8 posts categorized "Undenatured Whey Protein"

March 22, 2012

Whey Protein Q&A - Protein Bars and Protein Requirements

BlogProQAC Q. What’s wrong with protein bars?

A. There are  potentially several things wrong with protein bars, beginning with the low quality of protein often used in them (protein bars often contain many of the sub-optimal protein sources previously mentioned in this series of articles –  i.e., powdered casein/caseinate, whey protein concentrate, and/or soy protein).  Some protein bars do contain whey protein isolate, but in all likelihood, even the whey isolate used in protein bars will be nutritionally inferior as well. 

One of the challenges in creating protein bars is preventing the bar from drying out and becoming hard and unpalatable during the shelf life of the product.  To combat this challenge in recent years, whey protein manufacturers have created proteins (including versions of whey isolate) specifically for use in protein bars.  These proteins are purposefully denatured to reduce their affinity for moisture.  The idea is, if proteins are prevented from absorbing and attracting moisture in the first place, this reduces the chance of the protein in the bar subsequently drying out and becoming hard during its shelf life.  But, as we’ve seen, denaturation of whey protein may significantly compromise many of its unique health benefits.

Protein and food bars are also often made with nut and seed butters and oils which are very concentrated sources of polyunsaturated fats, including the omega-6 fat, linoleic acid (e.g., almond butter, peanut butter, sesame butter, canola oil et al.).  At Integrated Supplements, we’ve written many articles on the harmful effects of linoleic acid at the doses currently found in the modern Western diet.  Because of the fats they contain, most protein and natural food bars only serve to exacerbate this excess.  As we’ve documented elsewhere, the research gives every reason to believe that such lipids are disruptive to thyroid function, cellular respiration, immune function, and blood sugar control to name just a few.  Because they disrupt metabolic function by so many different mechanisms, these lipids are among the most “fattening” sources of calories available.

As the ingredients they contain are sub-optimal nutrition, protein bars can hardly be expected to improve most diets.   In fact, the real problem with protein bars may be that they can very easily perpetuate the practice of constant snacking on low-quality, calorically-dense processed foods.  For the health- and physique-conscious individual, it’s important to realize that protein bars will more likely hinder their efforts, rather than help.

By their very nature, protein (and other “food bars”) are among the most calorically-dense foods available – i.e., they contain a high amount of calories relative to the overall weight of the food.  Studies have shown that calorically dense foods can often lead to weight gain, whereas foods which are less calorically dense – i.e., foods like fruit which contain phytonutrients, fiber and water – are more filling, and may thus help with weight loss:

Study Link - A satiety index of common foods.

Quote from the above study:

Protein, fibre, and water contents of the test foods correlated positively with [satiety index] scores.

To the best of our knowledge, studies have yet to investigate how eating protein bars affects overall calorie consumption. 

Of course, with the fast-paced lifestyles of today, it’s easy to see why their convenience has made protein bars staples of many people’s diets.  And while protein bars have never been particularly high-quality nutrition, their quality has steadily declined even further as they’ve been increasingly marketed towards the mainstream market. Over the past several years especially, protein bar manufacturers have learned what junk-food and fast-food producers have known for many decades: nutritional content doesn’t matter much when it comes to the bottom line.  In other words, if a product tastes good, it sells – almost regardless of its nutritional composition.  Of course, users of protein bars will often say they want bars with a certain nutritional composition, but in the end, sales numbers don’t lie – bars with the highest fat, sugar, and calorie content are often the best sellers.

When viewed objectively based upon their ingredients and nutritional composition, the vast majority of protein bars aren’t even close to healthy food options.  But marketing protein-laced candy bars as healthy foods plays into what many consumers already want to believe – that health and fitness can be achieved with almost no effort whatsoever.

Generally, those who replace meals with protein bars are consuming low-quality nutrition which is almost certain not to reduce appetite nearly as well as a healthy balanced meal.  Those who use protein bars between meals are simply snacking on some of the most calorie-dense foods available anywhere – hardly a recipe for health and fitness success. Those who only eat protein bars every once in a while are on the right track, although, all things considered, some traditional candy bars may actually be better choices.

Q. Isn’t it important to eat every couple of hours to keep the metabolism going?  How can a person do this with only “real” food?

A. Maintaining steady blood sugar and serum protein (albumin) levels are important goals of any healthy diet, but constant snacking usually isn’t necessary to achieve this – especially if the chosen snacks contain substances which inhibit the metabolism, as we’ve seen most protein bars and drinks do.

For the general health-conscious individual – especially one looking to lose bodyfat – the key is consuming balanced meals which enhance metabolic function instead of disrupting it.  Along these lines, every effort should be made to consume nutrient-dense meals which contain (at the very least) combinations of protein and carbohydrates.

Properly-constructed meals will support healthy blood sugar, trigger the fed state, and control appetite automatically, without the need for constant snacking.  At Integrated Supplements, we’ve written elsewhere about the types of foods which are likely to stimulate the appetite (e.g., starch), and the types of foods which are likely to reduce it (e.g., dairy/whey protein, fruit, certain types of fiber).

Some people, however (e.g., those with hypoglycemia and related blood sugar abnormalities), may function better on more frequent feedings throughout the course of the day.  If snacks are necessary in addition to the traditional meals of breakfast lunch and dinner, there are many suitable options available “on-the-go.”  These days, most convenience stores carry foods such as fruit, yogurt, cheese sticks, salads, hard-boiled eggs, and milk – all of which are far superior to the protein bars and ready-to-drink protein shakes which are often offered up as healthy convenience foods.

Q. What about those looking to build muscle? Doesn’t it take upwards of 1 gram of protein per pound of bodyweight to maximize muscle growth? 

A. People who work out do, indeed, have a higher protein requirement than sedentary individuals.  Even still, in a misguided attempt to support muscle growth, many bodybuilders and fitness enthusiasts consume more protein (and overall calories) than their bodies actually need. 

Evidence suggests that the often-recommended protein intake of “one gram per pound of bodyweight” for strength-training athletes is a bit high.  Research shows that a more reasonable goal may be 0.8 grams per pound of bodyweight:

Study Link - Evaluation of protein requirements for trained strength athletes.

Quote from the above study:

A suggested recommended intake for [sedentary subjects] was 0.89 g.kg-1.day-1 [0.4 grams/lb bodyweight] and for [strength-training subjects] was 1.76 g.kg-1.day-1[0.8 grams/lb bodyweight].

For a 175-pound individual, 0.8 grams of protein per pound of bodyweight equals 140 grams of protein per day.  Consuming this amount of protein daily may take a bit of planning and preparation, but it’s easily achievable through whole foods and relatively small amounts of high-quality protein supplements like whey protein isolate.

