Whey Protein Alone Won't Cover the EAA Requirements of Hard Working Athletes, Study Says. Plus: US Whey More Digestible & 88% Higher in Leucine than Brazilian Whey

Not all protein supplements are created equal. And this goes for whey supplements from different countries, too.

In their accepted manuscript for LWT - Food Science and Technology, Cristine Couto Almeida and her colleagues write: "When the calculated AAS and PDCAAS based on the suggestion for adult athletes were considered, both [US & Brazilian whey protein] supplements exhibited suboptimal score values for several EAA [... and] were unable to supply the suggested adult athlete EAA requirement" (Almeida. 2014).

Shocked? I'd hope not. I mean, you don't even know what the scientists base their conclusion on - right? So before we even try to put things into perspective, it would be wise to take a look a the design of this in vitro study.

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While the researchers from the Universidade Federal de Rio de Jaieiro acknowledge that whey protein, in general, is an effective adjunct to the diet of strength and even endurance athletes, they insist that there is too little "information regarding the WP supplement protein quality" and thus set out to "to investigate the protein quality of commercial WP supplements produced by U.S. and Brazilian companies based on in vitro digestibility (IVPD) assay, EAA, AAS and [protein digestibility-corrected amino acid] PDCAAS." (Almeida. 2014)

To this ends, the researchers acquired fifteen samples of whey protein (WP), soy protein, and caseinate isolate powder from a commercial retailer specialized on nutritional supplements. The supplements had been manufactured at different countries - eight from USA companies (WP-USA), and seven from Brazilian companies (WP-BRA). The supplements manufactured with soy protein and caseinate isolate powder were used as references in a study that yielded quite surprising results.

Figure 1: Essential amino acid composition of two commercial whey protein supplements (Almeida. 2014).

As you can see in Figure 1 the amino acid composition of the whey proteins from Brazil and the US varied significantly. The US whey, for example had significantly higher amounts of leucine, while the Brazilian whey was loaded with the essential amino acid lysine. While it is possible that the variations in the other amino acids are a result differences that were present in the milk, already, I would guess that the US whey was either openly (the scientists don't disclose the brands, otherwise I'd check) or secretly spiked with leucine to promote muscle anabolism.

Figure 2: Relative loss (%) of amino acids during simulated (in vitro) digestion in US and Brazilian whey (Almeida. 2014).

What are the numbers based on: Whether the amount of aminos is sufficient or not was calculated based on the WHO recommendation (WHO. 2007), assuming a normal (=comparatively low) protein intake.

If you consume twice the WHO suggestions for athletes, you are thus not at a risk of being deficient in any of the EAAs, but could maybe optimize the ratio of the individual amino acids by not covering your protein needs from a single protein source.

Even if we assume the latter was the case and the producer added free form amino acids to the whey, though, this does not explain the other differences, because if you add say 20g of leucine to 100g of EAA and measure the amino acid content of the 100g of your new mix, the content of all other amino acids would be lower.

 As you can easily see in Figure 1, though, this was not the case in the study at hand. Plus: There were also significant differences in the protein digestibility-corrected amino acid composition, i.e. the marker of whether or not the content of a certain essential amino acid per gram of protein was sufficient or not. In that, values <1.0 indicate there is too little of this amino acid in the mix.

Figure 3: Amino acid score and protein digestibility-corrected amino acid composition for the commercial
US and Brazilian whey supplements (Almeida. 2014).

As you can see in Figure 3, the latter was the case for threonine and valine in the US whey and for isoleucine and leucine in the whey protein from Brazil.

Figure 4: According to the standardized in vitro digestion assay (AOAC. 2012) the scientists used soy protein has by far the lowest digestibility and will thus be effectively delivering the lowest percentage of the amino acids it contains into your circulation (Almeida. 2014).

What does this mean? I must admit this sounds awful, but in practice it means only that you would end up getting your EAAs at an allegedly suboptimal ratio (I doubt we know what this ratio is, though) if you covered your complete protein needs with whey protein. In that, it is interesting that you would get too little threonine and valine form US wheys and too little leucine and isoleucine from Brazilian wheys.

Actual deficiency symptoms as you may have expected them, when you've read the statement that whey protein supplements were "unable to supply the suggested adult athlete EAA requirement" (Almeida. 2014), however are unlikely, because (a) I assume most of you won't live off whey protein as their only protein source and (b) even if you did, you would probably consume more than the WHO recommendation for athletes (WHO. 2014) that's at the heart of Almeida et al.'s calculation suggests | Comment of Facebook!

