Ultimate BCAA Guide: Benefits, Intake & Dosage

Ultimate BCAA Guide: Benefits, Intake & Dosage

Ultimate BCAA Guide: Benefits, Intake & Dosage

0 comments 📅13 July 2015, 07:37
2
Shares
Share with your friends










Submit


By Damian N. Minichowski

There are less useful supplements out there than you might expect in the first place. When speaking about workout nutrition you might bet on a solid whey protein (or a mixture of fast and slow assimilating protein), if you’re on a small budget. Your long-term progress will depend mostly upon your workout routine and your nutritional habits than on supplementation.

However, besides traditional whey protein and maybe creatine/beta-alanine, there is another quite interesting supplement, you might consider adding to your regular stack (especially if you’re into intermittent fasting and/or work out on an empty stomach): BCAAs!

Ultimate BCAA Guide: Benefits, Intake & Dosage

BCAAs: What is it?

The term “BCAAs” stands for Branched-Chain Amino Acids – a group consisting of 3 special amino acids, that are considered as essential by today’s standards. Those amino acids are:

  • Leucine
  • Valine
  • Isoleucine

You might already know, that there are 8 essential amino acids in total [1]. They are called essential, because we need to get them with our daily nutrition, since our bodies aren’t capable of synthesizing them. Unfortunately these amino acids are necessary to keep us healthy, since they’re part of other molecules, hormones, enzymes and tissue.

So, why are these 3 amino acids called “branched-chain? It’s because they have a side-chain, which makes them look a little bit like forks. Only a few people are aware of the importance of the BCAAs, but once you take into consideration that approximate 14-18 % of your muscle tissue consists of out them (and that they make up the biggest reservoir of bound amino acids in the whole body – approx. 35-40 % [2][3][4]), you might finally change your mind.

Where can you find these BCAAs? Answer: They’re part of many protein-rich foods, amongst them chicken breast, beef, fish (salmon, tuna), eggs, egg whites and nuts. BCAAs are also found in soy and soy products, although I wouldn’t go as far as to recommend getting your daily dose of BCAAs through soy (products). If you’re a vegetarian, you might consider adding milk and dairy into your daily eating plan to ensure adequate intake. If your vegan, you should add more nuts, wheat germs, legumes and peas onto your plate – and aim for a complete amino acid profile [5].

BCAAs in Bodybuilding and Weightlifting: Do you really need them?

BCAA supplements are quite popular among athletes, since they can enrich a diet, which might be poor on protein already (and thus such supplements maximize the cost-benefit factor, because they’re are in high demand for muscle tissue). On the other hand they work anti-catabolic and help in stimulation of protein synthesis (due their leucine content) – and thus they’re able to spare muscle and improve body composition.

Simply spoken: BCAAs can help on a weight loss diet and they protect lean mass (and may even contribute to muscle grow) if taken in an appropriate manner and dosage.

BCAA Metabolism

Most people don’t distinguish between proteins and even less of them know the real difference between proteins, peptides and amino acids (and therefore, a lot of layman use this terms as synonyms) although they can have quite dissimilar effects and benefits. Speaking on behalf of BCAAs you can bet your ass that it makes a huge difference on how those building blocks are being metabolized – this is what makes them so special in the first place:

  • Metabolization of most other amino acids: Takes place in the liver (via “deamination” or “transamination” – see your favourite book about human physiology)
  • Metabolization of BCAAS: Takes place in the mitochondria of muscle tissue [6].

So what does that mean exactly? Well, while most amino acids take the route to the liver, our little BCAAs (namely Leucine, Valine and Isoleucine) are taken up by the blood, where they’re transported straight to energy facilities of the working muscle cells – the mitochondria. Therefore, you could say that they’re an important energy substrate (similar to medium-chain triglycerides aka MCTs (fat) or dextrose / maltodextrin (carbohydrate)).