The supplement industry, however, often perpetuates the myth that “hardcore” bodybuilders need to consume significantly higher amounts of protein than this – a convenient lie which often begets a reliance on protein bars and drinks (not to mention large quantities of lower-quality/ less-expensive protein powders).  Similarly, the supplement industry also has a tendency to divert consumer’s attention away from readily-available real food sources of protein and towards protein supplements.  The recent marketing of casein/caseinates as “slow-digesting” proteins is a perfect example of this (milk and other dairy foods are far better sources of casein and muscle-building nutrients than casein/caseinate powders, and almost all real food proteins are slow-digesting). 

In actual practice, therefore, many aspiring bodybuilders simply eat too many calories from low-quality sources.

The ironic part is, they’re not only compromising their long-term health by doing so, but their physiques as well.  The chronically “pudgy” appearance of many would-be bodybuilders is often actually testament to the effectiveness of this sort of supplement marketing.

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February 25, 2012

Whey Protein Q&A - Whey Protein Isolate Versus Whey Protein Concentrate Part 2 - Denatured Proteins

BlogProQAC Q. What are denatured proteins and what are their health effects?

A. In simple terms, a protein is said to be denatured when its chemical shape changes in response to heat or extremes of pH (acid or alkaline). Some proteins (many enzymes, for example) lose their biological function when denatured; and particularly fragile proteins from whey protein must remain undenatured in order to exert their full biological activity.

Studies have found, for example, that heat and pH used in processing may denature up to 53% of the whey proteins found in whey protein concentrate:

Study Link - Influence of pH and heat treatment of whey on the functional properties of whey protein concentrates in yoghurt.

Quote from the above study:

Cheddar whey was heated at pH 6.4 or pH 5.8 at 72 °C for 15 s, eventually heated further at 82 or 88 °C for 78 s, ultrafiltered, and spray dried. Resulting WPC contained 38% protein; the denaturation level of the whey protein was 10–53%. 

Whey protein is somewhat unique among proteins in that its full biological function is largely dependent upon it being undenatured.  By contrast, many common food–based proteins are known to be somewhat denatured under normal cooking conditions; and, of course, these proteins still offer nutritional benefit. For example, an egg white which stiffens and turns white when cooked, is an example of a protein denaturing right before our very eyes.  Our body is still able to break the egg white down into its constituent amino acids, and is able to absorb and utilize these amino acids for use as the building blocks of our muscles, organs, tissues, and metabolic enzymes.  Cooking egg whites also denatures and inactivates certain substances which inhibit vitamin absorption – this is one instance, therefore, where denaturing protein is actually beneficial.

Similarly, many protein-based antinutrients (e.g., trypsin inhibitors) are denatured and inactivated by cooking.  So, clearly, it’s inaccurate to say that all denatured proteins are harmful, or that all undenatured proteins are beneficial.  The protein structures that are altered by cooking and processing really need to be assessed on a case-by-case basis.

But, as profitable methods of processing and preserving foods exploded in the early part of the twentieth century, there was often a tendency among food producers to simply ignore the health effects of the novel protein structures which formed as a result of processing.

This oversight continues to have serious effects upon public health.

Some modern industrial processes are likely to create unique protein structures which are not formed when foods are cooked normally. The extrusion cooking process, for example, allows for the creation of foods such as “puffed” breakfast cereals and snack foods (as well as protein “crisps” from soy and whey which are now commonly used to add texture to protein bars). Not only do the chemical changes resulting from the extrusion process reduce the amount of biologically active protein in the food, but the altered protein structures formed may impart some degree of toxicity.

Study Link - Nutritional effects of extrusion-cooking.

Though the scientific research gives clear reason for concern, we rarely hear about the health risks which arise when some foods are powdered, extruded, alkali-treated, or high-heat processed.  Perhaps this is partly because even the “health food” industry employs such methods in the processing of protein powders, drinks, breakfast cereals, meat replacements, and many non-dairy milks like soy milk.  These processes give the resulting products remarkably long shelf lives, which makes them far more profitable than fresh, perishable foods.

As scientists continue to study the effects of protein processing on nutritional quality, however, some interesting studies have emerged showing that many of the unnatural proteins formed in the production of modern foods and protein supplements are likely to be at least mildly toxic.

Q. What harmful denatured proteins can be formed in the production of protein powders and protein-containing beverages?

A. Scientists have long studied various toxic substances which are known to be formed during the production of protein–containing powders and beverages.  Though it’s likely that many protein–based toxins still have yet to be discovered, there is enough evidence in the scientific literature to make any educated person wary of certain protein powders and protein-containing beverages.

Alkali–treatment of proteins (including common nutritional supplement ingredients such as soy protein isolate, and calcium caseinate/casein), can lead to the production of unnatural cross–linked amino acids like lysinoalanine (LAL).  In animal studies at least, lysinoalanine has been shown to have many negative effects on digestion and overall metabolism:

Study Link – Influence of feeding alkaline/heat processed proteins on growth and protein and mineral status of rats.

Quote from the above study:

The data suggested that LAL, an unnatural amino acid derivative formed during processing of foods, may produce adverse effects on growth, protein digestibility, protein quality and mineral bioavailability and utilization. The antinutritional effects of LAL may be more pronounced in sole–source foods such as infant formulas and formulated liquid diets which have been reported to contain significant amounts (up to 2400 ppm of LAL in the protein) of LAL.

Study Link – Interaction of lysinoalanine with the protein synthesizing apparatus.

Quote from the above study:

These results indicate that LAL is an inhibitor of both prokaryote and eukaryote lysyl–tRNA–synthetase. Furthermore, it is incorporated into protein. Both of these actions can be factors in the nephrotoxicity [i.e., kidney toxicity] of this common food contaminant.

So, according to the above studies, processed proteins containing lysinoalanine may:

Inhibit growth

Inhibit protein synthesis

Inhibit digestion

Inhibit mineral absorption

• Harm the kidneys

• And impart numerous anti–nutritional effects

It’s more than a bit ironic then, that lysinoalanine (and many similar toxic “anti–nutrients”) can so commonly be found in the ingredients used by the nutritional supplement industry in an ever–increasing number of protein powders, bars, and drinks.