References:

• Almeida, Cristine Couto, et al. "In vitro digestibility of commercial whey protein supplements." LWT-Food Science and Technology (2014). 
• AOAC International, and George W. Latimer. Official Methods of analysis of AOAC International. AOAC International, 2012.
• Hsu, H. W., et al. "A multienzyme technique for estimating protein digestibility." Journal of Food Science 42.5 (1977): 1269-1273.
• WHO. "Protein and amino acid requirements in human nutrition." World Health Organization technical report series 935 (2007):

Licorice More Estrogenic Than Estradiol: Some of the Flavonoids in Glycyrrhiza Glabra Roots Turn Out to Be Superinductors of the Estrogen-α & -β Receptors

Image 1: In view of the fact that most confectionary licorice contains no more than ~3% of the roots of the licorice plant, I would rather bother about the tricks the ~74g of carbohydrates (on a 100g base) of this treat may play on your insulin levels than about any potential negative effects the consumption of a few or even a whole bunch of these licorice wheels may have on your testosterone levels or overall manliness ;-)

You probably have heard about licorice, the root of Glycyrrhiza glabra, a legume with a slightly sweet taste and one of the ingredient of the eponymous candy being a potent adrenal "revitalizer" that is used and advocated my many naturopathic doctors. If you frequent any of the major health and fitness boards on the Internet, you will yet also be familiar with some of its unwanted side-effects, first and foremost its scientifically validated anti-androgenic (specifically testosterone reducing) effects (Zamansoltani. 2009). While Zamansoltani et al. yet still speculated, whether the reduction in serum testosterone they observed as a result of administration of 150-300mg/kg of licorice extract (HED ~ 40-80mg/kg; 3.2-6.4g for a 80kg human) to male rats still speculated, whether these reduction were the result of "[i]ncreas[es] in T metabolism, down-regulation of androgen receptors or activation of oestrogen [sic!] receptors", a recent study that was published in the Annals of Bioanalytical Chemistry shows that the latter, i.e. the (profound!) activation of both types of estrogen receptors probably was the underlying cause of the emasculation of the licorice treated bucks (Simons. 2011).

Estrogen receptor superinductors were not invented by Dr. Spock

In a pretty meticulous analysis, Rudy Simons et al. found that several fractions of an ethyl acetate extract from licorice root displayed estrogenic activities at either the estrogen-alpha or estrogen-beta receptor that were more pronounced than the ones of the reference "drug", estradiol (E2).

Figure 1: Relative estrogenic activity (in % of estradiol = E2) of 51 fractions that were isolated from an ethyl acetate extract from licorice root (data adapted from Simons. 2011).

If you take a closer look at the 51 fractions the scientists identified by liquid chromatography-massspectrometry and analyzed for their activity by the means of yeast estrogen bioassays, you will recognize that not just one or two, but a whole host of these "fractions", which themselves were complex mixtures of similar compounds, exhibit partly profound estrogenic activity. In that it is particularly noteworthy that the superinduction (activity >E2=100%) was not caused by a post-translational stabilization of the firefly luciferase reporter enzyme, which would have disqualified these results as shortcomings of the yeast essay Simons et al. had used - a effect which has been previously described for genistein, one of the phytoestrogens in soy and soy products.

Figure 2: Relative content and estrogenic activity of individual fractions F1-F5, F6-F21 and F22-F51 from the ethyl acetate extract from licorice root used in the study (calculated based on Simons. 2011).

Of all the fractions, the scientists isolated from the licorice extract, which was supplied by Frutarom US, fraction 41 (F41) with an estrogen-alpha receptor activity of 159.9% at the low (3µg/ml) and 186.9% at the high (10µg/ml) concentrations was by far the 'worst offender'. In view of the fact that we do not know how much of these flavonoids actually make it into the bloodstream, the 103.1, 97.9, 95.5, 74.6, 68.7, 57.2 and 57.3% estrogen-beta activity of fractions F24-F30 at a much lower concentration of 0.3µg/ml is probably more of a concern and most likely the underlying cause of the anti-androgenic effects of licorice, which have also been established in a human study on seven 22-24 year old healthy male subjects by Decio Armanini et al. in 1999 (Armanini. 1999):

Figure 3: Changes in testosterone, androstenedione and 17-hydroxy-progesterone levels (ng/dl) in 7 healthy men upon oral adminstration of 7g of a commercial licorice preparation (data based on Armanini. 1999)

As you can see in figure 3, the 7 g of a commercial preparation of licorice (containing 0.5 g of glycyrrhizic acid) the men in the Amanino study received in the form of tablets (Saila, Bologna, Italy) on a daily basis had an immediate and pretty profound anti-androgenic effect (-44% total testosterone within 2 days!) resulting from the negative feedback of the phytoestrogenic components from Glycyrrhiza glabra. The levels of androstenedione and 17-hydroxy-progesterone on the other hand did not change.

