INTRODUCTION

Many years ago when I re-made Ultra Energy into SPIZ, I selected a “hydrolyzed” whey protein as my protein source because whey is the highest quality dietary protein based on its excellent amino acid profile and easy digestibility.

Whey protein also contains the sulfur containing amino acid cysteine, which is needed to synthesize the body’s number one intracellular antioxidant, glutathione. Glutathione is a potent antioxidant that defends the body against free radical damage and is necessary for lymphocyte proliferation and immune function. Animal studies suggest that whey protein may reduce the risk of cancer due to its glutathione stimulating effect. In fact, one of the first whey protein products to come on the market in the 1990’s was “ImuPlus”, a non-denatured whey protein isolate that was/is promoted to cancer and AIDS patients specifically for its glutathione stimulating effects. Due to its antioxidant effects, whey protein is being researched for its ability to prevent degenerative diseases like cancer, Parkinson’s and heart disease. There are also indications that glutathione can alter gene expression in a way that promotes muscle growth.

A very interesting study compared supplementation of 20 grams of whey protein concentrate per day with 20 grams of casein protein per day for 3 months. The results showed that supplementation with whey significantly increases lymphocyte glutathione levels by over 35% and also improved peak power and 30 second maximal work capacity. There were no changes in the casein group. The whey group also had a decrease in bodyfat percentage while maintaining their bodyweight, meaning they were gaining muscle mass at the same time! These are the kind of positive changes typically seen with testosterone replacement therapy!

In the ensuing years research into whey protein has continued to strengthen my initial impression that whey is simply the best protein source to improve performance in athletes of all types. It can help build and maintain muscle mass and strengthen as well as assist those with catabolic illnesses trying to prevent loss of lean body mass, improve immune function, detoxify and improve antioxidant function. One-sub-fraction of whey has been found to stop bone catabolism and may reverse osteoporosis. This product is called “milk basic protein” and consists of 54% lactoferrin and 41% lactoperixidase and a few other proteins and is approved in Japan as a “functional food” ingredient in tofu and natto. Adding whey to fermented soy…..Hmmm! That should give you a bit of insight into a comparison of whey protein to soy protein coming later on in this review.

Depending on the type of whey protein selected, any or all of these health and/or exercise performance objectives can be achieved. This “primer” will review what is known about whey protein, the importance of its source and processing, how it improves performance and immune function and the differences between whey concentrates, isolates and hydrolysates . Proof of its superiority over casein or soy protein will also be presented.

TYPES OF WHEY PROTEIN

Whey protein is one of three types of proteins found in dairy, the other being casein and “milk basic protein” which is actually a sub-fraction of whey. Whey proteins are being studied for their ability to have a positive effect on nitrogen balance, which is the chemical element that makes protein different from carbohydrates or fatty acids which contain carbon, oxygen and hydrogen only. Certain whey proteins can have profound effects on immune function and can reduce inflammation in the body. Although milk allergy and/or lactose intolerance is fairly common, one form of whey is essentially free of both these issues and can be used by anyone without risk of GI tract distress or allergic response.z

Whey is a byproduct of cheese manufacturing. The fat (“curds”) are filtered from the milk as is much of the other milk protein, casein. The remaining product is a whey protein “concentrate” which also contains a 5% solution of lactose in water, some fats, minerals and different types of lactalbumin. If not heated (pasteurized), whey concentrate is “undenatured”, and is in its most biologically active, immune stimulating form and is 40 – 85% protein by weight. For those who are lactose intolerant, this form of whey is more likely to provoke a GI tract reaction. Likewise those whose who are allergic to milk will have an allergic response to whey concentrates due to the many intact protein structures. Whey concentrate contains a mixture of beta-lactoglobulin (65%), alpha-lactoglobulin (25%) serum albumin (8%) and immunoglobulins such as lactoferrin, lactoperoxidase and glycomacropeptide which are all very beneficial to the immune system.

Recently research published in the journal PLoS One found that breast-fed children are more protected against cancer than formula-fed children. The alpha-lactoglobulin referred to above combines with oleic acid which is found in babies stomachs. The combined protein is called “Human Alpha-lactalbumin Made LEthal to Tumor cells“ (HAMLET) and can effectively kill cancer cells for years to come. HAMLET can also trigger cancer cells apoptosis pathways, which is programmed cancer cell death. A pilot study of bladder cancer patients who had a HAMLET solution injected via a catheter found it killed cancer cells and shrunk tumors within 5 days.

WHEY VS CASEIN – WHEY IS WAY BETTER!

Interestingly, human mother’s milk is 60% whey and 40% casein. Cow’s milk is 20% whey and 80% casein. This ratio difference suggests humans do better on whey protein than casein protein, which is problematic for another reason. There are two types of casein that differ by one amino acid. Milk from Bos Taurus subspecies of cows which includes Holsteins, Ayshsires and Frisians produce A1 beta casein while milk from humans, goats and Guernsey cows contains A2 beta casein. The vast majority of cows in the Western Hemisphere produce A1 beta casein. A1 beta casein is highly inflammatory and has been shown to provoke an autoimmune response. It has been found that many cases of Type I childhood onset diabetes is linked to cow’s milk consumption containing A1 beta casein, which sets off an autoimmune response that destroys the beta cells in the pancreas that make insulin.

A1 beta casein results from a genetic variation at position 67 of the casein 209 long amino acid structure. A1 beta casein has the amino acid histidine at this point while A2 beta casein has the amino acid proline instead. This results in a 7 amino acid peptide called “casomorphin-7” (BCM-7) being cleaved off the A1 casein, a process that does not occur with A2 beta casein. BCM-7 is an opioid resistant to degradation and creates rampant oxidative stress in the gut and blood stream as well as a strong immune response. BCM-7 can cause “leaky gut syndrome” with digestive disorders and is itself absorbed and circulated in the blood. It can cross the blood brain barrier causing a number of neurodegenerative changes. BCM-7 injected into rats has been shown to cause autistic and schizophrenic type behavioral changes. It can cause reduced GI tract motility and constipation and is most damaging in infants who naturally have increased intestinal permeability. Giving cow’s milk containing A1 beta casein to infants under age 2 would not be a good idea for these reasons alone. However, the story of casein gets worse!

Studies of A1 beta casein consumption and the incidence of coronary heart disease in populations of many countries around the world has shown a strong correlation between the two. The reported correlation coefficient between the two is 0.76, which is as high as the correlation coefficient between smoking with lung cancer. Now correlation does not prove causation, however studies of dietary intake of A2 beta casein and childhood diabetes and adult onset coronary artery disease shows NO correlation. By the way, research has found that cheese, yogurt and fermented milk products like kefir from A1 beta casein containing breeds produce around the same amount of BCM-7 as regular milk. The graph below illustrates the dietary A1 beta casein/heart disease link:

Clearly whey protein is superior in every important measurement of protein quality and utilization relative to soy. So I hope this Whey Protein Primer has given you an education and some insights into the differing kinds of whey and what whey product would be best for your particular application whether it be exercise performance, recovery, muscle or strength building or just for health purposes. Feel free to contact me if you have any questions.

Randy Ice PT, CCS

It is theorized that BCM-7 oxidizes LDL cholesterol (OxLDL) which accumulates in the arterial wall and is the mechanism of how A1 beta casein contributes to coronary atherosclerosis.

Casein is also a much slower absorbing protein in the intestinal tract relative to all forms of whey, hence is less desirable from the standpoint of getting branched chain amino acids to the muscle cells as quickly as possible during or after exercise, even if one had access to A2 beta casein which in the USA is very difficult if not impossible.