Decades ago, research into the toxic effects of protein processing centered on ways to create the least toxic infant formulas, or the least toxic enteral feeding formulas for hospital settings. Industrially processed proteins were never thought of as healthy, and the products in which they were used were produced for situations in which even poor nutrition was clearly better than dying of starvation. But, in recent years many of the same (or very similar) protein ingredients have been promoted as dietary staples for health–conscious consumers (e.g., soy and casein protein powders). Since so many people are currently being misled by flashy advertising and fancy product packaging, it’s important to point out the potentially harmful effects of some of the proteins found in nutritional powders, drinks, and bars.

In addition to alkali–treatment, toxins like lysinoalanine can also be formed as a result of the high heat processes now commonly used to pasteurize protein-containing beverages. Ultra heat treatment, or ultra high temperature (UHT) pasteurization and sterilization processes are now able to produce milk and milk–based products (like protein drinks), and non-dairy milks (e.g., soy milk, almond milk, rice milk) which require no refrigeration – but the formation of lysinoalanine in some of these products has been found to be shockingly high:

Study Link – Determination of lysinoalanine in foods containing milk protein by high–performance chromatography after derivatisation with dansyl chloride.

Quote from the above study:

The LAL contents analysed in raw and pasteurised milk ranged from 4 to 24 and 17 to 69 mg kg−1 crude protein, respectively. Compared to that, UHT–treated milk and sterilised milk showed higher LAL levels up to 186 and 653 mg kg−1 crude protein, respectively.

Note: As the above study indicates, normal pasteurization processes don’t necessarily lead to the production of high levels of lysinoalanine in milk.  Despite the common assumption among some health enthusiasts, pasteurization doesn’t always alter the nutritional value of milk to a great degree.  Milk (including organic milk) which has been “ultra-pasteurized,” however, is probably best avoided.

Protein drinks and many non-dairy milks (e.g., soy milk) are produced using protein powders.  Unlike fresh milk, the powders used in the production of these beverages may already contain significant lysinoalanine, even before further heat treatment:

Study Link - Lysinoalanine Content of Formulas for Enteral Nutrition

Quote from the above study:

. . .the preparation of caseinates and the thermal stabilization of the end products are the two steps more favorable for the formation of LAL.

And it’s important to note that lysinoalanine is far from the only toxic product formed by heat and pH treatment of proteins – it’s just one of the most extensively studied:

From: Lysinoalanine in Foods and Antimicrobial Proteins

Heat and alkali treatment of food proteins widely used in food processing results in the formation of crosslinked amino acids such as lysinoalanine, ornithinoalanine, lanthionine, and methyl lanthionine, and concurrent racemization of L–amino acid isomers to D–analogs.

Although many of the byproducts produced by protein processing have yet to be studied individually, there is clear evidence in the scientific literature that heat–treated protein drinks (the kind very commonly available, from soymilks, to protein–containing sports drinks) are likely to impart a cumulatively toxic effect.

As a practical example, the following study showed that both soy and casein protein, when subjected to ultra heat treatment (UHT) caused a significant elevation in LDL cholesterol levels:

Study Link – Ultra heat treatment destroys cholesterol–lowering effect of soy protein.

Quote from the above study:

Unexpectedly, at the end of the study, low–density lipoprotein cholesterol concentrations were significantly increased compared with baseline in all study groups. The magnitude of this increase (17–19%) was similar in all active and placebo study groups. Soy protein supplements previously shown to be effective in reducing serum cholesterol had in this study no such lipid–lowering effect after ultra heat treatment.

Without undergoing UHT treatment, soy protein or casein either have no effect, or may even lower LDL cholesterol. With UHT treatment, however, these proteins led to a 17% to 19% increase in LDL cholesterol. The study authors concluded that the altered protein structures resulting from heat treatment were responsible, and noted that the “heart health” claim currently allowed by the FDA for soy proteins should likely be revised to exclude UHT-treated soy protein.  This study is clear evidence that changes in protein structure can markedly increase the toxicity of food proteins in humans.

Note: the above study has nothing to do with the cholesterol content of the drinks, as soy and casein (unlike whey protein concentrate) don’t contain cholesterol.  The cholesterol elevation caused by heat-treated soy and casein is evidence of the generally toxic nature of these altered proteins.

Q. It is often assumed that since stomach acid breaks down or “denatures” proteins that the denaturation of protein is no big deal.  Why are the denatured proteins from protein powders and high-heat-treated beverages uniquely harmful?

A. While stomach acid does break down, or denature proteins to facilitate their absorption, some industrial and cooking processes (e.g., spray-drying of protein powder, extrusion of breakfast cereals, high-heat cooking and pastuerization) create unique protein-based structures (not just proteins broken down into their constituent amino acids).  In addition, these processes also create unique protein structures which are likely not to be broken down by stomach acid. Glycation products formed when proteins chemically combine with sugars and fats, for example, are increasingly being seen as a significant factor in aging and disease – the reason is likely to be precisely because the most toxic of them are unable to be broken down by stomach acids.

Unlike native, undenatured proteins (protein which the body recognizes as nutritive), these foreign protein–containing substances are apt to be poorly utilized and absorbed.  And if proteins aren’t absorbed properly, they don’t simply pass through the body unscathed. Rather, in their journey through our digestive tract, altered proteins are likely to be fermented into various other toxic compounds such as phenols, cresols, indoles, amines and ammonia by the bacteria which inhabit the colon (the vast majority of digestible protein is absorbed in the small intestine, and never makes it to the colon).

This is one reason why so many protein supplements (including many of the lower–quality whey protein supplements) often cause gas, bloating, cramping, or an upset stomach – this phenomenon is likely due to the fermentation of glycated proteins by colonic bacteria, and is not simply due to lactose intolerance as some people believe.

Because they support the growth of pathogenic colonic bacteria, denatured and glycated proteins can represent a unique toxic burden:

Study Link – p–cresol: a toxin revealing many neglected but relevant aspects of uraemic toxicity.

Quote from the above study:

P–Cresol is an end–product of protein breakdown, and an increase of the nutritional protein load in healthy individuals results in enhanced generation and urinary excretion. The serum p–cresol concentration in uraemic patients can be decreased by changing to a low–protein diet. p–Cresol is one of the metabolites of the amino acid tyrosine, and to a certain extent also of phenylalanine, which are converted to 4–hydroxyphenylacetic acid by intestinal bacteria, before being decarboxylated to p–cresol (putrefaction).

The action of intestinal bacteria on proteins (especially overly–processed, altered, and poorly absorbed proteins) may explain why the consumption of certain protein–rich foods (processed meat, for example) has often been implicated in the development of colon cancer:

Study Link – Meat Consumption and Risk of Colorectal Cancer.