But let’s take a closer look:

  • Leucine is a strictly ketogenic amino acid – that means, that it is metabolized through fat metabolism pathways. The end products are Acetyl-CoA and Acetoacetate, a ketone. Both substances play a major role in the krebs cycle (“citric acid cycle”).
  • Valine is a strictly glucogenic amino acid – that means, that it is metabolized through carbohydrate metabolism pathways. The end product is Succinyl-CoA, another intermediate in the krebs cycle.
  • Isoleucine is both, a ketogenic and a glucogenic amino acid – that means that it will get converted either to Acetyl-CoA or Succinyl-CoA. It’s the most variable AA in this mix.
Krebs Cycle & BCAAs

Click to Zoom: Different amino acids get metabolized differently. Their destinies depend on their type (ketogenic, glucogenic, both) and thus the preferred pathway of metabolization. This may alter its contribution and impact on adequate energy supply of the body. BCAAs get metabolized in muscle tissue, where they can serve as an immediate energy substrate (and this work anti-catabolic in times of high energy turnover) (Source: WIkimedia.org / Spinnat ; CC Licence)

The metabolization of the branched-chain amino acids takes place via two specific enzymes: BCAT (branched-chain aminotransferase) and BCKDH (branched-chain alpha-keto dehydrogenase) – those enzymes can be regarded as the bottle-neck of oxidation (“limiting factor”). BCAA intake (through food) or physical exercise and bodily exertion can facilitate the activity of these enzymes (which was shown in several studies, which were done on rats [7][8] and humans [9] already). This can be translated into a higher BCAA demand for athletes [4].

The oxidation of BCAA in muscle tissue contributes to the synthesis of ATP (Adenosine-Tri-Phosphate), the energy currency of the body, and thus enables the body to engage in additional mechanical work (e.g. working out and moving). Believe me when I tell you that you wouldn’t be able to do much if you ran out of ATP. Every movement, every rep, every set is literally being paid in ATP. No ATP, no muscle contraction, no movement.

For the working body, BCAAs are a welcomed, fast available, energy substrate which helps regenerating ATP, therefore it is not really surprising that the intake of BCAAs can improve regeneration of energy stores and helps sparing muscle protein (since the body doesn’t need to break down muscle protein anymore to ensure adequate energy supply – he just takes the incoming BCAAs instead).

BCAAs and Performance

Gets delivered where it is needed: BCAA supplementation raises BCAA concentration in muscle tissue (Source: Ergo-Log.com)

Gets delivered where it is needed: BCAA supplementation raises BCAA concentration in muscle tissue. (Source: Ergo-Log.com)

The last few paragraphs showed that there is a reasonable (physiological) explanation for performance improvements due to BCAA intake – can this theoretical approach translate into practical application? Does BCAA supplementation really raise performance?

Well, first things first: There are a lot of studies, which validate that BCAA intake can improve performance [10][11][12][13][14][16][17].

BCAAs not only serve as a fast-fueling energy substrate for the body. Better performance leads to raised fat-burning properties, once glycogen reserves are depleted [10]. It’s just like a perpetuum mobile, since you can work out harder and longer, due to better energy availability [12][13][15][16][18][19]. There is a good change, that a more intensive workout will lead to a preferable alteration in body composition, more muscle gains and better fat-burning [15].

BCAAs and Glycogen Stores

There is another point, which might justify BCAA supplementation: A glycogen-sparing effect. Conversion of Valine and Isoleucine into Succinyl-CoA (via a process called gluconeogenesis) can lead to glycogen sparing. That means that BCAA could improve regeneration (in between sets and post-workout).

Shimomura et al. (2000) showed that rats exhibit a glycogen-sparing effect in muscle and liver, when given BCAAs [8]. These results were replicated by Flavigna et al. (2012) in another rat model, where rodents were force to swim until exhaustion. These BCAA-mice (4,76% BCAA content in chow) swam 37 % longer than a placebo group [20].

Of course – those were rodents after all. Fortunately, Blomstrand et al. (1997) conducted a similar study with human subjects (dosage: 90mg/kg resp. 41mg/lb) and got similar results [12].

BCAAs and Body Composition

Again, it makes sense that a more intensive workout will lead to greater accumulation in muscle mass in the long-term, which might positively affect body composition.

12 healthy trained males received (n=12) 14 grams of pure BCAAs daily in an experiment done by Stoppani et al. (2009). These subjects also followed a routine with resistance training. There were two other groups involved in this study: One of them received either 28 grams of whey protein (n=12) or 28 grams of carbohydrates instead (n=12).

Our BCAA athletes reduced their body fat % by -2,2% while also gaining +4,2 kg mass on average [21]. But what about the other two groups? Well, those subjects, who received whey protein gained +2,4 kg lean mass and reduced their bf% by -1,2%, while the carbohydrate group gained +1,4kg lean mass and reduced their bf% by -0,6 %.

Unfortunately, this study had some flaws, that should be mentioned here as well. Scientists failed to control for nutritional habits and they gave these athletes 5 additional grams of glutamine and 2 grams of citrulline. Research + sports drinks were funded by Scivation.