Image 2: Licorice could help with menopause symptoms such as hot flashes, but it has potential corticosteroid-like side effects you should keep an eye on.

Update: Evelyn from CarbSane asked in the comment section whether licorice would not make a good addition to any natural menopause treatment. In fact, she is right that the very estrogenicity of the licorice extracts that is detrimental to men could be of great use for women going through menopause. A cursory search of the databases (how else could it be in view of the fact that you cannot patent licorice) does yet reveal that no one appears to be willing to invest serious money into studies on the effects of licorice / licorice extracts in menopausal women. Nevertheless, there is evidence for estrogen-like bone-building effects (Somjen. 2004) and a -2.4% reduction in the dreaded hot flashes over placebo (Nahidi. 2011).

Moreover, licorice appears to act as an SSRI (selective serotonine reuptake inhibitor) and may thus also help with moodswings and neurotransmitter-imbalances (Ofir. 2003), which can also cause sugar cravings and thusly induce weight gain. If you add to that the growth-inhibitory action the glabridins in licorice exhibit on breast-cancer cells (Tamir. 2000), it may be well worth to try to alleviate menopause symptoms with licorice. In that, it is yet important to know that the glycyrrhetinic acid in licorice has mineralocorticoid-like side effect (i.e. it works like cortisol), which can become problematic especially if licorice is taken as part of one of the typical pharmacological protocols conventional doctors tend to prescribe to their patients (e.g. Inada. 2007). My advice would thus be to carefully monitor your reaction, Ladies ;-)

Against the background of the results of both the initially mentioned rodent study by Zamansoltani et al. (Zamansoltani. 2009), as well as the certainly more relevant data from the 1999 study by Armanini et al. (Armanini. 1999) the 'test-tube' findings by Simons et al. gain a degree of practical significance many of the likewise bio-essay based studies, the manufacturers of purported (!) testosterone boosters like to cite to underline the scientific validity of their products, are lacking... you may want to keep that in mind before you try to counter the unwanted side-effects of a licorice-based "adrenal optimizer" by popping a few servings of the latest and greatest "scientifically proven testosterone booster" ;-)

Only Dairy, not Soy-Based Meals are Truly Anabolic: Protein Signalling Response to Complete Meals Impaired W/ Soy vs. Whey. Plus: No Response in the Obese to Either Protein

Only dairy, not soy-based lasagna will help you build muscle.

What is it that makes the latest study from the Molecular Nutrition Unit at the School of Exercise and Nutrition Sciences of the Deakin University and colleagues from the The Liggins Institute at the Faculty of Medical and Science Health of the University of Auckland different from previous studies? Actually it's more than one thing: It's the pre-packaged lasagna and fruit yogurt that was used as a test meal in a study that was designed to examine whether meals differing in amino acid composition, yet matched for total energy and macronutrient composition, result in altered mTOR signalling.

Ah, and obviously to investigate if middle aged men with MetS display a resistance of anabolic signalling to mixed meal ingestion compared with healthy control.

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The latter already tells you that the subjects of Petra Grans study were obese. Twenty 40–60 year-old men who were recruited from newspaper, poster, and flyer advertisements to participate.

The subjects were classified as having MetS based on the International Diabetes Federation criteria which means they were abdominally obese (waist circumference≥94 cm) and had two of the following health issues: raised serum triglycerides (≥1.7 mmol/l), reduced serum HDL cholesterol (<1.03 mmol/l), impaired fasting glycaemia (fasting plasma glucose≥5.6 mmol/l) or raised blood pressure (systolic blood pressure≥130 mmHg or diastolic blood pressure≥85 mmHg).

A cohort of age and height matched healthy controls, without MetS were also included and subjects from both groups were randomly assigned to consume either a breakfast meal (had to be consumed withing 15 minutes) comprised of dairy-derived protein or void of dairy-derived proteins (replaced with the same level of soy based protein).

Table 1:  Amino acid composition of the test meals (Gran. 2014)

"The interval between the two test meals was at least four weeks. To prevent possible differences between subjects at baseline from their previous meal the night prior to the study day, subjects were provided with a controlled meal for dinner. The meal consisted of a pre-packaged lasagna and fruit yogurt providing a total of 2462 kJ as 20% fat, 18% protein and 62% carbohydrates. Subjects were asked to eat only the provided food and nothing else." (Gran. 2014)

The test breakfast meals consisted of cheese, butter, and full cream milk with white bread toast (dairy breakfast) and the second meal contained soy cheese analogue, soy beverage, a soy spread, and white bread toast and contained the same amount of protein (31 g) with similar carbohydrate content.