Quote from the above study:

Our results demonstrate the potential value of examining long–term meat consumption in assessing cancer risk and strengthen the evidence that prolonged high consumption of red and processed meat may increase the risk of cancer in the distal portion of the large intestine.

But despite the implication of some vegetarians that meats are the sole source of such protein–derived toxins, it seems that many overly processed, extensively heated, or denatured proteins are apt to produce significant amounts of toxic byproducts in the intestines. The following study found that extensively heat–treated (thermolyzed) casein, egg white, and soy proteins (the kinds of protein sources commonly found in dietary supplements) all caused a marked increase in the production of protein–derived intestinal toxins:

Study Link – Colonic Protein Fermentation and Promotion of Colon Carcinogenesis by Thermolyzed Casein.

Quote from the above study:

We found that the thermolysis of casein reduces its digestibility and increases colonic protein fermentation, as assessed by fecal ammonium and urinary phenol, cresol, and indol–3–ol. Thermolysis of two other proteins, soy and egg white protein, also increases colonic protein fermentation with increased fecal ammonia and urinary phenols.

Although the heat–treated proteins didn’t lead to the development of colon cancer in the above study (which actually surprised the researchers), the formation of toxic byproducts was significantly increased in animals who consumed the heat–treated protein supplements.

Studies by other researchers have shown that heat–treated casein does, indeed, lead to the production of aberrant crypt foci (ACF) – well–known precursors to colon cancer development:

Study Link – Promotion of aberrant crypt foci and cancer in rat colon by thermolyzed protein.

Quote from the above study:

Thermolyzed casein promotes early colonic precursor lesions in a dose–dependent and thermolysis time–dependent manner; thermolyzed casein also promotes colon cancer.

Researchers have also found that feeding mice and rats cooked combinations of casein, sugar, and fat led to the formation of microadenomas in the colon (microadenomas are small tumors, a step closer to colon cancer development than aberrant crypt foci):

Study Link – Promotion of Colonic Microadenoma Growth in Mice and Rats Fed Cooked Sugar or Cooked Casein and Fat.

Quote from the above study:

. . .a diet containing 20% of cooked sucrose, or 40% of casein and beef tallow cooked together, promotes the growth of colonic microadenomas in initiated mice and rats, and would appear to contain promoters for colon cancer.

Given the above study, it’s truly frightening to note that one of the most popular ready–to–drink protein shakes currently is a “muscle milkshake” which contains particularly high amounts of casein, sugar, and fat.  These drinks are shelf-stable (i.e, they don’t require refrigeration) which indicates that they are high-heat/UHT processed - yet it’s doubtful that the millions of people consuming this drink have the faintest idea that they may be dramatically increasing their risk of colon cancer in the process.

With regard to protein-containing foods, the existing research lends support to the idea of choosing those which are “minimally processed.”  Along these same lines, ideal protein supplements (which are significantly processed, by definition) would be those produced specifically to maintain nutritional value, and the integrity of the protein structure. 

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February 11, 2012

Whey Protein Q&A - Whey Protein Isolate Versus Whey Protein Concentrate Part 1 - Oxidized Cholesterol

BlogProQACQ. How is Whey Protein Isolate different from Whey Protein Concentrate?

A. Whey protein concentrate contains between 34% and 80% protein, and contains relatively high levels of lactose, fat, and cholesterol.  Whey protein isolate, on the other hand, contains 90% or greater protein by weight, and negligible levels of lactose, fat, and cholesterol.

Because whey protein concentrates are often used as filler ingredients in animal feed, baked goods, and processed dairy products, great care is often not taken to protect the delicate whey protein structures in the production of whey protein concentrate.  As a result, high levels of denatured and glycated proteins are often formed when whey protein concentrate is produced.

These denatured and glycated proteins (i.e., altered protein structures, and altered protein structures formed when proteins interact with sugars and lipids) greatly compromise the nutritional quality of whey protein concentrate, and may even prove harmful.

Properly-prepared whey protein isolates, on the other hand, are produced using selective filters which rid the product of essentially all denatured and glycated proteins (as well as lactose, fat, and cholesterol).  These are just some of the reasons why, we feel, a properly-prepared whey protein isolate is the only intelligent option for use in whey protein nutritional supplements.

Note: Not all whey protein isolates offer the full benefits of filtered whey isolates – whey isolates produced by the ion exchange method, for example, lack an important whey microfraction called glycomacropeptide.  Additionally, some whey concentrates may be produced so as to minimize the formation of denatured proteins – these whey concentrates, however, would still contain lactose, fat, and most importantly, cholesterol – which is prone to oxidation during the shelf life of the powder.

Q. What is oxidized cholesterol, and what are its health effects?

A. When a cholesterol molecule interacts with oxygen, oxidized cholesterol may be formed.  While unoxidized, or native cholesterol is an important substance needed for the building of cellular structure and hormone synthesis, oxidized cholesterol is metabolized differently, and may be a unique contributor to heart disease and other types of metabolic and hormonal disruption.

Oxidized cholesterol, for example, has been implicated in the development of atherogenesis – the thickening of the arterial wall due to the build-up of fatty material – in other words, the beginning of the clogged arteries of heart disease:

Study Link - Atherogenic effect of oxidized products of cholesterol.

Quote from the above study:

Cholesterol under certain in vitro and possibly in vivo conditions may be oxidized to oxysterols, which are suspected of being initiators of atherosclerotic plaques… Dietary oxysterols are absorbed in the gastrointestinal tract and are selectively transported by the athrogenic lipoproteins LDL and VLDL. The oxysterols cholestanetriol and 25-OH cholesterol have been shown to be atherogenic. Oxysterols are commonly found in dried egg products, powdered milk, cheeses and in a variety of high temperature dried animal products.

As the above study indicates, cholesterol can oxidize inside our body, but it can also oxidize in the foods we eat.  While fresh cholesterol-containing foods, cooked normally, contain relatively low levels of oxidized cholesterol, cholesterol-containing dried, powdered, and “shelf-stable” foods are apt to contain relatively high levels of oxidized cholesterol.  This includes foods such as powdered eggs, powdered milk, powdered cheese, and whey protein concentrate.

Studies have shown that the oxidized cholesterol in such foods is absorbed and is taken up by the cholesterol-carrying lipoproteins, leading researchers to note that dietary sources of oxidized cholesterol may be unique contributors to atherosclerosis:

Study Link - Oxidized cholesterol in the diet is a source of oxidized lipoproteins in human serum.

Quote from the above study:

It is possible that oxidized cholesterol in the diet accelerates atherosclerosis by increasing oxidized cholesterol levels in circulating LDL and chylomicron remnants.