I recently had a discussion with the owner of the Organic Pastures dairy in Fresno, California that is the only raw, unpasteurized milk producer in this state. In discussing the A1/A2 beta casein controversy, his feeling was that the science behind it is not settled, and the real issue for milk (and therefore whey) producing cows is whether they are grass fed or not. Grass fed cows lead to far healthier milk, and therefore a better protein content. The SPIZ whey protein does come from grass fed cows in New Zealand, which is another reason is it superior.

Whey protein also contains the sulfur containing amino acid cysteine, which is needed to synthesize the body’s number one intracellular antioxidant, glutathione. Glutathione is a potent antioxidant that defends the body against free radical damage and is necessary for lymphocyte proliferation and immune function. Animal studies suggest that whey protein may reduce the risk of cancer due to its glutathione stimulating effect. In fact, one of the first whey protein products to come on the market in the 1990’s was “ImuPlus”, a non-denatured whey protein isolate that was/is promoted to cancer and AIDS patients specifically for its glutathione stimulating effects. Due to its antioxidant effects, whey protein is being researched for its ability to prevent degenerative diseases like cancer, Parkinson’s and heart disease. There are also indications that glutathione can alter gene expression in a way that promotes muscle growth.

A very interesting study compared supplementation of 20 grams of whey protein concentrate per day with 20 grams of casein protein per day for 3 months. The results showed that supplementation with whey significantly increases lymphocyte glutathione levels by over 35% and also improved peak power and 30 second maximal work capacity. There were no changes in the casein group. The whey group also had a decrease in bodyfat percentage while maintaining their bodyweight, meaning they were gaining muscle mass at the same time! These are the kind of positive changes typically seen with testosterone replacement therapy!

WHEY PROTEIN ISOLATES

When whey concentrates are treated through the another process called “ion exchange” which denatures the protein and immunoglobulins with heat, and/or microfiltration the resulting end product is a whey isolate that is mostly, but not completely free of lactose. The ion exchange process literally wipes out all the valuable and health promoting sub-fraction peptides except beta lactoglobulin which is the most common milk protein allergen. Hence this would not be a good product to consume for those with milk allergy. Whey isolates contain 85 -90% protein that are absorbed faster than a whey concentrate. Like whey concentrates, they are mild to slightly milky in taste.

Whey is THE most abundant source of branched chain amino acids (BCAA’s) which are used to fuel working muscles and stimulate protein synthesis. The branched chain amino acids include leucine, valine, alanine and isoleucine, and have been also been found to inhibit the transport of heavy metals across the blood-brain barrier. In particular, the amino acid leucine plays a key role in initiating the transcription of protein synthesis. Adequate leucine intake is required to speed recovery and help with adaption to exercise. Since high intensity and/or prolonged aerobic exercise, or heavy weight training results in protein catabolism in the former and micro muscle tears in the latter, replenishing protein during and immediately after exercise is critical to a faster recovery process and maximizing training effects.

Another factor to remember is the contribution of protein to total energy expenditure in long distance sports such as cycling, running, swimming, triathlon and so forth, which has been measured at 5 to 15%. This can make the difference between winning and losing, or a good versus bad competitive performance if not addressed properly.

WHEY PROTEIN AS AN IMMUNE SYSTEM STIMULATOR

Whey protein also contains the sulfur containing amino acid cysteine, which is needed to synthesize the body’s number one intracellular antioxidant, glutathione. Glutathione is a potent antioxidant that defends the body against free radical damage and is necessary for lymphocyte proliferation and immune function. Animal studies suggest that whey protein may reduce the risk of cancer due to its glutathione stimulating effect. In fact, one of the first whey protein products to come on the market in the 1990’s was “ImuPlus”, a non-denatured whey protein isolate that was/is promoted to cancer and AIDS patients specifically for its glutathione stimulating effects. Due to its antioxidant effects, whey protein is being researched for its ability to prevent degenerative diseases like cancer, Parkinson’s and heart disease. There are also indications that glutathione can alter gene expression in a way that promotes muscle growth.

A very interesting study compared supplementation of 20 grams of whey protein concentrate per day with 20 grams of casein protein per day for 3 months. The results showed that supplementation with whey significantly increases lymphocyte glutathione levels by over 35% and also improved peak power and 30 second maximal work capacity. There were no changes in the casein group. The whey group also had a decrease in bodyfat percentage while maintaining their bodyweight, meaning they were gaining muscle mass at the same time! These are the kind of positive changes typically seen with testosterone replacement therapy!

WHEY PROTEIN, LEUCINE AND EXERCISE PERFORMANCE

Leucine is one of nine so called “essential amino acids” that can only be obtained through the diet. In one study of 26 untrained healthy men aged 20 – 36, half received 4000 mg of leucine and half a placebo. Twice weekly all subjects were supervised by professional trainers in 8 standard weight resistance training machines with strength testing before and after 12 weeks. At the end of the study the placebo group increased their maximum five repetition weight resistance ability by 31% while the leucine group increased by 41%, a 10% greater improvement with just leucine.

Another study of “elderly“ subjects, who have a more blunted response to protein than younger men examined a single leg resistance exercise protocol with either a whey or casein protein supplement immediately after exercise. Both drinks contained 20 grams of protein, however the whey protein had 2.6 grams of leucine while the casein protein had 1.6 grams of leucine. Muscle protein synthesis was calculated in the non-exercised leg and the exercised leg for 4 hours after exercise. Compared to casein, the whey group had 65% greater protein synthesis in the NON-exercised leg and 69% greater in the exercise leg. So whey is superior to casein in stimulating muscle protein synthesis even in “older” people/athletes!

WHEY PROTEIN HYDROLYSATES

If one takes a whey protein isolate and further treats it with heat and acid, the whey is degraded into much smaller peptide units called di and tripeptide amino acids. This process mimics our own digestion, hence the term “predigested” and the peptides are actually absorbed more rapidly than free form amino acids. Hydrolysis is an easy way to further purify the whey and remove the last vestiges of lactose, milk fats and immunoglobulins.

The resulting whey “hydrolysate” is 90 – 95% pure protein and is now in its most easily digestible form, and will be absorbed in the small intestine more quickly than whey concentrates or isolates. Those with lactose intolerance will have no issues with a hydrolyzed whey protein as virtually all the lactose is removed. Additionally those who have true milk allergy will be able to digest hydrolyzed whey protein without problem because the above mentioned beta lactoglobulin is hydrolyzed (digested) and is no longer present. The resulting whey hydrolysate is an extremely fine powder as it has been “pre-digested” into very small amino acid units. It has a fairly bland to not-so-great taste by itself.

THE BENEFITS OF CONSUMING A WHEY HYDROLYSATE DURING OR AFTER EXERCISE

Consumption of a whey protein hydrolsyate during and/or in post-exercise drinks is preferred because it results in a faster increase in blood amino acid concentrations AND a higher insulin response during a 1 – 2 hour period than does intact protein from any source. The simultaneous increase in blood amino acids and insulin significantly promotes muscle protein synthesis and inhibits muscle breakdown. Adding glucose to a whey protein hydrolysate results in a peak insulin level that is 2 – 4X HIGHER than after ingestion of milk with the same amount of glucose (15 grams in this study).

You may not realize it, but insulin is an anabolic hormone like testosterone that has muscle building effects. Hence spiking insulin briefly while ingesting BCAA’s during or after exercise has even more beneficial effects on hard working muscles. This can be either from an anabolic perspective with weight training (which is why competitive bodybuilders frequently inject insulin even though they are not diabetic) or in long distance endurance athletes trying to prevent muscle tissue catabolism (breakdown) that ultra long training and/or competition can create (think skinny and somewhat emaciated long distance runners).