Based on previous research you would expect that...

... switching from dairy to soy, will reduce the anabolic response to the meal. What really happened, however was that the pro-anabolic proteins mTOR (Ser448) and the ribosomal protein S6 increased only after the ingestion of the dairy, not after the consumption of the soy meal.

Figure 1: Activation of mTOR, p70S6K and S6 during the postprandial period in human skeletal muscle (Gran. 2014)

Gran et al. also found that another pro-anabolic signaling protein, i.e. p70S6K (Thr389; Figure 1 - middle), increased only in the healthy control subjects. For the guys with metabolic syndrome, on the other hand, neither the dairy nor the soy meal led to significant increases in the "protein pump" p70S6K, which is usually a good gauge for the actual protein synthetic response. As Gran et al. point out, ...

"[...] P70S6K is the primary readout used to assess the activity of the mTOR pathway (Drummond. 2009; Bodine. 2001); the lack of change in P70S6K phosphorylation after mixed-meal consumption in men with MetS is similar to the anabolic resistance induced by periods of inactivity (Glover. 2008; Breen. 2013) and is observed in older adults (Cuthbertson. 2005; Burd. 2013). Although protein synthesis was not directly measured in this study signalling deficits have been shown to underlie ageing induced anabolic resistance (Cuthbertson. 2005)." (Gran. 2014)

Now, the guys in the study at hand were not exactly old enough for age to be the determining factor, here. Rather than that, research by Villareal, et al. (2012) indicates that eating a clean, energy reduced diet - which was obviously not what the subjects consumed before the experiment in the study at hand - can restore / increase the protein anabolic response in subjects with metabolic syndrome. The non-existent increase in p70S6k in the study at hand could, as Gran et al. highlight, be evidence of this obesity / diet induced resistance to protein-induced skeletal muscle anabolism.

"Ok, being fat and gluttonous is bad, but..." the thing that's probably more interesting for most of you is the absence of increases in protein synthesis in the soy groups. As Gran et al. point out, the study at hand is one of the few studies that have looked at the effects of different proteins on muscle anabolism however - a potential explanation for the differences compared to previous soy vs. whey protein trials, 99% of which used protein shakes as test "meal", could thus be the high fat content (54g) of the test-meal in the study at hand.

Suggested: Only Whey, Not Soy Works 'Wheytloss Wonders' | more.

Yet while previous research indicates that a high fat diet leads to oversaturation of the oxidative capacity of mitochondria in muscle (Koves. 2008), the differences that were observed in the study at hand can hardly be the mere consequence of an inhibitory effect of dietary fat on protein synthesis, because the latter would have had to occur with both dairy and soy protein. We are thus - at least for the moment - left without a definitive answer to the underlying mechanism. Theoretically, it may also be possible that the increase in the soy protein trial was simply less pronounced (less leucine = lower mTOR activation) and the levels had returned to baseline, already after 2h.

It would furthermore be stupid to rely on the elevation of signaling molecules, alone. Theoretically, though, the actual protein synthesis in both trials could still have been similar. If you don't want to rely on the mere possibility that the protein synthetic response may have been similar irrespective of the absence of elevated levels of mTOR & co 2h after the meal, the study at hand does still provide another reason to prefer whey / dairy over soy proteins - in both, your post-workout shakes and regular meals.

References:

• Bodine, Sue C., et al. "Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo." Nature cell biology 3.11 (2001): 1014-1019.
• Breen, Leigh, et al. "Two weeks of reduced activity decreases leg lean mass and induces “anabolic resistance” of myofibrillar protein synthesis in healthy elderly." The Journal of Clinical Endocrinology & Metabolism 98.6 (2013): 2604-2612. 
• Burd, Nicholas A., Stefan H. Gorissen, and Luc JC van Loon. "Anabolic resistance of muscle protein synthesis with aging." Exercise and sport sciences reviews 41.3 (2013): 169-173.
• Cuthbertson, Daniel, et al. "Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle." The FASEB Journal 19.3 (2005): 422-424.
• Drummond, Micah J., et al. "Nutritional and contractile regulation of human skeletal muscle protein synthesis and mTORC1 signaling." Journal of applied physiology 106.4 (2009): 1374-1384.
• Glover, Elisa I., et al. "Immobilization induces anabolic resistance in human myofibrillar protein synthesis with low and high dose amino acid infusion." The Journal of physiology 586.24 (2008): 6049-6061.
• Grundy, Scott M. "Metabolic syndrome pandemic." Arteriosclerosis, thrombosis, and vascular biology 28.4 (2008): 629-636.
• Koves, Timothy R., et al. "Mitochondrial overload and incomplete fatty acid oxidation contribute to skeletal muscle insulin resistance." Cell metabolism 7.1 (2008): 45-56.
• Villareal, Dennis T., et al. "Effect of weight loss on the rate of muscle protein synthesis during fasted and fed conditions in obese older adults." Obesity 20.9 (2012): 1780-1786.