Because the formation of cholesterol oxides is inevitable in any powdered product which contains cholesterol, we feel that all cholesterol-containing powders (and many products made from them, like ready-to-drink protein shakes) should be avoided by any health-conscious consumer.

Studies have found, for example, that the formation of cholesterol oxides in dairy powders steadily increases during the shelf life of the powders – even when the products are stored sealed at room temperature:

Study Link - Determination of Cholesterol Oxides in Dairy Products. Effect of Storage Conditions.

Cholesterol oxidation is likely to be an even greater problem with many ready-to-drink protein shakes which are made with whey protein concentrate powder – and which are then pasteurized at high temperatures, often in the presence of oxidizing agents like unsaturated fats and minerals such as copper and iron.

Ultimately, it’s clear that oxidized cholesterol is metabolized in a fundamentally different way relative to native cholesterol, and is likely to be significantly harmful as a result. 

FamilyShot2013




February 01, 2012

Whey Protein Q&A - Whey Protein And Weight Loss

BlogProQAC Q. Can whey protein help with weight loss?

A. Whey protein is likely to have particular benefits for people looking to lose weight.  Out of the three macronutrients (protein, carbohydrate, and fat), protein is known to suppress appetite the most.  And while this is true for pretty much any protein source, whey protein may assist weight loss for several additional reasons.

The authors of the scholarly article below note that calcium, branched-chain amino acids (which whey contains in abundance), and unique whey peptides are all likely to make whey protein a powerful tool for weight management:

Study link - Role of whey protein and whey components in weight management and energy metabolism.

Quote from the above study:

…the anti-obesity effect [of whey] appears to result from calcium, high proportion of branched chain amino acids, and specific bioactive whey-derived peptides.

Whey protein has also been shown to reduce appetite particularly well – and the whey microfraction called glycomacropeptide (GMP) may be an important factor in this effect.  Studies have found that consuming whey proteins which contained GMP at breakfast led to reduced caloric intake at subsequent meals, relative to consuming whey proteins without GMP:

Study Link - Effects of complete whey-protein breakfasts versus whey without GMP-breakfasts on energy intake and satiety.

Quote from the above study:

[Energy intake] at lunch was lower after whey than after whey without GMP…GMP as a whey–fraction reduced energy intake coinciding with increased concentrations of certain amino acids, irrespective of the concentration of whey–protein. Although between different concentrations of whey–protein differences in hormone responses were observed, these were unrelated to satiety ratings or energy intake.

A recent study published in the Journal of Nutrition found that the long-term consumption of whey protein was associated with lower body weight and lower body fat mass in overweight and obese adults.

The study subjects consumed 56 grams of either whey or soy protein daily, or an equal amount of calories as carbohydrates.  The participants otherwise consumed their normal diets.  After 23 weeks of supplementation, the fat mass of those consuming whey protein was 2.3 kilograms (just over 5 pounds) less than those consuming an equal amount of calories as carbohydrates. 

Study Link – Whey Protein but Not Soy Protein Supplementation Alters Body Weight and Composition in Free-Living Overweight and Obese Adults.

Quote from the above study:

In this study in which energy restriction was not part of the intervention, changes in body weight and composition were small but nevertheless suggest that habitual consumption of supplemental protein may result in improved body composition and incremental, but ultimately significant, weight loss. These data suggest that supplemental dietary protein may reduce the risk of unhealthy weight gain observed in many populations (i.e. 500–1000 g/y).

An interesting aspect of the above study was that the subjects consuming whey protein lost weight and fat mass without consciously restricting calories. 

Similar studies have found that whey protein may allow dieters to not only lose weight, but to maintain significant muscle mass while dieting – an important aspect of long-term dieting success:

Study Link - A whey-protein supplement increases fat loss and spares lean muscle in obese subjects: a randomized human clinical study.

In all, quality whey protein is likely to be an important part of any weight-management program.

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January 30, 2012

Whey Protein Q&A - Whey Protein's Unique Benefits

BlogProQAC In recent years, protein powders and protein-fortified drinks and food bars have become increasingly common staples of many people’s diets.  While a select few of these products may have nutritional benefits, many may actually do more harm than good.  In this series of Q & A articles, we’ll see how to choose protein supplements that are actually health-promoting (such as undenatured whey protein isolate).  We’ll also see exactly how to use such protein supplements to achieve maximal benefit for growth, repair, recovery, and optimal health.

Q. What is Whey?

A. Whey is the watery part of milk separated from curds during the making of cheese.  Sweet dairy whey, which is the raw precipitate from cheddar-type cheeses, contains quite a bit of lactose and fat – and relatively small amounts of protein.  Where whey was originally thought of as a mere waste product, the dairy industry often sold powdered whey for use as a cheap animal feed, but researchers eventually found that the protein portion of whey (if protected from denaturation/damage by careful extraction methods) had potentially remarkable health benefits for humans.

Q. What is Whey Protein?

A. The small amount of protein in whey is greatly concentrated when water, lipids, and lactose are removed – the resultant product is known as whey protein.  Different whey proteins may contain anywhere from 34% to over 90% protein by weight depending upon how they’re processed.

The term whey protein doesn’t just refer to one type of protein, but actually encompasses many different subtypes of protein collectively called microfrations.  Research has found that each of whey’s microfractions imparts unique and often powerfully health-promoting benefits.  Whey protein microfractions include:

Beta-Lactoglobulin

Alpha-Lactalbumin

Glycomacropeptide

Bovine Serum Albumin

Immunoglobulins

Lactoferrin

Not all whey protein products, however, contain the full array of whey’s microfractions.  Many of the most health-promoting microfractions are often damaged in the production of whey protein powders, and some whey protein production methods (e.g., the ion-exchange method) are unable to extract the full gamut of whey’s microfractions. Ultimately, only products which are produced using low temperatures and selective filters are capable of delivering the full array of undenatured and active whey proteins.

Q. How is whey protein different than the protein in foods such as eggs, chicken, or beef?

A. The protein found in eggs, chicken, and beef is generally high quality, but because of whey’s unique composition, properly-prepared whey protein is capable of offering benefits above and beyond other such protein-containing foods.  For starters, whey protein is the richest source of key muscle-building amino acids such as leucine – likely a major reason why whey protein is unsurpassed in supporting muscle growth and repair. 

But, whey protein’s benefits aren’t solely due to its amino acid composition.  Whey’s unique microfractions have functional benefits above and beyond being a source of the amino acids which make up the body’s tissues and enzymes.  These microfractions, for example, may support immune function and cellular detoxification.  Several whey microfractions have been shown to support the growth of healthy bacteria in the intestines (meaning that whey protein may support digestive health, appetite suppression and weight loss).  Certain whey peptides may support healthy blood pressure, and whey protein has also been shown to support the proper metabolism and storage of carbohydrates, thus supporting healthy blood sugar levels.