Another practical advantage is that one can ingest a whey protein hydrolysate supplement immediately after exercise without becoming bloated and not excessively suppress appetite. So this means you can eat a meal sooner possibly increasing the post-exercise “anabolic window.”

WHEY PROTEIN PRODUCT CAVEATS

Beware that not all whey is the same. Consumer Reports tested several bodybuilding whey protein powders and found many were contaminated with heavy metals. Worse yet, the vast majority of whey protein powders you will find in health food stores are flavored with artificial sweetners such as aspartame, sucralose or Acesulfame K among others. These sweetners are not safe and are known to kill off healthy good bacteria in the colon in the case of sucralose, aka Splenda. Aspartame is a proven neurotoxin (think former Diet Coke addict, now Parkinson’s patient Michael J. Fox) that has more complaints for a wide variety of symptoms than any other nutritional product on file with the FDA, which they have chosen to ignore for over 25 years. The SPIZ whey protein available at www.SPIZ.net is a 100% hydrolyzed, unflavored whey protein with no artificial sweetners, flavoring agents, etc. and is the same hydrolyzed whey that is in SPIZ. I prefer to let you flavor it with whatever you wish as it can be mixed with anything. I mix it with fruit juice and ice cubes to make a healthy protein smoothy every morning for breakfast, and to drink right after my workouts.. Every serving has 65 grams of hydrolyzed whey di and tri-peptides with over 18.7 grams of BCAA’s, of which 7.8 grams is leucine. There is no lactose, no lactoglobulins (milk allergens), no heavy metals and no GMO’s (Genetically Modified Organism) in this product.

The highest quality whey protein comes from cows (or goats) fed pure 100% grass. Again, if you pick up a canister of whey protein in your local health food store, the type of feed and country of origin will more than likely not be specified. The number ONE country in the world for whey protein production and export is New Zealand, which takes great pains raising their cattle in pastures free of contaminants and fed grass or hay exclusively. When I developed SPIZ in the mid 1990’s, my research discovered these facts and I chose a hydrolyzed whey protein from New Zealand as its protein source. I knew it was the next best thing to putting pure amino acids in it (which is even more expensive as I used to do with SPIZ’s forerunner, Ultra Energy). I also knew it would be the protein that provides the most high quality BCAA’s and leucine as well as be digested and absorbed the most quickly. Time has proven that true as athlete after athlete in competition over the last 18 years has consumed 20 grams of the hydrolyzed whey protein in SPIZ every hour for hours and days on end in some cases.

RACE NUTRITION AND DIGESTION AS LIMITING FACTORS TO SUCCESSFUL ENDURANCE PERFORMANCE

Whey has also been found to increase liver and muscle glycogen stores compared to a casein-based diet containing the same amount of carbohydrates. Muscle glycogen is the primary carbohydrate fuel source needed to generate muscle contraction and energy. The more you can produce and store, the less likely you are to bonk. You must replace glucose continually during any sport lasting longer than 2.5 – 3 hours, and as it turns out, hydrolyzed whey protein assists with this process which is why carbohydrate/protein drinks have been proven superior to carb only products.

These are some of the multiple reasons why SPIZ energy drink/meal replacement gives superior performance by supplying key amino acids for generating energy production rapidly as well as protecting muscle protein stores from catabolism and also ensuring a faster recovery. No protein of any kind on the market is digested and absorbed more rapidly than hydrolyzed whey. This also accounts for the fact that virtually none of my customers has ever complained of a gastrointestinal issue or problem drinking SPIZ.

This is a BIG DEAL as a study published in the International Journal of Sports Physiology and Performance in 2011 examined factors related the successful performance of runners in the 2009 Western States 100 and Vermont Trail 100 mile run. Utilizing a post-race questionnaire, the researchers looked at a host of factors including training volume, maximum run volume, use of Non-Steroidal Anti-inflammatories, age, BMI, years of experience, number of 100 mile races completed and other factors, to determine what correlations could be made for those who finished versus those who had to drop out.

The number ONE cause of not finishing was “nausea and/or vomiting” as the culprit ( 23%), more than any other factor including runners citing injury, blisters, muscle cramps or exhaustion as the limiting factor ( 21.6%). In other words, more ultramarathon runners dropped out due to GI distress than injury, blisters, cramps and fatigue combined! Even 36% of the finishers reported nausea and/or vomiting affected their race performance, so many of them still did not have an optimum nutrition plan. This study strongly suggests that THE single most important factor in determining ultra distance success is nutritional intake during competition.

WHEY VS SOY – IT’S NO CONTEST!

Many health claims are purported for soy protein including “lowering cholesterol” (which is a worthless strategy for preventing or treating coronary disease) and relief of menopausal hot flashes (which is better accomplished with bioidentical estrogen and/or progesterone replacement). However, when it comes to building or maintaining muscle, then the protein with the largest concentration of usable amino acids in it is what you’re looking for. As we shall see, soy protein is quite inferior to whey protein in many different respects. Let’s start with Biological Value (BV).

BV measures the digestibility of a protein as well as its availability of the protein to the body. A BV of 100 was assigned to egg protein many years ago meaning that 100% of the egg protein was absorbed. Since then the evolution of protein powders have become better sources of protein than eggs, so some kinds of proteins have a score higher than 100. The higher the BV score the better the protein. When whey and soy proteins are compared using BV values a typical soy protein concentrate has a BV rating of about 74 while the typical whey protein has a BV of 104.

Another measure of a protein is called “Net Protein Utilization”, which is a measure of the amount of amino acids that are converted to protein in the body versus the amount of amino acids for the protein eaten. This measurement is also on a scale from 0 – 100% with 100% meaning all of the protein consumed is taken up in the body. A typical soy protein has a NPU of about 61% while a typical whey protein has a NPU of 92%. Protein Efficiency Ratio (PER) calculates the gain in body weight divided by the weight of the protein consume by infant laboratory rats. PER measures growth and the FDA uses the PER of a protein to derive the recommended daily allowance of protein that are found on all food labels. A PER of greater than 2.7 is classified as an “excellent” source of protein. Comparing whey to soy, PER scores reveals a rating of 3.2 for whey and 2.2 for soy.

Another way to look at the question of which protein is best is to look at its “Amino Acid Score (AAS).” In the AAS scale, a value greater than 1 demonstrates that the studied protein has higher levels of amino acids than the human body requires. In this respect whey as an AAS of 1.14 while the typical soy concentrate has an AAS of 0.99.

To evaluate protein quality based on the amino acid requirements of the human body, another measure is the “Protein Digestibility Corrected Amino Acid Score.” The FDA, World Health Organization and the Food and Agricultural Organization of the United Nations have all collectively decided to have the PDCAAS as the “best” method for determining protein quality. This score measures essential amino acids in a protein compared to a reference protein, which is what an everyday human body requires and is given a PDCAAS of 1.0. Unfortunately, as is typical of government bureaurats, this scoring method became politicized by “rounding down” any protein with a score of higher than 1.0. This lead to whey and soy proteins having identical 1.0 scores.

There are several other ways of looking at the question of which protein is better, whey or soy. The following table summarizes ALL of those methods and results:

Clearly whey protein is superior in every important measurement of protein quality and utilization relative to soy. So I hope this Whey Protein Primer has given you an education and some insights into the differing kinds of whey and what whey product would be best for your particular application whether it be exercise performance, recovery, muscle or strength building or just for health purposes. Feel free to contact me if you have any questions.

Randy Ice PT, CCS

Characteristics

Each SPIZ container has a 50cc scooper in it. You have the ability to experiment or change the concentration of SPIZ by using 2, 3, 4, or 5 scoops/22 or 28 ounce water bottle. This corresponds to 250, 375, 500 or 625 calories/bottle respectively when mixed with water.