Of course, you shouldn’t expect any miraculous outcomes, just because of BCAA supplementation. Big advantages and better progress can be expected with sound nutrition and intensive training. If you ignore the results of the above study, you still get to enjoy the anti-catabolic, glycogen-sparing effect mediated through BCAAs (see sections above).

BCAAs, Signalling and Protein Synthesis

Anti-Catabolic property of leucine

Once you block mTOR activity, there is a decrease in fractional protein synthesis (Source: Drummond et al. (2009))

Let’s take a closer look at one of the branched-chain amino acids, namely leucine. This single amino acids gained a lot of popularity in the last few years, because of its muscle building potential. My colleague Jonathan already wrote an extensive review about the properties of leucine (“Leucine: Driving Force of Muscle Protein Synthesis”), which you might want to check out.

Anyway, leucine serves as a signalling molecule, which activates protein synthesis via mTOR activation. One you block mTOR, you lose the anti-catabolic effect of leucine (which was demonstrated in animals and humans alike [22][23]).

Once stimulated, mTOR leads to a cascade, which facilitates protein synthesis in (muscle)-cells. Nice to know: Mechanical overload is also able to stimulate protein synthesis and thus, leads to muscle hypertrophy [24][25])

Common BCAA products have a 2:1:1 ratios, which means that for every part of valine and every part of isoleucine, we get 2 parts of leucine. Therefore, it shouldn’t come as a surprise, that BCAAs stimulate protein synthesis, due to their high leucine content [26][27][28], which can be translated into muscle gain.

BCAA – Intake and Dosage

What kind of products are available?

Today, it is fairly easy to get a decent BCAA supplement, but just in case you should take a closer look at the product label to ensure that yours got a decent amount of it. Just because your labels says that BCAAs are included, doesn’t mean necessarily that it contains and effective dose of it.

Because of that, I just cannot recommend BCAA capsule products, although they might be quite convenient – you’d have to take a ton of them, which would make it not really cost effective.

Some of you might settle on an all-in-one formula with BCAAs, which is fine, as long as you check the content per portion (not per 100 grams of the powdered product).

If you decide to buy a BCAA product, you should also watch the ratio. Usually, BCAA powder comes in a ratio of 2:1:1 (Leucine:Valine:Isoleucine). Just recently, the market was flooded with powders, which have a higher leucine content (e.g. 4:1:1 or 8:1:1). The logic behind such products is as follow: If some leucine is good, then more of it has to be better…right? Not necessarily.

If you want to maximize protein synthesis you need to get approx. 2-3 grams of leucine. More leucine doesn’t translate into higher protein synthesis and you should not forget, that the other BCAAs (valine & isoleucine) have some interesting properties, too (e.g. anti-fatigue effect).

Basically speaking: A BCAA powder with a ratio of 2:1:1 will satisfy your needs. Just don’t forget that your daily nutrition (and even your whey protein) also has BCAAs, so there is no need to go nuts about it.

BCAA Dosage: How much should you take?

The amount of BCAAs per dosage will depend on your body weight, but you don’t have to do the math with a calculator.

  • Below 70 kg (154 lbs): 5-6 grams pre-workout per 1 hour of training
  • +70kg (154 lbs): +8-10 grams pre-workout per 1 hour of training

If you train for an hour, these amounts should get you covered. Add another dose for each additional hour of training to get the most out of BCAAs.

BCAAs Timing: When should you take it?

BCAAs supplementation is recommended in the pre- and intra-workout phase, but of course, you can add some to your post-workout shake or you could consume it on other times of the day (e.g. as muscle protection on a cutting diet).

If you want to stimulate protein synthesis to the fullest, you it would be more cost effective to take isolated leucine (2-3 grams per dose).

Remember: Once activated and maxed out, protein synthesis remains high for several hours (3-5 hours) and cannot be stimulated further. Consume your BCAAs and/or leucine with meals or 3-5 hours apart from the last meal (e.g. if you trained in the morning and you do follow an intermittent fasting approach, consume either 5-10 grams of BCAAs or 3 grams of leucine every 3-5 hours).

General recommendation

  • Take your BCAAs round about 15 minutes pre-workout or during your workout
  • (Optional) Add 3 grams BCAAs / leucine to your post-workout shake
  • Combine with 1g HMB (anti-catabolic leucine metabolite) for better effect (article on HMB to come)

Consume small amounts of BCAAs throughout the day, to ensure muscle protection on an intermittent fasting scheme, although I’d say that this isn’t necessary and might get quite expensive. Save the BCAAs for your workout nutrition.

