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2 posts from March 2012

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.


March 03, 2012

Whey Protein Q&A - Whey Protein Isolate Versus Whey Protein Concentrate Part 3 - Glycation Products in Protein Supplements

BlogProQAC Q. What are glycation products?

A. Glycation products are altered protein structures resulting from the chemical interaction of proteins, sugars, and fats.  Glycation products can be produced both in our foods and in our bodies as well.  When the chemical changes proceed far enough, the resulting structures are called advanced glycation endproducts, or, AGEs, for short. Various glycation products and AGEs have been found to be consistently elevated in the body under conditions of aging and disease.

For example, a particular glycation product, called furosine, has been shown to be elevated in patients with Alzheimer’s disease and diabetes:

Study Link – Plasma protein glycation in Alzheimer's disease.

Quote from the above study:

Recent studies have suggested that formation of advanced glycation end–products (AGEs) in some brain proteins could be associated with Alzheimer's disease…Protein glycation was evaluated in plasma with a highly specific HPLC–UV technique, using furosine, which is the acid hydrolysis product of epsilon–deoxy–fructosyl–lysine Plasma furosine was almost two times higher in subjects with Alzheimer's disease (p<.005) than in controls, but still 50% lower than in diabetic patients (P<.02).

And similar to the glycation phenomenon which occurs in our body under the conditions of aging, certain types of food processing are known to result in the production of high amounts of furosine as well. 

As relates specifically to protein powders, the following study tested the furosine content of several commercially available sports supplements produced using milk based ingredients like whey protein isolate, whey protein concentrate, and casein. The furosine levels the researchers found was shockingly high in products which contained whey protein concentrate:

Study Link – Assessing nutritional quality of milk–based sport supplements as determined by furosine.

Quote from the above study:

Furosine content ranged from 2.8 to 1125.7 mg/100 g protein in commercial sport supplements being usually lower in samples containing mainly whey protein isolates or casein, as compared with whey protein concentrates. It is estimated that 0.1–36.7% of the lysine content is not available in this type of products. The use of high quality ingredients for the manufacture of sport supplements reveals important, since it could be the major source of protein intake of certain group of consumers in high or moderate training regime. Furosine is an appropriate indicator to estimate the nutritional quality of sport supplements. A reference value of 70 mg furosine/100 g protein content in dried sport supplements could be set up for controlling the quality of milk–based ingredients used in the formulation. Samples with higher levels are suspected of use of low quality milk–based ingredients or inappropriate storage conditions.

Knowing that glycation products formed in our body may be partly responsible for the degenerative effects of aging, and knowing that glycation products have repeatedly been associated with various degenerative diseases, it’s logical to think that perhaps eating these same glycated proteins may not be such a great idea if we value our long–term health.

Q.  It’s often assumed that high protein intakes aren’t particularly harmful because the body will simply rid itself of the excess.  Is this true?

A.  Some proteins which have been altered by the industrial processes we’ve been describing are likely to have vastly different toxicity profiles relative to minimally-processed protein foods.  In other words, high protein intakes, per se, aren’t likely to be problematic, but high amounts of protein supplements and industrially-processed proteins may be. 

As a bit of background, mainstream nutritionists and doctors often maintain that the average American diet contains sufficient (and, perhaps, too much) protein, and that even the protein requirements of hard-training athletes are only slightly above those of sedentary individuals.  These same experts sometimes also warn that, not only is high protein consumption unnecessary, but that excess protein intake could tax kidney function, and may, thus, actually be harmful.  The bodybuilding, fitness, and supplement communities, however, have largely ignored these warnings, citing evidence of cultures consuming high protein intakes without apparent harm. 

Slowly, some within the medical community have begun to realize that their peers may have previously underestimated the importance of protein in a healthy diet geared towards fat loss and muscle growth or maintenance.  Perhaps spurred by the low-carb and high-protein diet craze of several years ago, the value of high protein intakes has received increasing justification from the medical community.  It’s common now, in fact, to see various protein-centric diet books - and their accompanying protein-containing snack bars and concoctions - peddled by medical doctors.

But, almost universally, both the medical and fitness crowds completely ignore the uniquely toxic effects of the denatured and glycated proteins commonly found in nutritional supplements.  

As protein supplements and protein-fortified foods have become more widely used across various segments of society, it’s likely that the consumption of glycated and industrially-denatured proteins has increased commensurately.  As such, because protein supplements may have completely unique toxicity profiles relative to traditional protein-containing foods, the health effects of industrially-denatured and glycated proteins should be more widely addressed.

While the human body does possess mechanisms to rid the body of excess protein, “getting rid” of glycated proteins is exactly what the body does not do efficiently – and this is what makes many protein–based nutritional supplements uniquely toxic relative to minimally–cooked protein–rich foods.  We’ve already seen, for example, how altered protein structures may promote the growth of harmful intestinal bacteria.  In addition, eating denatured proteins and glycation products (as many users of protein powder, protein bars and ready–to–drink protein shakes unknowingly do), has been shown to add to the AGE burden of the body, and may be particularly detrimental to kidney function:

Study Link – Advanced glycation endproducts (AGEs) as uremic toxins.

Quote from the above study:

Dietary AGEs may contribute significantly to the total AGE load of the body, particularly in uremia.

So, while high intakes of food-based proteins have not been shown to impair kidney function in healthy individuals, there is significant reason to believe that high intakes of many common protein supplements may.

It has been found, for example, that eating glycated protein causes a major increase in systemic inflammation – including inflammatory disease markers such as C–reactive protein, even in healthy subjects:

Study Link – Diet–derived advanced glycation end products are major contributors to the body's AGE pool and induce inflammation in healthy subjects.

Quote from the above study:

Advanced glycation end products (AGEs) are a heterogeneous group of compounds that form continuously in the body. Their rate of endogenous formation is markedly increased in diabetes mellitus, a condition in which AGEs play a major pathological role. It is also known, however, that AGEs form during the cooking of foods, primarily as the result of the application of heat. This review focuses on the generation of AGEs during the cooking of food, the gastrointestinal absorption of these compounds, and their biological effects in vitro and in vivo. We also present preliminary evidence of a direct association between dietary AGE intake and markers of systemic inflammation such as C–reactive protein in a large group of healthy subjects. Together with previous evidence from diabetics and renal failure patients, these data suggest that dietary AGEs may play an important role in the causation of chronic diseases associated with underlying inflammation.

AGEs are also known to damage blood vessels, and many researchers have implicated AGEs as the major factors responsible for the vascular damage associated with kidney disease and diabetes. Building logically from this, some researchers have proposed a very plausible connection between the ingestion of glycation products in foods and the development of diabetes and subsequent diabetic complications like kidney disease:

Study Link – Possible link of food–derived advanced glycation end products (AGEs) to the development of diabetes.

Quote from the above study:

The formation and accumulation of advanced glycation end products (AGEs) have been known to progress at an accelerated rate under diabetes, and there is accumulating evidence that AGEs play a role in the development of diabetes by inducing islet beta cell damage and/or insulin resistance. Further, there are several animal studies to suggest that dietary AGEs are involved in insulin resistance, visceral obesity and the development of diabetes.

So, despite the common misconception that denatured and glycated proteins are merely inert, or “wasted,” the evidence is overwhelmingly clear that they are, instead, often mildly and cumulatively toxic.


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