SPIZ allows you the flexibility of finding out what caloric concentration works best for you based on your body size, metabolic rate, exercise intensity and temperature conditions. Smaller, lighter folks may require 250 or 375 calories every 60-90 minutes of exercise while large athletes will need 500 to 750 calories. Likewise, a more dilute solution can be used in hot water when hydration becomes more important.

SPIZ also eliminates the need for a different pre-workout or “recovery” product, as well as the need for gels, bars, and weak electrolyte sports drinks. Everything and more is included in SPIZ. Use SPIZ at full strength 1-1½ hours pre-workout or pre-competitionv, every 60-120 minutes at your pre-selected concentration during exercise and 1-2 full strength servings immediately after exercise.

For cancer and AIDS patients, 5 servings/day will provide 2500 calories of pre-digested food that is absorbed by the body with minimal metabolic effort and maximum nutritional delivery.

Characteristics

The Dangers Of Using Fructose Sweetener Article on the dangers of using high fructose corn sweetener in your diet.

How bad is fructose? 1,2 George A Bray

1. 1 From the Pennington Biomedical Research Center, Louisiana State University System, Baton Rouge, LA
2. Reprints not available. Address correspondence to GA Bray, Boyd Professor, Pennington Biomedical Research Center, LSU System, 6400 Perkins Road, Baton Rouge, LA 70808. E-mail: brayga@pbrc.edu.

See corresponding article on page 1174.

This issue of the Journal contains another disturbing article on the biology of fructose (1). Why is fructose of concern? First, it is sweeter than either glucose or sucrose. In fruit, it serves as a marker for foods that are nutritionally rich. However, in soft drinks and other “sweets,” fructose serves to reward sweet taste that provides “calories,” often without much else in the way of nutrition. Second, the intake of soft drinks containing high-fructose corn syrup (HFCS) or sucrose has risen in parallel with the epidemic of obesity, which suggests a relation (2). Third, the article in this issue of the Journal (1) and another article published elsewhere last year (3) implicate dietary fructose as a potential risk factor for cardiovascular disease.

The intake of dietary fructose has increased significantly from 1970 to 2000. There has been a 25% increase in available “added sugars” during this period (4). The Continuing Survey of Food Intake by Individuals from 1994 to 1996 showed that the average person had a daily added sugars intake of 79 g (equivalent to 316 kcal/d or 15% of energy intake), approximately half of which was fructose. More important, persons who are ranked in the top one-third of fructose consumers ingest 137 g added sugars/d, and those in the top 10% consume 178 g/d, with half of that amount being fructose. If there are health concerns with fructose, then this increased intake could aggravate those problems.

Before the European encounter with the New World 500 years ago and the development of the worldwide sugar industry, fructose in the human diet was limited to a few items. For example, honey, dates, raisins, molasses, and figs have a content of >10% of this sugar, whereas a fructose content of 5–10% by weight is found in grapes, raw apples, apple juice, persimmons, and blueberries. Milk, the main nourishment for infants, has essentially no fructose, and neither do most vegetables and meats, which indicates that human beings had little dietary exposure to fructose before the mass production of sugar.

Most fructose in the American diet comes not from fresh fruit, but from HFCS or sucrose (sugar) that is found in soft drinks and sweets, which typically have few other nutrients (2). Soft drink consumption, which provides most of this fructose, has increased dramatically in the past 6 decades, rising from a per-person consumption of 90 servings/y ({approx}2 servings/wk) in 1942 to that of 600 servings/y ({approx}2 servings/d) in 2000 (5). More than 50% of preschool children consume some calorie-sweetened beverages (6). Children of this age would not normally be exposed to fructose, let alone in these high amounts. Because both HFCS and sucrose are “delivery vehicles for fructose,” the load of fructose has increased in parallel with the use of sugar.

Fructose is an intermediary in the metabolism of glucose, but there is no biological need for dietary fructose. When ingested by itself, fructose is poorly absorbed from the gastrointestinal tract, and it is almost entirely cleared by the liver—the circulating concentration is {approx}0.01 mmol/L in peripheral blood, compared with 5.5 mmol/L for glucose.

Fructose differs in several ways from glucose, the other half of the sucrose (sugar) molecule (4). Fructose is absorbed from the gastrointestinal tract by a different mechanism than that for glucose. Glucose stimulates insulin release from the isolated pancreas, but fructose does not. Most cells have only low amounts of the glut-5 transporter, which transports fructose into cells. Fructose cannot enter most cells, because they lack glut-5, whereas glucose is transported into cells by glut-4, an insulin-dependent transport system. Finally, once inside the liver cell, fructose can enter the pathways that provide glycerol, the backbone for triacylglycerol. The growing dietary amount of fructose that is derived from sucrose or HFCS has raised questions about how children and adults respond to fructose alone or when it is accompanied by glucose. In one study, the consumption of high-fructose meals reduced 24-h plasma insulin and leptin concentrations and increased postprandial fasting triacylglycerols in women, but it did not suppress circulating ghrelin, a major appetite-stimulating hormone (4).

Fructose is metabolized, primarily in the liver, by phosphorylation on the 1-position, a process that bypasses the rate-limiting phosphofructokinase step (4). Hepatic metabolism of fructose thus favors lipogenesis, and it is not surprising that several studies have found changes in circulating lipids when subjects eat high-fructose diets (4). In the study conducted by Aeberli et al (1), dietary factors, especially fructose, were examined in relation to body mass index, waist-to-hip ratio, plasma lipid profile, and LDL particle size in 74 Swiss schoolchildren who were 6–14 y old. In that study, plasma triacylglycerols were higher, HDL-cholesterol concentrations were lower, and lipoprotein (LDL) particle size was smaller in the overweight children than in the normal-weight children. Fatter children had smaller LDL particle size, and, even after control for adiposity, dietary fructose intake was the only dietary factor related to LDL particle size. In this study, it was the free fructose, and not sucrose, that was related to the effect of LDL particle size. Studies in rodents, dogs, and nonhuman primates eating diets high in fructose or sucrose consistently show hyperlipidemia (4). The current report by Aeberli et al suggests that the higher intake of fructose by school-age children may have detrimental effects on their future risk of cardiovascular disease by reducing LDL particle size. It is interesting that this study did not find a relation of dietary fructose with triacylglycerols but did find a relation with the more concerning lipid particle, LDL cholesterol. Another recent report has proposed a hypothesis relating fructose intake to the long-known relation between uric acid and heart disease (3). The ADP formed from ATP after phosphorylation of fructose on the 1-position can be further metabolized to uric acid. The metabolism of fructose in the liver drives the production of uric acid, which utilizes nitric oxide, a key modulator of vascular function (3). The studies by Aeberli et al and Nakagawa et al suggest that the relation of fructose to health needs reevaluation.

Acknowledgements

This article, courtesy of medaus.com

The author had no personal or financial conflict of interest.

References1

1. Aeberli I, Zimmermann MB, Molinari L, et al. Fructose intake is a predictor of LDL particle size in overweight schoolchildren. Am J Clin Nutr 2007;86:1174–8.[Abstract/Free Full Text]
2. Bray GA, Nielsen SJ, Popkin BM. Consumption of high-fructose corn syrup in beverages may play a role in the epidemic of obesity. Am J Clin Nutr 2004;79:537–43.[Abstract/Free Full Text]
3. Nakagawa T, Hu H, Zharikov S, et al. A causal role for uric acid in fructose-induced metabolic syndrome. Am J Physiol (Renal Physiol) 2006;290:F625–31.[Abstract/Free Full Text]
4. Havel PJ. Dietary fructose: implications for dysregulation of energy homeostasis and lipid/carbohydrate metabolism. Nutr Rev 2005;63:133–57.
5. Vartanian LR, Schwartz MB, Brownell KD. Effects of soft drink consumption on nutrition and health: a systematic review and meta-analysis. Am J Public Health 2007;97:667–75.[Abstract/Free Full Text]
6. Harnack L, Stang J, Story M. Soft drink consumption among US children and adolescents: nutritional consequences. J Am Diet Assoc 1999;99:436–41.

