replenish amino acids and fast, such as immediately upon waking, and immediately post training. At all other times you are looking to consume highly anti-catabolic and anabolic proteins such as micellar casein.

The Science Of Muscle Building
Basically, through the sound, scientific principles of "Fast and Slow Dietary Proteins", research has concluded that no single source protein supplement is the ideal method to grow new muscle tissue (anabolism) while, at the same time, preventing muscle tissue breakdown in the body (catabolism).

If one consumes only Fast proteins such as whey, the amino acids enter the bloodstream too fast, stimulating protein synthesis, but also causing the body to divert a significant percentage of the amino acids to the liver, where they are oxidized and used for energy instead of for promoting lean tissue growth.

If you combine quality proteins with differing digestion rates in the correct ratios, you can eliminate this uneconomical scenario by creating a sustained release effect. This is what is truly going to place your body into a highly anabolic and anti-cataboic state, primed for muscular recovery and growth. We have to recommend that one combins different types of Fast proteins, in the form of whey protein concentrate, isolate, hydrolysate, and egg white, with a Slow protein source, micellar casein. With this combination of Fast and Slow Dietary Proteins you are essentially trying to ensure that precise amounts of amino acids will be released into the system at exactly the right times, so as to maintain a constant positive nitrogen balance and an ideal anabolic / anti-catabolic environment for muscle tissue development.

So for anybody who is serious about making lean tissue gains, a mixture of Fast and Slow Dietary Proteins is the only logical and scientific option to consider. Anything else is substandard and that doesn't mean that it does not work, it merely means that it is not the most optimal way we know, nor, is it the best option available to you in the real world.

Groundbreaking studies have come to the following conclusions:
• Micellar casein significantly inhibited protein breakdown (anti-catabolic function) over seven hours after ingestion. Whey protein had no effect on protein breakdown.
• Micellar casein moderately stimulated protein synthesis (anabolic function).
• Less amino acids were wasted through liver oxidation after micellar casein ingestion than after whey protein ingestion.
• Micellar casein resulted in better overall nitrogen retention in the body compared to whey protein! Micellar casein is anti-catabolic and is an important component in the sustained release of amino acids into the system for maximizing anabolism.

Whey and Casein And Their Biological Value's
All proteins are made up from different ratios of amino acids, the make-up of which determine the proteins Biological Value. This is the measurement of protein quality expressing the rate of efficiency with which protein is used for growth.

Of the whole foods, Egg contains the highest quality food protein known. It is so nearly perfect, in fact, that egg protein is often the standard by which all other proteins are judged. Based on the essential amino acids it provides, egg protein is second only to mother's milk for human nutrition.

On a scale with 100 representing top efficiency, these are the biological values of proteins in several foods:
Protein Ratings

Eggs (whole) 100
Eggs (whites) 88
Chicken / Turkey 79
Fish 70
Lean Beef 69
Cow's Milk 60
Unpolished Rice 59
Brown Rice 57
White Rice 56
Peanuts 55
Peas 55

As far as sources of protein created in the lab are concerned, here is a short list of some protein sources you can find in supplements common today. See how they compare to the natural sources listed above:

Whey Protein Isolate 159
Whey Protein Concentrate 104
Casein 77
Soy 74

As you see, the BV of whey is very very high, but this is wasted if it cannot be absorbed and used by the body in the short period it is in your system. Now take a look at the BV value of casein which is lower than that of Whey. What is unique about casein protein however is the slow digestion rate. Studies that compare whey and casein administered in the workout period inevitably find that whey protein exerts a far stronger anabolic response in this case. However, when casein is administered at other periods the strength gains are twice of those seen with whey. This is because while whey stimulates protein synthesis much more than casein in the short term, casein causes a sustained release of amino acids, preventing muscle breakdown for a more extended period of time . This makes whey the protein of choice for the workout period, with casein preferably added at other times, especially before periods of fasting (such as sleep).


This has got to be the longest running debate in the whole training and nutritional institutions ever. Just how much protein does a person need. Of course the answer lies in your training level, your type of training, your genetic make-up and the amount, if any, of chemical assistance you may be using in your athletic goals. Study after study show varying results. However one must realise that study after study uses different dietary and training principles and clean and drug using athletes and non athletes (sedentary folk). Thankfully some evidence corresponds with real life logic.

The long-standing belief is that you require about 0.75gm of protein per kilo of bodyweight, which may well be adequate for sedentary people. However, studies on people performing even moderate levels of exercise showed that this was inadequate. These studies were based on measuring nitrogen retention, positive balances showing that adequate protein is being eaten, negative balances showing that muscle protein is being broken down to meet the body's needs.

It is now commonly accepted that protein levels need to be in line with activity levels. The harder and more intense you train, demanding more muscle growth from your body, the more protein you generally require. Or whatever other stimulus may indeed be causing a required higher level of protein, such as performance enhancing drugs.

Studies on strength athletes showed that protein levels of 3-4 gm per kilo of bodyweight gave significant strength and size increases.

It must be stressed that it is training effort that determines protein needs. Eating more protein will not create more muscle, or increase strength, unless the body's demand for protein increases as a direct result of training effort.

With this in mind most sports nutritionists would recommend protein levels around a gm per pound of bodyweight daily for people training to build muscle size and strength. This should be split into six evenly sized meals. For example a 180lb man requires 180 gm's of protein, which gives him 6 meals of around 30gms of protein.

To minimise saturated fats, whilst maximising protein quality, you should select from whey, egg whites, turkey, tuna, chicken, trout, and most white fish. Beans, grains and pulses also contain high protein to fat ratios. Sports nutrition protein drinks, especially those based on whey and other milk proteins, should also play a significant part especially in the post workout period.

Don't forget, that protein quantity is not the only issue. We must consider protein quality too. There is no use in eating 180 grams of useless and poor quality vegetable proteins that are poorly digested and assimilated into muscle. That would be very different from consuming 180 grams of micellar casein and ion exchanged whey proteins. It is in fact a world of a difference. So remember, the lower the quality of your protein, the more you are going to have to eat and combine with varying proteins to obtain a reasonable amino acid score. With the increase in quantity you run the risk of experiencing problems and stress upon your system. So logically thinking, you want to improve the quality of your proteins and eat the correct amount.

Recent studies with many of the pharmaceutical assisted athletes around the globe show that when using anabolic agents both the quantity and quality of the proteins should increase and dramatically so. There have been studies showing improvements in muscle size and strength with protein increases upto 3 or even 4 grams per lb of bodyweight (preferably lean body weight - don't calculate your fat mass). The missing element here, is whether the controlling factor is the drugs, the protein or of course a combination of the two factors together.

It is also known that the human body can only efficiently digest a certain quantity of protein at any one meal. There is no use in trying to force feed 100 grams of protein down your neck in one sitting as most of this will not be digested efficiently. It is better to almost drip feed amino acids into your system by consuming smaller more regular meals throughout the day. Nobody is quite sure how much protein the human body can absorb in one sitting, however, the professional community generally agree that you are adapting all of the time, and the more protein you eat on a regular basis, the more you will digest and absorb. This is also correlates with a supply on demand basis. If your body is stimulated to require higher demands of protein it will become more efficient at absorbing your dietary proteins. However, there are likely to be some undetermined limits.

Below is a table outlining the protein quantities found in many popular whole foods:-

Per 100g Uncooked Weight





Chicken Breast





Rump Steak





Cod Fillet





Skimmed Milk





Turkey Breast





Egg Whites





Whole Eggs





Tuna fish in Brine





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