In all, whey protein is far more than just a “building block” for the body’s tissues – it may support both the structure and function of our body’s cells like no other protein available.

Q. Research shows that, for all its shortcomings, the standard American diet contains sufficient protein.  Even athletes can easily meet their elevated protein requirements with readily-available foods.  Why should people consider taking a whey protein supplement?

A. Properly-prepared, undenatured whey protein is likely to offer unique benefits above and beyond those of other protein sources.  While most sources of protein such as beef, chicken, and eggs simply supply amino acids for growth and repair of the body’s tissues, the unique peptides in undenatured whey protein impart numerous biological benefits involving immunity, antioxidant status, healthy blood sugar, bone health, blood pressure, and digestive health to name just a few.  Because of its far-reaching effects, whey protein is far more than just a means to add additional protein to the diet, and even those whose diet already contains sufficient protein can still benefit from adding undenatured whey protein.

For example, unique sulfur-containing peptides in whey may be able to enhance the production of the cellular antioxidant and detoxifier known as glutathione.  Glutathione plays an important role in the immune system and in the proper growth and repair of the body’s cells.  Numerous studies show that whey protein may be able to enhance glutathione levels in those with compromised immune systems (including athletes):

Study Link - Whole blood and mononuclear cell glutathione response to dietary whey protein supplementation in sedentary and trained male human subjects.

Quote from the above study:

The aerobic training period resulted in significantly lower glutathione concentrations in whole blood, an effect that was mitigated by WPI [Whey Protein Isolate] supplementation. A significant increase in mononuclear cell glutathione was also observed in subjects receiving the WPI supplement following the 40 km simulated cycling trial.

Study Link - Oral supplementation with whey proteins increases plasma glutathione levels of HIV-infected patients.

Quote from the above study:

In glutathione-deficient patients with advanced HIV-infection, short-term oral supplementation with whey proteins increases plasma glutathione levels.

Study Link - Improved glutathione status in young adult patients with cystic fibrosis supplemented with whey protein.

Studies have also found that, unlike casein protein (another protein in milk), whey protein may support healthy blood lipids, insulin, and blood pressure levels in overweight and obese individuals:

Study Link - Effects of whey protein isolate on body composition, lipids, insulin and glucose in overweight and obese individuals.

Quote from the above study:

The present study demonstrated that supplementation with whey proteins improves fasting lipids and insulin levels in overweight and obese individuals.

Study Link - The chronic effects of whey proteins on blood pressure, vascular function, and inflammatory markers in overweight individuals.

Quote from the above study:

This study demonstrated that supplementation with whey protein improves blood pressure and vascular function in overweight and obese individuals.

The whey microfraction, gycomacropeptide, may exert its wide-ranging biological effects via its ability to support healthy bacterial populations in the intestines.  Such an effect could lead not only to appetite reduction, but to benefits for digestive, and overall health.

In research published in the Journal of Nutrition, for example, researchers from the University of Granada School of Pharmacy found that Glycomacropeptide was able to reduce intestinal inflammation on par with anti-inflammatory drugs in a rat model of chemically-induced colitis:

Study Link - Bovine Glycomacropeptide Is Anti-Inflammatory in Rats with Hapten-Induced Colitis

Quote from the above study:

The magnitude of the anti-inflammatory effect was generally comparable to that of sulfasalazine, an established drug used in the treatment of inflammatory bowel disease.

Recently, researchers have found that whey protein may possess the unique ability to stimulate bone–building cells, called osteoblasts, while at the same time reducing bone resorption, or, the breaking down of bone:

Study Link – Effect of whey protein on the proliferation and differentiation of osteoblasts.

Quote from the above study:

This study establishes whey protein as a potent novel anabolic factor in osteoblasts, and which also reduces bone resorption.

And though the above study was conducted in vitro, animal and human studies have also shown various whey proteins to offer bone–building benefits above and beyond other types of protein. The following study, for example, found that rats fed small amounts of whey protein had higher levels of bone–specific proteins and stronger bones than those fed exclusively casein:

Study Link – Effects of whey protein on calcium and bone metabolism in ovariectomized rats.

Quote from the above study:

These data indicate that the milk whey protein influence in OVX rats is an increase in bone proteins such as collagen and enhanced bone–breaking energy.

Whey protein may also offer unique benefits for regulating blood sugar.  Because of the unique proteins it contains, whey protein in insulinogenic – meaning, that it facilitates the release of insulin and thus aids in the storage and utilization of carbohydrates.

Human studies have shown that mixtures of whey and casein protein combined with carbohydrates led to significantly greater rates of glycogen storage relative to either carbohydrate or protein alone:

Study Link - Carbohydrate-protein complex increases the rate of muscle glycogen storage after exercise.

Quote from the above study:

The rate of muscle glycogen storage during the CHO-PRO treatment [35.5 +/- 3.3 (SE) mumol.g protein-1.h-1] was significantly faster than during the CHO treatment (25.6 +/- 2.3 mumol.g protein-1.h-1), which was significantly faster than during the PRO treatment (7.6 +/- 1.4 mumol.g protein-1.h-1). The results suggest that postexercise muscle glycogen storage can be enhanced with a carbohydrate-protein supplement as a result of the interaction of carbohydrate and protein on insulin secretion.

Subsequent animal studies have found that whey protein (more so than casein) is uniquely responsible for increasing glycogen levels after exercise.  Such research gives us important clues as to how to use whey protein to maximize exercise recovery – a topic we’ll cover later in this Q&A.

Study Link - Dietary whey protein increases liver and skeletal muscle glycogen levels in exercise-trained rats.

Quote from the above study:

Total glycogen synthase activity in the skeletal muscle in the whey protein group was significantly higher than that in the casein group. The present study is the first to demonstrate that a diet based on whey protein may increase glycogen content in liver and skeletal muscle of exercise-trained rats.

An excess of iron is a common cause of the oxidative stress and free radical production found in aging and disease.  The iron-binding whey microfraction, called lactoferrin, has been associated with numerous health benefits, and It’s likely that lactoferrin may help our bodies use iron safely and efficiently:

Study Link - Milk whey protein decreases oxygen free radical production in a murine model of chronic iron-overload cardiomyopathy.

To be continued...

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April 27, 2011

Whey Protein Enhances Muscle and Liver Glycogen Storage – Implications For Muscle Growth and Exercise Recovery.