Transfats the Last Bastion of the "Bad Fats"!? Two New Studies Shed Some Light onto Their Impact on Your Health.

Image 1: The Meet the Fats campaign is part of the stultification... ah I mean educational program of the American Heart Association

Meanwhile, even mainstream dietitians are beginning to understand that fats, which have been a, if not THE staple energy source in human history are not the bad boys the anti-fat hysteria of the 1980s would make us believe. Even the American Heart Association begins to advocate the use of "healthy fats" as part of a "heart healthy diet" - unfortunately, the AHA guys still lump Sat (that is the obese guy in the left) Trans (that is the sleazy guy in green) together, although the evidence against poor Sat (who obviously represents all saturated fats) is less conclusive than that against Poly, his money-grubbing sister who would do everything for her sponsors from the corn-industry... well, be that as it may, today's charge is against Trans who is accused of arson, or whole body inflammation, to be precise ;-)

New evidence against Trans is provided by two teams of experts, one from Europe (Bendson. 2011) and the Middle East (Dhibi. 2011). In what I personally would consider battery, Nathalie T. Bendson and her colleagues from Denmark and France assigned 52 (formerly ;-) healthy women randomly to receive
either 15.7g partially hydrogenated soybean oil or control oil without any industrially produced  trans fatty acids (IP-TFA) on a daily basis. The results were not life-threatening, but certainly not desirable:

After 16 weeks, IP-TFA intake increased baseline-adjusted serum tumor necrosis factor (TNF) by 12% more in the IP-TFA group compared with controls. Plasma soluble TNF receptors 1 and 2 were also increased by IP-TFA.

With TNF-alpha's role in the modulation of endothelial and vascular smooth muscle cell function as well as endothelial cell-blood cell interaction and "the importance of such alterations for vascular dysfunction, the initiation and progression of atherosclerosis" (Kleinbongard. 2010), Bendson et al.'s asssumption that

the IP-TFA-associated increase in cardiovascular risk beyond the adverse effect explained by changes in blood lipids may be partly due to induction of systemic low-grade inflammation

is possibly correct. Nevertheless, the jury is still out on how bad TNF-alpha actually is, as its role in cardiovascular disease is actually quite ambiguous with the aforementioned low-grade inflammation on the one hand and its ability to protect your heart by ischemic conditioning on the other hand.

Figure 1: Trans fat content of fresh soy oil, oxidized soy oi and margarine (data based on Dhibi. 2011).

More comprehensive evidence comes from a rodent study by Dhibi et al. who fed 48 male Wistar rats one out of four experimental diets which were either high in fat and included 20% fresh soybean oil diet (FSO), 20% oxidized soybean oil diet (OSO) and 20% margarine (MG) or based on the standard chow (control) with a protein/carbohydrate/fat ratio of 17/62/4 for 4 weeks (Dhibi. 2011). The liver function of the rats, as evidenced by the elevated transaminase levels (ALT, AST) and the increases in alkaline phosphatase (ALP) and lactate dehydrogensase (LDH) in figure 2, took a major beating.

Figure 2: Relative changes in transaminases (ALT, AST), alkaline phosphatase (ALP) and lactate dehydrogensase (LDH) in rats after 4 weeks on diets containing 20% fresh soybean oil, oxidized soybean oil or margarine (data calculated based on Dhibi. 2011)

I suppose the sponsors of the American Heart Association won't like this observation, but it is as plain as the nose in your face that even the "transfat free, heart-healthy polyunsaturated soybean oil" led to statistically significant increases in alkaline phosphatase (ALP) and lactate dehydrogenase (LDH) levels... what, ah... of course that is because the diet was high in fat - how could I forget that 20% fat is still way too much and humans, just like rats should eat a 62% carb 4% fat diet ... I guess that was enough sarcasm for one blogpost, so let's back to the facts, now.

Figure 3: Correlation  between  fatty  acid  isomers  in  the  diet  and  oxidative  stress
  parameters in rat’s liver and plasma hepato-specific enzymes (data based on Dhibi. 2011).

The changes in liver function were accompanied by profound reduction in antioxidant enzyme activity (SOD: superoxide dismutase; GPx: glutathione peroxidase; CAT: catalase) and increased accumulation of conjugated dienes (CD) and malondialdehyde (MDA), the respective correlations of which with the fatty acids isomers (trans fats from mono-unsaturated and poly-unsaturated fatty acids, as well as total transfat content) are plotted in figure 3.