Related articles in AJCN:

My friend, the late Dr. Bob Breedlove, sent me an article published in the Des Moines Sunday Register in early May about 6 weeks before his untimely death in the 2005 Race Across America.

His comment alongside the article was, “I thought you made Spizerinctum up!” Here is the complete article illustrating the word Spizerinctum has been around for quite some time and actually has had many meanings. The author works for the Merriam-Webster’s Collegiate Dictionary, 10th edition Wordwatch program.

Question: My nephew claims that there is a word, “Spizzerinctum” that means something like “zest for life.” I looked in several dictionaries and did not find this word. It sounds to me like something he made up and I wonder if he is pulling my leg.

Answer: Over the years, we’ve answered a number of inquiries like yours about “spizzerinctum” (a word that has many spelling variants.) Here’s one from a letter written in 1917: “I have just had a discussion about some such word as “spizzerinctum.” Last winter I heard a speaker use the word and say it then was the newest word in the English vocabulary and meant “vim and vigor.” My friends maintain there is no such word. Could you kindly advise me?

“Spizzerinctum” is one of those words that people love to discover. It is indeed a real word – real enough to be entered in our unabridged Webster’s Third New International Dictionary, where it is defined as “the will to succeed; vim, energy, ambition.”

Spelled “Spizarinctum,” this peculiar word was used in the mid – 1800’s for “specie,” that is, for money in the form of coins. In fact, the word “spizarinctum” is thought to be simply a fanciful coinage” from “Specie.” Here’s the word used with a slightly different spelling in 1869, by someone writing about “greenbacks,” or paper money: “They (greenbacks) had gotten no further west than Marshall (Texas), and everywhere west of that, when a man named a price, he meant “Spizerinctums.”

A 1913 streetcar sign in Washington, D.C. announcing the publication of a new dictionary featured “Spizzerinktum”; “See if you can find the word in any other dictionary, “the sign boasted. As “pizzeringtom” the word was noted circa 1922 as meaning “the quintessence of pep”. “Spizerinkum” was defined in a 1944 book of US Marine Corps slang as “intestinal fortitude.”

A mayor in Columbus, Ohio is said to have been fond of the word in the 1950’s and 60’s, but in general the word seems to have floated in and out of popularity. Now it may be experiencing something of a revival. Not long ago, a catalog featuring chickens for breeding even described one particular breed as noted for being especially endowed with “spizzerinktum.”

The true story behind how I came across the word Spizerinctum goes back to 1993 when I was doing home health physical therapy. A Louisiana woman announced when I entered her home and asked how she was, “I don’t have any spizerinctum today!” I said, “What is that?” She explained it was a Southern term for pep or energy! I loved that word and when the opportunity to use it came along after the demise of my 1986 Pete Penseyres concocted complete liquid food drink known as “Ultra Energy,” I jumped at it! Spizerinctum (my spelling) made perfect sense for a nutritionally complete energy drink, especially now in light of so many other appropriate meanings for what I have tried to create with this product. To my friend Bob Breedlove I wish you God’s speed and thank you for your long friendship and camaraderie. You will be greatly missed!

Randy Ice P.T., C.C.S.

Longevity Plus

INTRODUCTION

Many years ago when I re-made Ultra Energy into SPIZ, I selected a “hydrolyzed” whey protein as my protein source because whey is the highest quality dietary protein based on its excellent amino acid profile and easy digestibility.

Whey protein also contains the sulfur containing amino acid cysteine, which is needed to synthesize the body’s number one intracellular antioxidant, glutathione. Glutathione is a potent antioxidant that defends the body against free radical damage and is necessary for lymphocyte proliferation and immune function. Animal studies suggest that whey protein may reduce the risk of cancer due to its glutathione stimulating effect. In fact, one of the first whey protein products to come on the market in the 1990’s was “ImuPlus”, a non-denatured whey protein isolate that was/is promoted to cancer and AIDS patients specifically for its glutathione stimulating effects. Due to its antioxidant effects, whey protein is being researched for its ability to prevent degenerative diseases like cancer, Parkinson’s and heart disease. There are also indications that glutathione can alter gene expression in a way that promotes muscle growth.

A very interesting study compared supplementation of 20 grams of whey protein concentrate per day with 20 grams of casein protein per day for 3 months. The results showed that supplementation with whey significantly increases lymphocyte glutathione levels by over 35% and also improved peak power and 30 second maximal work capacity. There were no changes in the casein group. The whey group also had a decrease in bodyfat percentage while maintaining their bodyweight, meaning they were gaining muscle mass at the same time! These are the kind of positive changes typically seen with testosterone replacement therapy!

In the ensuing years research into whey protein has continued to strengthen my initial impression that whey is simply the best protein source to improve performance in athletes of all types. It can help build and maintain muscle mass and strengthen as well as assist those with catabolic illnesses trying to prevent loss of lean body mass, improve immune function, detoxify and improve antioxidant function. One-sub-fraction of whey has been found to stop bone catabolism and may reverse osteoporosis. This product is called “milk basic protein” and consists of 54% lactoferrin and 41% lactoperixidase and a few other proteins and is approved in Japan as a “functional food” ingredient in tofu and natto. Adding whey to fermented soy…..Hmmm! That should give you a bit of insight into a comparison of whey protein to soy protein coming later on in this review.

Depending on the type of whey protein selected, any or all of these health and/or exercise performance objectives can be achieved. This “primer” will review what is known about whey protein, the importance of its source and processing, how it improves performance and immune function and the differences between whey concentrates, isolates and hydrolysates . Proof of its superiority over casein or soy protein will also be presented.

TYPES OF WHEY PROTEIN

Whey protein is one of three types of proteins found in dairy, the other being casein and “milk basic protein” which is actually a sub-fraction of whey. Whey proteins are being studied for their ability to have a positive effect on nitrogen balance, which is the chemical element that makes protein different from carbohydrates or fatty acids which contain carbon, oxygen and hydrogen only. Certain whey proteins can have profound effects on immune function and can reduce inflammation in the body. Although milk allergy and/or lactose intolerance is fairly common, one form of whey is essentially free of both these issues and can be used by anyone without risk of GI tract distress or allergic response.z

Whey is a byproduct of cheese manufacturing. The fat (“curds”) are filtered from the milk as is much of the other milk protein, casein. The remaining product is a whey protein “concentrate” which also contains a 5% solution of lactose in water, some fats, minerals and different types of lactalbumin. If not heated (pasteurized), whey concentrate is “undenatured”, and is in its most biologically active, immune stimulating form and is 40 – 85% protein by weight. For those who are lactose intolerant, this form of whey is more likely to provoke a GI tract reaction. Likewise those whose who are allergic to milk will have an allergic response to whey concentrates due to the many intact protein structures. Whey concentrate contains a mixture of beta-lactoglobulin (65%), alpha-lactoglobulin (25%) serum albumin (8%) and immunoglobulins such as lactoferrin, lactoperoxidase and glycomacropeptide which are all very beneficial to the immune system.

Recently research published in the journal PLoS One found that breast-fed children are more protected against cancer than formula-fed children. The alpha-lactoglobulin referred to above combines with oleic acid which is found in babies stomachs. The combined protein is called “Human Alpha-lactalbumin Made LEthal to Tumor cells“ (HAMLET) and can effectively kill cancer cells for years to come. HAMLET can also trigger cancer cells apoptosis pathways, which is programmed cancer cell death. A pilot study of bladder cancer patients who had a HAMLET solution injected via a catheter found it killed cancer cells and shrunk tumors within 5 days.