WorkoutCurl Even in academic circles, dietary protein is often simplistically viewed as a mere source of amino acid “building blocks” for the body’s tissues and enzymes.  Decades’ worth of research clearly shows, however, that certain food proteins and peptides exert remarkable biological effects independent of their role in forming the structural material of tissues and enzymes.

Dairy proteins – and whey proteins in particular – happen to be among the richest sources of such bioactive peptides.  In previous Integrated Supplements Blog articles, for example, we’ve examined how the potent antioxidant activity of whey’s cysteine-containing peptides may be of unique benefit in conditions characterized by oxidative stress such as diabetes:

Select Studies on Whey Protein - Whey Protein, Blood Sugar, and Oxidative Stress

We’ve seen how the iron-binding properties of whey’s lactoferrin peptide may protect against iron-induced oxidative damage:

Select Studies on Whey Protein - Whey Protein Protects Against The Toxic Effects Of Iron

And, we’ve seen how the whey peptide called glycomacropeptide may suppress appetite, ultimately leading to reduced caloric intake:

Study Finds Whey Protein Containing Glycomacropeptide Leads To Reduced Calorie Consumption

As it turns out, even the muscle-building properties of whey protein aren’t solely due to protein’s role as a structural component of muscle tissue.  Whey protein may have the unique ability to facilitate the uptake and storage of carbohydrate in the body’s cells – thus creating the optimal environment for exercise recovery and muscle growth.

Muscle and Liver Glycogen – Keys to Exercise Performance, Recovery, and Muscle Building

Glycogen is the storage form of carbohydrate found in the body’s cells.  When energy demands are taxed – as they are in intense exercise – levels of muscle glycogen and the “emergency reserve” of liver glycogen become drained.  In this scenario, not only does performance suffer (glycogen depletion is thought to be a major factor in the fatigue of endurance athletes, for example), but recovery from training is hindered as well.  This is why the muscle-building effects of weight training are often hindered by inadequate nutrition.  In other words, no matter how much protein is consumed, muscle protein synthesis (i.e., muscle growth) simply cannot occur optimally until glycogen stores are replenished.

In fact, monitoring the level of liver glycogen may be a fundamental way in which the body gauges a fed state (i.e., a metabolic environment suitable for growth and repair).  When liver glycogen is low, the body may elicit the adrenaline-driven “fight-or-flight” response which converts structural (e.g., muscle) proteins into fuel sources – obviously, not the ideal situation for muscle growth. 

Note – the role of liver glycogen as a signal of the fed state is outlined in our article:

A Diet For Long-Term Weight Control And Optimal Health - Part 2 - The True Role of Sugar in Weight Gain, Diabetes, and Metabolic Syndrome

Whey Protein Increases Glycogen Levels

Recent research has shown that whey protein may be unique among protein sources in facilitating the uptake and storage of muscle and liver glycogen.

Human studies have shown that mixtures of whey and casein protein combined with carbohydrates led to significantly greater rates of glycogen storage relative to either carbohydrate or protein alone:

Study Link - Carbohydrate-protein complex increases the rate of muscle glycogen storage after exercise.

Quote from the above study:

The rate of muscle glycogen storage during the CHO-PRO treatment [35.5 +/- 3.3 (SE) mumol.g protein-1.h-1] was significantly faster than during the CHO treatment (25.6 +/- 2.3 mumol.g protein-1.h-1), which was significantly faster than during the PRO treatment (7.6 +/- 1.4 mumol.g protein-1.h-1). The results suggest that postexercise muscle glycogen storage can be enhanced with a carbohydrate-protein supplement as a result of the interaction of carbohydrate and protein on insulin secretion.

Subsequent animal studies have found that whey protein (more so than casein) is uniquely responsible for increasing glycogen levels after exercise.

Study Link - Dietary whey protein increases liver and skeletal muscle glycogen levels in exercise-trained rats.

Quote from the above study:

Total glycogen synthase activity in the skeletal muscle in the whey protein group was significantly higher than that in the casein group. The present study is the first to demonstrate that a diet based on whey protein may increase glycogen content in liver and skeletal muscle of exercise-trained rats. 


In all, it seems that whey protein along with a source of carbohydrates (including some fructose) – consumed either before or after workouts – is the ideal way to maximize the muscle-building effects of exercise.

Ideally, the whey protein chosen will contain the full spectrum of whey’s bioactive peptides, be all-natural, and free of residual amounts of cholesterol – as is Integrated Supplements CFM® Whey Protein Isolate.

Related Articles:

Building The Perfect Workout Drink With Whey Protein Isolate

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April 10, 2008

Select Studies on Whey Protein - Whey Protein, Blood Sugar, and Oxidative Stress

Blood_sugar72In keeping with our recent theme of oxidative stress and aging, it seems that yet another disorder in which oxidative stress plays a particularly major and multi-faceted role is diabetes.

It’s important to clear up any misconceptions right from the beginning – diabetes is not simply a disease of altered carbohydrate and sugar metabolism as many people think. As research accumulates, it’s becoming well-recognized that diabetes, although it obviously involves faulty blood sugar regulation, would be more precisely classified as fundamentally a disease of oxidative stress.

In other words, oxidative stress is now thought to be the primary underlying cause of faulty blood sugar regulation in diabetes. When we reduce our levels of oxidative stress, our blood sugar naturally tends to normalize.

Study Link - Diabetes, oxidative stress, and antioxidants: a review.

Increasing evidence in both experimental and clinical studies suggests that oxidative stress plays a major role in the pathogenesis of both types of diabetes mellitus.

Diabetes Is Deadly

With how frighteningly common diabetes has become, it’s important for us to recognize how profoundly dangerous and life threatening diabetes can be. Left uncorrected, a chronically elevated level of blood sugar will eventually damage virtually every organ system and function of the body. In diabetes, the cellular damage characteristic of oxidative stress is known to ultimately manifest as extensive damage to the tissues of:

The eyes, (often resulting in blindness)

The blood vessels (often resulting in heart disease, and even sexual dysfunction)

The kidneys (called diabetic nephropathy, often requiring dialysis or a kidney transplant)

And:

Foot ulcers (caused by nerve damage called diabetic neuropathy – often requiring amputation)

With the extensive damage diabetes can cause, finding safe and effective ways of reducing our burden of oxidative stress should be a first priority for any health-conscious person looking to avoid the ravages of the disease.