Image 2: Rat liver histology.

Due to its scale (only two different transfat profiles, i.e. oxidized soybean oil and margarine) the study's statistical power is yet so small that we can only make a definite case against the total transfat content for decreases in catalase activity and oxidized polyunsaturated fatty acids for the accumulation of conjugated dienes. With correlations in the the >0.5 and <-0.5 range for many other suspects and crimes, I will yet leave it up to you, the jury, to decide, which members of the transfat family (I suppose the American Heart Associations Trans character must have a whole bunch of children, then - just like in every honorable mafia family ;-) are to be held responsible for which of these crimes against health, the ultimate result of which you see in the histological changes in the livers of the rats fed with oxidized soy oil (OS) and margarine (MG)... So, members of the Jury, on the Case of Trans Fatty Acid (and his mafia clan) vs. the Suppversity, what you say?

Only Whey, Not Soy Works 'Wheytloss Wonders': Add. 60g+ Protein 30 Min Before Ad-Lib Meal Decreases Appetite & Energy Intake, Cuts 9% Body & Adds 18% Muscle in 12 Wks

If you want weight loss support, chose the "Wheytloss Wonder" whey concentrate over the allegedly "healthy plant proteins" in soy isolates - if your physiology works anyway similar to the one of the study subjects you won't regret it - promise!

We all know that whey is wonderful, don't we? And we all know that soy is the devil, right? Ok, I guess both assumptions are not exactly accurate, but when you're having your next discussion with that overweight lady "gone vegan", because it's so good for your waist line, you may point her to a soon-to-be-published study by Atefeh Tahavorgar, Mohammadreza Vafa, Farzad Shidfar, Mahmoodreza Gohari, Iraj Heydari, a group of scientists from the Teheran University of Medical Sciences (Tahavorgar. 2014).

Based on the existing evidence of the weight loss benefits of high(er) protein diets, the Iranian scientists hypothesized that supplemental preloads of whey protein concentrate (WPI) and soy protein isolate (SPI) would decrease appetite, caloric intake, anthropometry, and alter the body composition of healthy overweight and obese men in free living conditions.

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To test this hypothesis, we supplemented free living overweight and obese men with WPC and SPI 30 min before their ad libitum afternoon meals, and monitored each subject’s appetite, calorie intake, anthropometry, and body composition.

Using a monthly bulletin to advertise, volunteer employees of a power plant in Karaj city were recruited to participate in the study. Inclusion criteria included: no cigarette smoking and/or alcohol consumption, no medication and/or supplement usage, no high amounts of caffeine consumption (>250-300 mg/d), no history of diseases or clinical problems that increase oxidative stress (injuries or burns), no allergy to soy/cow's milk, and no severe weight changes within the last three months. Exclusion criteria included any changes in physical activities (PA), diets, and a compliance of 70% or lower for consumption of treatment beverages.

This is a randomized, controlled trial, no epidemiological "healthy plant protein guesswork"

At the first visit, eligible participants were randomly assigned to either the WPC or SPI (26 in each) group, using a convenience allocation. Individuals were instructed to deliver empty sachets in exchange for full ones at visits 2 through 12, in order to calculate compliance.

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All participants had ad libitum access to calories and were asked to maintain their usual dietary intake and physical activity.

"Preload proteins included 80% WPC (DMV, Netherlands) and 90% SPI (Red Crown, China), with similar color and texture. Sachets contained 67.5 g WPC and 60 g SPI (54 g effective compound as a protein / sachet).Calorie contents of WPC and SPI sachets were 261.8 Kcal and 216 Kcal, respectively. They were closely matched for taste with strawberry flavor and sucralose (Vita Sweet, China) (0.2 gr and 0.1 gr in each sachet respectively), as a no-energy sweetener since sucralose is not metabolized in the body and has no effect on blood glucose or insulin secretion." (Tahavorgar. 2014)

After packing 4368 similar sachets, they were numbered 1- 84. The numbers were randomly divided into groups A and B (SPI and WPC, respectively) and kept by the executive director of research until study commencement.

One of the strenghts of the study is the fact that dietary intake and physical activity were closely monitored. If the subjects didn't lie about their food intake and activity levels the results of the study at hand are thus highly accurate. Unfortunately, the same cannot be said of the relatively unreliable body fat measurements that were conducted with a body fat monitor by Jawon Medical.