WHEY VS CASEIN – WHEY IS WAY BETTER!

Interestingly, human mother’s milk is 60% whey and 40% casein. Cow’s milk is 20% whey and 80% casein. This ratio difference suggests humans do better on whey protein than casein protein, which is problematic for another reason. There are two types of casein that differ by one amino acid. Milk from Bos Taurus subspecies of cows which includes Holsteins, Ayshsires and Frisians produce A1 beta casein while milk from humans, goats and Guernsey cows contains A2 beta casein. The vast majority of cows in the Western Hemisphere produce A1 beta casein. A1 beta casein is highly inflammatory and has been shown to provoke an autoimmune response. It has been found that many cases of Type I childhood onset diabetes is linked to cow’s milk consumption containing A1 beta casein, which sets off an autoimmune response that destroys the beta cells in the pancreas that make insulin.

A1 beta casein results from a genetic variation at position 67 of the casein 209 long amino acid structure. A1 beta casein has the amino acid histidine at this point while A2 beta casein has the amino acid proline instead. This results in a 7 amino acid peptide called “casomorphin-7” (BCM-7) being cleaved off the A1 casein, a process that does not occur with A2 beta casein. BCM-7 is an opioid resistant to degradation and creates rampant oxidative stress in the gut and blood stream as well as a strong immune response. BCM-7 can cause “leaky gut syndrome” with digestive disorders and is itself absorbed and circulated in the blood. It can cross the blood brain barrier causing a number of neurodegenerative changes. BCM-7 injected into rats has been shown to cause autistic and schizophrenic type behavioral changes. It can cause reduced GI tract motility and constipation and is most damaging in infants who naturally have increased intestinal permeability. Giving cow’s milk containing A1 beta casein to infants under age 2 would not be a good idea for these reasons alone. However, the story of casein gets worse!

Studies of A1 beta casein consumption and the incidence of coronary heart disease in populations of many countries around the world has shown a strong correlation between the two. The reported correlation coefficient between the two is 0.76, which is as high as the correlation coefficient between smoking with lung cancer. Now correlation does not prove causation, however studies of dietary intake of A2 beta casein and childhood diabetes and adult onset coronary artery disease shows NO correlation. By the way, research has found that cheese, yogurt and fermented milk products like kefir from A1 beta casein containing breeds produce around the same amount of BCM-7 as regular milk. The graph below illustrates the dietary A1 beta casein/heart disease link:

Clearly whey protein is superior in every important measurement of protein quality and utilization relative to soy. So I hope this Whey Protein Primer has given you an education and some insights into the differing kinds of whey and what whey product would be best for your particular application whether it be exercise performance, recovery, muscle or strength building or just for health purposes. Feel free to contact me if you have any questions.

Randy Ice PT, CCS

It is theorized that BCM-7 oxidizes LDL cholesterol (OxLDL) which accumulates in the arterial wall and is the mechanism of how A1 beta casein contributes to coronary atherosclerosis.

Casein is also a much slower absorbing protein in the intestinal tract relative to all forms of whey, hence is less desirable from the standpoint of getting branched chain amino acids to the muscle cells as quickly as possible during or after exercise, even if one had access to A2 beta casein which in the USA is very difficult if not impossible.

I recently had a discussion with the owner of the Organic Pastures dairy in Fresno, California that is the only raw, unpasteurized milk producer in this state. In discussing the A1/A2 beta casein controversy, his feeling was that the science behind it is not settled, and the real issue for milk (and therefore whey) producing cows is whether they are grass fed or not. Grass fed cows lead to far healthier milk, and therefore a better protein content. The SPIZ whey protein does come from grass fed cows in New Zealand, which is another reason is it superior.

Whey protein also contains the sulfur containing amino acid cysteine, which is needed to synthesize the body’s number one intracellular antioxidant, glutathione. Glutathione is a potent antioxidant that defends the body against free radical damage and is necessary for lymphocyte proliferation and immune function. Animal studies suggest that whey protein may reduce the risk of cancer due to its glutathione stimulating effect. In fact, one of the first whey protein products to come on the market in the 1990’s was “ImuPlus”, a non-denatured whey protein isolate that was/is promoted to cancer and AIDS patients specifically for its glutathione stimulating effects. Due to its antioxidant effects, whey protein is being researched for its ability to prevent degenerative diseases like cancer, Parkinson’s and heart disease. There are also indications that glutathione can alter gene expression in a way that promotes muscle growth.

A very interesting study compared supplementation of 20 grams of whey protein concentrate per day with 20 grams of casein protein per day for 3 months. The results showed that supplementation with whey significantly increases lymphocyte glutathione levels by over 35% and also improved peak power and 30 second maximal work capacity. There were no changes in the casein group. The whey group also had a decrease in bodyfat percentage while maintaining their bodyweight, meaning they were gaining muscle mass at the same time! These are the kind of positive changes typically seen with testosterone replacement therapy!

WHEY PROTEIN ISOLATES

When whey concentrates are treated through the another process called “ion exchange” which denatures the protein and immunoglobulins with heat, and/or microfiltration the resulting end product is a whey isolate that is mostly, but not completely free of lactose. The ion exchange process literally wipes out all the valuable and health promoting sub-fraction peptides except beta lactoglobulin which is the most common milk protein allergen. Hence this would not be a good product to consume for those with milk allergy. Whey isolates contain 85 -90% protein that are absorbed faster than a whey concentrate. Like whey concentrates, they are mild to slightly milky in taste.

Whey is THE most abundant source of branched chain amino acids (BCAA’s) which are used to fuel working muscles and stimulate protein synthesis. The branched chain amino acids include leucine, valine, alanine and isoleucine, and have been also been found to inhibit the transport of heavy metals across the blood-brain barrier. In particular, the amino acid leucine plays a key role in initiating the transcription of protein synthesis. Adequate leucine intake is required to speed recovery and help with adaption to exercise. Since high intensity and/or prolonged aerobic exercise, or heavy weight training results in protein catabolism in the former and micro muscle tears in the latter, replenishing protein during and immediately after exercise is critical to a faster recovery process and maximizing training effects.

Another factor to remember is the contribution of protein to total energy expenditure in long distance sports such as cycling, running, swimming, triathlon and so forth, which has been measured at 5 to 15%. This can make the difference between winning and losing, or a good versus bad competitive performance if not addressed properly.

WHEY PROTEIN AS AN IMMUNE SYSTEM STIMULATOR

Whey protein also contains the sulfur containing amino acid cysteine, which is needed to synthesize the body’s number one intracellular antioxidant, glutathione. Glutathione is a potent antioxidant that defends the body against free radical damage and is necessary for lymphocyte proliferation and immune function. Animal studies suggest that whey protein may reduce the risk of cancer due to its glutathione stimulating effect. In fact, one of the first whey protein products to come on the market in the 1990’s was “ImuPlus”, a non-denatured whey protein isolate that was/is promoted to cancer and AIDS patients specifically for its glutathione stimulating effects. Due to its antioxidant effects, whey protein is being researched for its ability to prevent degenerative diseases like cancer, Parkinson’s and heart disease. There are also indications that glutathione can alter gene expression in a way that promotes muscle growth.

A very interesting study compared supplementation of 20 grams of whey protein concentrate per day with 20 grams of casein protein per day for 3 months. The results showed that supplementation with whey significantly increases lymphocyte glutathione levels by over 35% and also improved peak power and 30 second maximal work capacity. There were no changes in the casein group. The whey group also had a decrease in bodyfat percentage while maintaining their bodyweight, meaning they were gaining muscle mass at the same time! These are the kind of positive changes typically seen with testosterone replacement therapy!