Not coincidentally, research is beginning to indicate that reducing oxidative stress via stimulating the production of glutathione may be one of the most important keys to healthy blood sugar metabolism:

Study Link - Meal cysteine improves postprandial glucose control in rats fed a high-sucrose meal

Dietary cysteine alleviates sucrose-induced oxidative stress and insulin resistance

Diets that promote oxidative stress favor impairment in glucose homeostasis. In this context, increasing the cysteine intake may be beneficial by maintaining glutathione status. . . Of great interest was the observation that all beneficial effects of cysteine supplementation were duplicated by the consumption of a cysteine-rich protein. These data show that increasing the cysteine intake limits [sugar]-induced impairment of glucose homeostasis and suggest that these effects are mediated by a reduction in oxidative stress.

In the above studies, whey protein was able to improve glucose control, and reduce oxidative stress in rats given high-sugar diets.

And of course, as we’ve shown you before, Integrated Supplements CFM® Whey Protein Isolate is among the richest sources of glutathione-boosting compounds including cysteine and glutamylcysteine.

By itself, it’s certainly premature to say that whey protein will be able to treat or prevent diabetes (remember, supplements by themselves should never be expected to treat, cure, or prevent any disease), but as part of a healthy diet and lifestyle, whey protein isolate may very well be a sound nutritional choice for anyone looking to support a healthy blood sugar through the production of glutathione.

Other Factors


As we’ve showed you in recent editions of the Integrated Supplements Newsletter and blog, other major dietary factors contributing to oxidative stress include excessive amounts of unsaturated fats, oxidized cholesterol, and iron.

Those looking for a comprehensive approach to reducing oxidative stress, may want to read the following articles and Blog posts to get up to speed.

Newsletters:

Rancid Fats and Oxidative Stress - Strategies To Reverse Aging - Part 1

Combating Oxidative Stress - Strategies to Reverse Aging - Part 2

The Anti-Aging Diet Part 1 - Can Some Foods Accelerate Aging?

The Anti-Aging Diet Part 2 - The Dark Side of Iron

The Anti-Aging Diet Part 3 - Solving The Puzzle of Iron

Blog Posts:

Select Studies on Whey Protein - Whey Protein Protects Against The Toxic Effects Of Iron

Oxidative Stress And Exercise - Too Much of a "Good Thing"

How To Combat The REAL Risk Factor For Heart Disease And Aging

Studies Find Antioxidants Harmful. Well, Sort Of.

And, of course, stay tuned here for more.

BottleGroup

April 05, 2007

Study Finds Oxidized Cholesterol In All Dairy Powders Tested - Levels Increased With Storage

ProteinScoopWhen a cholesterol molecule interacts with oxygen, oxidized cholesterol may be formed.  While unoxidized, or native cholesterol is an important substance needed for the building of cellular structure and hormone synthesis, oxidized cholesterol is metabolized differently, and may be a unique contributor to heart disease and other types of metabolic and hormonal disruption.

Oxidized cholesterol, for example, has been implicated in the development of atherogenesis – the thickening of the arterial wall due to the build-up of fatty material – in other words, the beginning of the clogged arteries of heart disease:

Study Link - Atherogenic effect of oxidized products of cholesterol.

Quote from the above study:

Cholesterol under certain in vitro and possibly in vivo conditions may be oxidized to oxysterols, which are suspected of being initiators of atherosclerotic plaques… Dietary oxysterols are absorbed in the gastrointestinal tract and are selectively transported by the athrogenic lipoproteins LDL and VLDL. The oxysterols cholestanetriol and 25-OH cholesterol have been shown to be atherogenic. Oxysterols are commonly found in dried egg products, powdered milk, cheeses and in a variety of high temperature dried animal products.

As the above study indicates, cholesterol can oxidize inside our body, but it can also oxidize in the foods we eat.  While fresh cholesterol-containing foods, cooked normally, contain relatively low levels of oxidized cholesterol, cholesterol-containing dried, powdered, and “shelf-stable” foods are apt to contain relatively high levels of oxidized cholesterol.  This includes foods such as powdered eggs, powdered milk, powdered cheese, and whey protein concentrate.

Studies have shown that the oxidized cholesterol in such foods is absorbed and is taken up by the cholesterol-carrying lipoproteins, leading researchers to note that dietary sources of oxidized cholesterol may be unique contributors to atherosclerosis:

Study Link - Oxidized cholesterol in the diet is a source of oxidized lipoproteins in human serum.

Quote from the above study:

It is possible that oxidized cholesterol in the diet accelerates atherosclerosis by increasing oxidized cholesterol levels in circulating LDL and chylomicron remnants.

So, the existing research clearly implicates oxidized cholesterol as a contributing factor to the atherosclerotic plaque of heart disease.  The research also shows that oxidized cholesterol is able to be absorbed from the foods we eat and is taken up as part of the LDL particle.  It’s logical to wonder, therefore: how much oxidized cholesterol is actually in the foods we eat?

Oxidized Cholesterol in Protein Powders

Ironically, many supposedly health-conscious people may be consuming particularly high levels of oxidized cholesterol.  Some dairy powders – especially whey protein concentrate used in many protein drinks and sports supplements – contain remarkably high levels of cholesterol.  Because it’s a relatively cheap source of protein (relative to higher-quality whey isolates), supplement companies often use high amounts of whey concentrate in their formulations.  As such, it’s not uncommon for a serving of a whey-concentrate-based protein powder to contain 20, 30, 40, or even more milligrams of cholesterol per serving.

Researchers who have studied the formation of cholesterol oxides in such dairy powders have found their level to increase in relationship to the amount of time the product was stored:

Study Link - Determination of Cholesterol Oxides in Dairy Products. Effect of Storage Conditions.

Quote from the above study:

We also observed a relationship between storage time and cholesterol oxide generation.

In the above study, cholesterol oxide generation increased steadily even when the products were stored sealed at room temperature.

Time In Storage is The Key

It’s important to note that oxidized cholesterol generally wasn’t formed when these dairy powders were produced – even though the dairy from which they came was pasteurized, and they were exposed to additional heat and oxygen during the production of the powders.  The real driver of cholesterol oxidation was time in storage.  For this reason, it’s safe to assume that cholesterol oxidation will occur over time in any cholesterol-containing powder regardless of how (or at what temperature) the powder was produced.  This includes whey concentrate products marketed as organic, or from grass-fed cows, etc.  If there’s cholesterol in a powder, there’s simply no viable way to prevent its continual oxidation during the shelf life of the product.

This is why we at Integrated Supplements have advocated products made exclusively with ceramic-filtered CFM whey isolate.  This is a process by which whey protein is rid of essentially all cholesterol and lactose, and which maintains the integrity of all delicate whey microfractions.

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