The consumption of the protein shakes (65 gr WPC or 60 gr SPI that was dissolved in 500 ml water) 30 min before the ad libitum dinner (late afternoon) lead to significant increases of the total protein intake in both groups, with a slightly higher total protein intake of 33.5% of the total energy intake (vs. 28.7%) in the whey vs. soy group. No wonder that the mean changes in appetite (p=0.032), CI (p=0.045), anthropometry (body weight (BW) (p=0.008), body mass index (BMI) (p=0.006), and waist circumference (WC), body composition (body fat mass (BFM) and lean muscle (LM) were significant in both groups.

Figure 1: Changes in appetite, calorie intake and body composition during the 12-week study (Tahavorgar. 2014)

If you look at the overall outcomes in Figure 1, it is yet obvious that the appetite reduction and loss of body weight were significantly more pronounced in the whey protein group. More importantly, however, these changes occurred as a consequence of similar absolute, albeit slightly higher relative reductions in energy intake (there is a problem with the data, here, because the pre- vs. post valued differ from the calculated mean difference, if we use the latter, the soy group would have had a greater reduction in energy intake, i.e. 1186kcal vs. 624kcal - that would make the results even more impressive, but somewhat questionable) and trigger significantly more pronounced improvements in body composition than the soy protein isolate, namely increases in lean mass (+18%) and significant reductions in body fat (-9.2%) and waist circumference (-9.7 cm on average vs. +1.1 cm in the soy group) - not too bad, considering there was no "dieting" or training involved.

Please remember: The weight loss and increases in lean mass occured in the absence of a deliberate energy restriction (all subjects still ate "ad libitum", i.e. as much as they wanted) and without the need to train. It was "just" the addition of high quality protein in form of the ~60g of whey protein concentrate (again there is no reason to buy isolates, unless you are lactose intolerant) that did the trick!

Bottom line: The study at hand is only one out of many experimental trials which refute the notion that plant proteins are healthier and eating plant instead of protein from animal sources would help you lose weight and improve your body composition. The latter is a myth that's based on questionable epidemiological data, where confounding factors such as the "pizza salami = meat" factor (i.e. the way the meat intake is estimate) are hard to control.

Since I hope that we all put more faith in hard experimental vs. "soft" epidemiological data, it should be obvious that anyone (including your vegan friends) who is planning to lose body fat and improve his / her body composition is much better off with whey vs. soy protein; and that not just as a replacement for a complete meal, but rather as an addition that increases the total protein content of the diet and reduces the food and energy intake on ad-libitum meals, when the shake is consumed 30 minutes before a meal | Comment on Facebook!

Reference:

• Tahavorgar, Atefeh, et al. "Whey protein preloads are more beneficial than soy protein preloads in regulating appetite, calorie intake, anthropometry, and body composition of overweight and obese men." Nutrition Research (2014).

18% Increased Protein Breakdown W/ 20g of Egg Protein Before Workout - Reason Enough for Avoiding Pre-Workout Protein Supps? Rational & Experimental Counter-Evidence

Protein before workouts "accelerates protein catabolism"? That sounds worse than it actually is (photo BSN).

Most of you will probably consume a protein shake after their workout. Probably whey, if you've read all SuppVersity articles, maybe 25g whey + 10g casein (learn why), or something like that. But what do you do before your workouts? Do you consume a protein shake 60-90 minutes before your workout? If so, you will be shocked about the conclusion of a recent study from the Tokyo University of Agriculture which says: "[...]  pre-exercise protein supplementation taken in excess may accelerate protein catabolism" (Hasegawa. 2014).

But is it actually possible that consuming more protein (albeit at the wrong time) will have a negative impact on your gains?

You can learn more about protein intake at the SuppVersity

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Before we can answer this important question it is necessary to take a look at the actual design of the randomized cross-over study.

Figure 1: Graphical overview of the experimental protocol (Hasegawa. 2014)

The participants, six healthy male university students [21.2 (±0.3) years, 173.6 (±2.8) cm, and 62.7 (±2.8)kg] with no allergies to egg white or soy, the two protein sources the effects of which the researchers initially wanted to compare, underwent three 8-day testing periods with an exercise at the end (the 8-day intervals were separated by at least seven days).

"Each  testing period began on Day-1 and ended the meat-free diet  consisting of grains, beans, and milk, and 24- hour urine sample collection on Day-8 (Figure 1). Participants were allocated into  one of three groups; egg white protein (E), soy protein (S), and mineral water control (C) group with no additive, and all were carried out this study protocol three times, and asked not to change their lifestyle behaviors." (Hasegawa. 2014). 

The result of this study should remind you of the "Protein-Wheysting" Article | more is not always better!