WHEY PROTEIN, LEUCINE AND EXERCISE PERFORMANCE

Leucine is one of nine so called “essential amino acids” that can only be obtained through the diet. In one study of 26 untrained healthy men aged 20 – 36, half received 4000 mg of leucine and half a placebo. Twice weekly all subjects were supervised by professional trainers in 8 standard weight resistance training machines with strength testing before and after 12 weeks. At the end of the study the placebo group increased their maximum five repetition weight resistance ability by 31% while the leucine group increased by 41%, a 10% greater improvement with just leucine.

Another study of “elderly“ subjects, who have a more blunted response to protein than younger men examined a single leg resistance exercise protocol with either a whey or casein protein supplement immediately after exercise. Both drinks contained 20 grams of protein, however the whey protein had 2.6 grams of leucine while the casein protein had 1.6 grams of leucine. Muscle protein synthesis was calculated in the non-exercised leg and the exercised leg for 4 hours after exercise. Compared to casein, the whey group had 65% greater protein synthesis in the NON-exercised leg and 69% greater in the exercise leg. So whey is superior to casein in stimulating muscle protein synthesis even in “older” people/athletes!

WHEY PROTEIN HYDROLYSATES

If one takes a whey protein isolate and further treats it with heat and acid, the whey is degraded into much smaller peptide units called di and tripeptide amino acids. This process mimics our own digestion, hence the term “predigested” and the peptides are actually absorbed more rapidly than free form amino acids. Hydrolysis is an easy way to further purify the whey and remove the last vestiges of lactose, milk fats and immunoglobulins.

The resulting whey “hydrolysate” is 90 – 95% pure protein and is now in its most easily digestible form, and will be absorbed in the small intestine more quickly than whey concentrates or isolates. Those with lactose intolerance will have no issues with a hydrolyzed whey protein as virtually all the lactose is removed. Additionally those who have true milk allergy will be able to digest hydrolyzed whey protein without problem because the above mentioned beta lactoglobulin is hydrolyzed (digested) and is no longer present. The resulting whey hydrolysate is an extremely fine powder as it has been “pre-digested” into very small amino acid units. It has a fairly bland to not-so-great taste by itself.

THE BENEFITS OF CONSUMING A WHEY HYDROLYSATE DURING OR AFTER EXERCISE

Consumption of a whey protein hydrolsyate during and/or in post-exercise drinks is preferred because it results in a faster increase in blood amino acid concentrations AND a higher insulin response during a 1 – 2 hour period than does intact protein from any source. The simultaneous increase in blood amino acids and insulin significantly promotes muscle protein synthesis and inhibits muscle breakdown. Adding glucose to a whey protein hydrolysate results in a peak insulin level that is 2 – 4X HIGHER than after ingestion of milk with the same amount of glucose (15 grams in this study).

You may not realize it, but insulin is an anabolic hormone like testosterone that has muscle building effects. Hence spiking insulin briefly while ingesting BCAA’s during or after exercise has even more beneficial effects on hard working muscles. This can be either from an anabolic perspective with weight training (which is why competitive bodybuilders frequently inject insulin even though they are not diabetic) or in long distance endurance athletes trying to prevent muscle tissue catabolism (breakdown) that ultra long training and/or competition can create (think skinny and somewhat emaciated long distance runners).

Another practical advantage is that one can ingest a whey protein hydrolysate supplement immediately after exercise without becoming bloated and not excessively suppress appetite. So this means you can eat a meal sooner possibly increasing the post-exercise “anabolic window.”

WHEY PROTEIN PRODUCT CAVEATS

Beware that not all whey is the same. Consumer Reports tested several bodybuilding whey protein powders and found many were contaminated with heavy metals. Worse yet, the vast majority of whey protein powders you will find in health food stores are flavored with artificial sweetners such as aspartame, sucralose or Acesulfame K among others. These sweetners are not safe and are known to kill off healthy good bacteria in the colon in the case of sucralose, aka Splenda. Aspartame is a proven neurotoxin (think former Diet Coke addict, now Parkinson’s patient Michael J. Fox) that has more complaints for a wide variety of symptoms than any other nutritional product on file with the FDA, which they have chosen to ignore for over 25 years. The SPIZ whey protein available at www.SPIZ.net is a 100% hydrolyzed, unflavored whey protein with no artificial sweetners, flavoring agents, etc. and is the same hydrolyzed whey that is in SPIZ. I prefer to let you flavor it with whatever you wish as it can be mixed with anything. I mix it with fruit juice and ice cubes to make a healthy protein smoothy every morning for breakfast, and to drink right after my workouts.. Every serving has 65 grams of hydrolyzed whey di and tri-peptides with over 18.7 grams of BCAA’s, of which 7.8 grams is leucine. There is no lactose, no lactoglobulins (milk allergens), no heavy metals and no GMO’s (Genetically Modified Organism) in this product.

The highest quality whey protein comes from cows (or goats) fed pure 100% grass. Again, if you pick up a canister of whey protein in your local health food store, the type of feed and country of origin will more than likely not be specified. The number ONE country in the world for whey protein production and export is New Zealand, which takes great pains raising their cattle in pastures free of contaminants and fed grass or hay exclusively. When I developed SPIZ in the mid 1990’s, my research discovered these facts and I chose a hydrolyzed whey protein from New Zealand as its protein source. I knew it was the next best thing to putting pure amino acids in it (which is even more expensive as I used to do with SPIZ’s forerunner, Ultra Energy). I also knew it would be the protein that provides the most high quality BCAA’s and leucine as well as be digested and absorbed the most quickly. Time has proven that true as athlete after athlete in competition over the last 18 years has consumed 20 grams of the hydrolyzed whey protein in SPIZ every hour for hours and days on end in some cases.

RACE NUTRITION AND DIGESTION AS LIMITING FACTORS TO SUCCESSFUL ENDURANCE PERFORMANCE

Whey has also been found to increase liver and muscle glycogen stores compared to a casein-based diet containing the same amount of carbohydrates. Muscle glycogen is the primary carbohydrate fuel source needed to generate muscle contraction and energy. The more you can produce and store, the less likely you are to bonk. You must replace glucose continually during any sport lasting longer than 2.5 – 3 hours, and as it turns out, hydrolyzed whey protein assists with this process which is why carbohydrate/protein drinks have been proven superior to carb only products.

These are some of the multiple reasons why SPIZ energy drink/meal replacement gives superior performance by supplying key amino acids for generating energy production rapidly as well as protecting muscle protein stores from catabolism and also ensuring a faster recovery. No protein of any kind on the market is digested and absorbed more rapidly than hydrolyzed whey. This also accounts for the fact that virtually none of my customers has ever complained of a gastrointestinal issue or problem drinking SPIZ.

This is a BIG DEAL as a study published in the International Journal of Sports Physiology and Performance in 2011 examined factors related the successful performance of runners in the 2009 Western States 100 and Vermont Trail 100 mile run. Utilizing a post-race questionnaire, the researchers looked at a host of factors including training volume, maximum run volume, use of Non-Steroidal Anti-inflammatories, age, BMI, years of experience, number of 100 mile races completed and other factors, to determine what correlations could be made for those who finished versus those who had to drop out.

The number ONE cause of not finishing was “nausea and/or vomiting” as the culprit ( 23%), more than any other factor including runners citing injury, blisters, muscle cramps or exhaustion as the limiting factor ( 21.6%). In other words, more ultramarathon runners dropped out due to GI distress than injury, blisters, cramps and fatigue combined! Even 36% of the finishers reported nausea and/or vomiting affected their race performance, so many of them still did not have an optimum nutrition plan. This study strongly suggests that THE single most important factor in determining ultra distance success is nutritional intake during competition.

WHEY VS SOY – IT’S NO CONTEST!

Many health claims are purported for soy protein including “lowering cholesterol” (which is a worthless strategy for preventing or treating coronary disease) and relief of menopausal hot flashes (which is better accomplished with bioidentical estrogen and/or progesterone replacement). However, when it comes to building or maintaining muscle, then the protein with the largest concentration of usable amino acids in it is what you’re looking for. As we shall see, soy protein is quite inferior to whey protein in many different respects. Let’s start with Biological Value (BV).

BV measures the digestibility of a protein as well as its availability of the protein to the body. A BV of 100 was assigned to egg protein many years ago meaning that 100% of the egg protein was absorbed. Since then the evolution of protein powders have become better sources of protein than eggs, so some kinds of proteins have a score higher than 100. The higher the BV score the better the protein. When whey and soy proteins are compared using BV values a typical soy protein concentrate has a BV rating of about 74 while the typical whey protein has a BV of 104.

Another measure of a protein is called “Net Protein Utilization”, which is a measure of the amount of amino acids that are converted to protein in the body versus the amount of amino acids for the protein eaten. This measurement is also on a scale from 0 – 100% with 100% meaning all of the protein consumed is taken up in the body. A typical soy protein has a NPU of about 61% while a typical whey protein has a NPU of 92%. Protein Efficiency Ratio (PER) calculates the gain in body weight divided by the weight of the protein consume by infant laboratory rats. PER measures growth and the FDA uses the PER of a protein to derive the recommended daily allowance of protein that are found on all food labels. A PER of greater than 2.7 is classified as an “excellent” source of protein. Comparing whey to soy, PER scores reveals a rating of 3.2 for whey and 2.2 for soy.

Another way to look at the question of which protein is best is to look at its “Amino Acid Score (AAS).” In the AAS scale, a value greater than 1 demonstrates that the studied protein has higher levels of amino acids than the human body requires. In this respect whey as an AAS of 1.14 while the typical soy concentrate has an AAS of 0.99.

To evaluate protein quality based on the amino acid requirements of the human body, another measure is the “Protein Digestibility Corrected Amino Acid Score.” The FDA, World Health Organization and the Food and Agricultural Organization of the United Nations have all collectively decided to have the PDCAAS as the “best” method for determining protein quality. This score measures essential amino acids in a protein compared to a reference protein, which is what an everyday human body requires and is given a PDCAAS of 1.0. Unfortunately, as is typical of government bureaurats, this scoring method became politicized by “rounding down” any protein with a score of higher than 1.0. This lead to whey and soy proteins having identical 1.0 scores.

There are several other ways of looking at the question of which protein is better, whey or soy. The following table summarizes ALL of those methods and results:

Clearly whey protein is superior in every important measurement of protein quality and utilization relative to soy. So I hope this Whey Protein Primer has given you an education and some insights into the differing kinds of whey and what whey product would be best for your particular application whether it be exercise performance, recovery, muscle or strength building or just for health purposes. Feel free to contact me if you have any questions.

Randy Ice PT, CCS

Introduction SPIZ is a scientifically blended formulation of carbohydrates, proteins, fatty acids, vitamins and minerals that is mixed with water.

It is a complete liquid food source developed to fuel the human engine during times of illness, stress, exercise and/or increased caloric need; a nutritional food and meal replacement drink that is being used by endurance athletes (cyclists, runners, triathletes, etc.), cancer and AIDS patients as well as geriatric folks trying to maintain or increase lean body mass.

The superiority of SPIZ comes from both the correct ratio of ingredients as well as the sources of these ingredients. The following is an explanation of what’s in SPIZ, why and how to use it.

1. Hydrolyzed Whey Protein Hydrolysate

First, whey protein hydrolysate is the highest-quality currently available in supplemental form, although many people think egg white protein is the highest quality, whey protein is superior.

Second, hydrolyzed WPC is WPC that has been partially broken down so that it is more readily assimilated by the body. This is especially beneficial to the athlete who is taking the product during exercise when the digestive system is not functioning at full capacity.

Third, most products contain just carbohydrates when in reality the body does utilize protein for energy during exercise, up to 15% of total energy expenditure! Protein is also very important after exercise for not only protein metabolism, but also glycogen resynthesis.

Fourth, branched chain amino acids-(BCAA’s) have documented anabolic effects (promoting muscular growth) as well as anti-catabolic activity (preventing muscle breakdown). SPIZ has a high concentration of BCAA-to-tryptophan, which compete with each other to cross the blood-brain barrier. Keeping brain trytophan levels down will reduce brain serotonin levels, preventing CNS-induced fatigue and promoting a wakeful state. SPIZ has over 4 grams of BCAA per serving which creates both a “protein sparing” effect at the muscle cell level and a “glycogen sparing effect” as well.

2. Chelated Minerals

The chelated minerals used in Spiz are the most bioavailable form of minerals currently available as well as being the most expensive. SPIZ contains only the highest quality chelated minerals from the most well respected name in mineral manufacturers, Albion Laboratories.

3. 100% US Daily Values for vitamins per serving (except for vitamin D)

Including 100% of the US Daily Values for the antioxidants, vitamin E, and Beta-carotene, which can help protect the body from the potentially damaging effects of free radicals. These highly-reactive substances are formed during exercise and can cause damage to the human body. In fact, these free radicals are believed to be integral to the aging process itself, as well as in the development of cancer and heart disease. The body utilizes various vitamins at significant rates during exercise, in fact in direct proportion to exercise intensity.

100% of the US Daily Values of the entire B-Complex, which are intimately involved in energy production.

In addition, each serving contains only 10% of the US RDA for vitamin D since this vitamin is a fat-soluble vitamin that is not only stored in the body, but which can be synthesized through sufficient sunlight exposure, which most athletes are exposed to on a daily basis. In fact, everyone should obtain 20-30 minutes of sunlight exposure each day.

Extra Vitamin C (501 mg/serving) for stress or exercise-induced oxidation protection.

4. Short, and long-chain glucose polymers, along with smaller amounts of sugars.

This helps to energize the exercising individual with a supply of both long and short-acting carbohydrates.

5. Covalent Bonded L-Glutamine has been added to the formula for the following reasons:

Conditionally-essential amino acid, meaning that the human body cannot manufacture enough L-glutamine during certain conditions and must therefore obtain this amino acid from the diet. One of those conditions appears to be stress, such as that resulting from physical exercise.

Helps maintain blood sugar levels which can be very important in maintaining energy levels during exercise.

Considered to be the “thinkers” amino acid, as it can help maintain concentration and focus during exercise.

Has been shown to be the most important amino acid in regulating muscle protein synthesis. Consequently, according to research, if muscle glutamine levels are decreased (which is a normal occurrence in exercise), muscle protein synthesis is reduced. Conversely, if muscle glutamine levels can be maintained or increased, then muscle protein synthesis occurs in direct proportion to muscle glutamine level, an issue very important to proper recovery.

6. High sodium/potassium concentration

Sodium and potassium losses lead to Hyponatremia (low sodium levels) and less frequently in long-distance athletes, Hypokalemia (low potassium levels). High intakes of sodium and potassium prevent these electrolyte disturbances and will prevent muscle cramping.

Sodium is a “carrier” molecule which serves to facilitate the transfer of glucose and amino acids into the bloodstream across the intestinal wall. Hence, high sodium concentrations promote faster absorption of nutrients during exercise, an important factor as, GI blood distribution is reduced.