On Day-5, the day of the workout, the  participants arrived at the  laboratory at 8:00 AM, and had a breakfast consisting of a rice ball (energy, 355 kcal; protein, 6.7 g; carbohydrate, 78.1 g). At 9:30 AM, after the baseline blood sample collection and perceived muscle soreness (MS) measurements, the subjects received one of the three test beverages which contained

• 20 g of egg protein,
• 20g of soy protein, or
• an isoenergetic placebo without protein

that had been dissolved in 200ml of mineral water. 90 minutes later, at 11:00 AM, the previously untrained participants started a resistance training protocol that involved seated rows, flys, leg extensions, and leg presses.

The exercises were performed for three sets of 10 repetitions at ~80% of a predetermined 1-RM with one min rest between sets and two minutes between each exercise.

Figure 2: no significant difference in perceived fatique, but a significant reduction in peak muscle soreness in the soy (grey blocks) vs. the control (white triangles) group (Hasegawa. 2014).

As you can see in Figure 2, the initially mentioned negative effects of the protein supplement were not the only significant inter-trial differences the scientists observed; and what's more, the significantly decreased muscle soreness in response to both protein powders (the peak levels differed statistically significantly only for control vs. soy) stands in stark contrast the mainstream interpretation of protein breakdown (which is "protein breakdown = muscle loss").

How is that possible? Increased protein breakdown and reduced muscle soreness?

So, here we are with an obvious contradiction between the reduced muscle soreness (Figure 2) and the scientists claim that "pre-exercise protein supplementation taken in excess may accelerate protein catabolism" (Hasegawa. 2014)... you already guessed it: The contradiction depends on the false assumption that "protein catabolism" means "catabolism of muscle protein", which is not generally the case and in this specific case certainly wrong.

Figure 3: Urinary nitrogen excretion measured for 72h after the workout (Hasegawa. 2014)

The process we are talking about here is thus most likely not an increase in "mucle catabolism" but rather about the absence of a reduction in protein wasting, i.e a "protein sparing" mechanism that won't be triggered if there is plenty of protein around during the workout.

"So you're saying we don't have to worry?" Basically this is the message of today's SuppVersity article, yes. The notion that the increased amount of nitrogen the scientists measured in their subjects urine is the end product of muscle protein breakdown is highly questionable. It's more likely that the provision of extra protein makes the initiation of protein sparing mechanisms which would otherwise reduce the nitrogen excretion in the control group superfluous - I mean, look at Figure 3 again: Compared to Day 4 (i.e. baseline before workout), the levels remain stable in both protein supplementation groups.

If your pre-workout protein makes you hypo, stop using it or buffer the drop in blood sugar w/ CHO | learn why

You still have doubts!? Well, I have evidence to support my conclusion. Wycherley et al. (2010), for example, were able to show that their dieting subjects saw the same improvements in body composition no matter whether they consumed their protein + carbohydrate beverage (likewise 20g of protein) before or after their resistance training workouts. Rasmussen et al. (2000) report significant increases in muscle protein anabolism after resistance training with pre-workout EAA supplementation. And a protein + carbohydrate supplement reduced (not increased) the muscle damage (as evidenced by 33% reduced increase in myoglobin) in some, but not all subjects in a resistance training study by Baty et al. (7 free weight ex; 3 sets x8 reps to failure | Baty. 2007).

All in all, it does therefore not appear to be indicated to change your current supplementation practice (if you are consuming protein before your workouts)... well, unless you feel wiped out, whenever you consume protein before your workout. In that case, the protein induced increase in insulin is probably sending you right down the hypoglycemia alley. In view of given negative effects on your exercise performance and the touted increases in obesity risk, this is something you should try to avoid by either buffering the insulin spike with carbs or simply avoiding the ingestion of fast digesting protein supplements before your workouts | Comment on Facebook!

References:

• Baty, Jacob J., et al. "The effect of a carbohydrate and protein supplement on resistance exercise performance, hormonal response, and muscle damage." The Journal of Strength & Conditioning Research 21.2 (2007): 321-329.
• Hasegawa, Yuko, et al. "Effect of Egg White Protein Supplementation Prior to Acute Resistance Training on Muscle Damage Indices in Untrained Japanese Men." Monten. J. Sports Sci. Med. 3 (2014) 2: 5–12.
• Rasmussen, Blake B., et al. "An oral essential amino acid-carbohydrate supplement enhances muscle protein anabolism after resistance exercise." Journal of Applied Physiology 88.2 (2000): 386-392.
• Wycherley, Thomas Philip, et al. "Timing of protein ingestion relative to resistance exercise training does not influence body composition, energy expenditure, glycaemic control or cardiometabolic risk factors in a hypocaloric, high protein diet in patients with type 2 diabetes." Diabetes, Obesity and Metabolism 12.12 (2010): 1097-1105.