BCAAs & Intermittent Fasting

Martin Berkhan recommended BCAAs for their anti-catabolic properties on intermittent fasting (Leangains), e.g. sipping 10 grams of BCAAs, which got dissolved in 1,5 ltr. Water every 3 hours until you reach your eating window in the evening. You should try it out, if you work out in the morning but prefer to eat in the evening.

Final Words

It’s time to bring this short guide to an end. After reading, you should get a good picture about what you can expect from BCAAs (and what not).

Apart from whey protein, creatine, beta-alanine, fish oil, vitamin D and zinc, BCAA supplements can be regarded as a nice addition to your stack with a small benefit for dedicated athletes – especially if you follow an intermittent fasting style approach for nutrition.

This is a supplement type you might want to check out, if you have some money left and if you plan on investing it into supplements – but it is not a necessity.

BCAA: Where to get?

If you’re looking for a high quality source for a reasonable price, I can recommend the BCAA powder from Myprotein (you can get it even cheaper, if you watch out for offers and voucher codes). It tastes like shit and it doesn’t dissolve really well, but you can put it into your shaker and then shake the hell out of it, before downing the entire thing.

There is another version available: iBCAAs are already instantised (flavoured) and some people say, that the dissolubility is far greater than in the standard version. I can’t really recommend those, but if you’re looking for a convenient way, you can try the capsules, like BCAA Plus or BCAA 1500. They are far from cost effective, though.

Discuss this article on the forums

AesirSports on the web – follow us on our other social media channels, too:

Don’t miss out the latest articles: Subscribe our Newsletter NOW!

Subscribe to our newsletter and get FREE updates about muscle building, fitness, health and nutrition. Enter your email address below and make sure to never miss an article again in the future.

Picture source title: Flickr / Sin Amigos ; CC Lizenz

About the Author

Damian “Furor Germanicus” Minichowski is the founder and mastermind behind the bodybuilding and nutrition online magazine Aesir Sports (AesirSports.net & AesirSports.de). Besides numerous authorships Damian is writing for several well known and respected weightlifting and fitness magazines. He authored more than 200 articles about bodybuilding, training, training philosophy, nutrition, health and supplementation already.

Damian worked as a long-term fitness coach in local gyms. His profession lies in evidenced-based article writing and revolves about one of his biggest passions in life – Physical fitness, nutrition, supplementation and health.

References (Click to Expand)

[1] Yoshizawa, F. (2012): New therapeutic strategy for amino acid medicine: notable functions of branched chain amino acids as biological regulators. In: J Pharmacol Sci. URL: http://www.ncbi.nlm.nih.gov/pubmed/22293293.

[2] Layman, DK. / Baum, JI. (2004): Dietary Protein Impact on Glycemic Control during Weight Loss. In: J Nutr. URL: http://jn.nutrition.org/content/134/4/968S.abstract.

[3] Riazi et al. (2003): The total branched-chain amino acid requirement in young healthy adult men determined by indicator amino acid oxidation by use of L-[1-13C]phenylalanine. In: J Nutr. URL: http://www.ncbi.nlm.nih.gov/pubmed/12730426.

[4] Shimomura et al. (2006): Nutraceutical Effects of Branched-Chain Amino Acids on Skeletal Muscle. In: J Nutr. URL: http://jn.nutrition.org/content/136/2/529S.short.

[5] Fuhrman, J. / Ferreri, DM. (2010): by the American College of Sports Medicine. Unauthorized reproduction of this article is prohibited. In: Nutrition & Ergogenic Aids. URL: https://www.drfuhrman.com/library/vegan_athlete.pdf.

[6] Harper, AE. / Miller, RH. / Block, KP. (1984): Branched-chain amino acid metabolism. In: Annu Rev Nutr. URL: http://www.ncbi.nlm.nih.gov/pubmed/6380539.

[7] Kobayashi et al. (1999): Hepatic branched-chain alpha-keto acid dehydrogenase complex in female rats: activation by exercise and starvation. In: J Nutri Sci Vitaminol. URL: http://www.ncbi.nlm.nih.gov/pubmed/10524349.

[8] Shimomura et al. (2000): Suppression of glycogen consumption during acute exercise by dietary branched-chain amino acids in rats. In: J Nutri Sci Vitaminol. URL: http://www.ncbi.nlm.nih.gov/pubmed/10885793.

[9] Howarth et al. (2007): Exercise training increases branched-chain oxoacid dehydrogenase kinase content in human skeletal muscle. In: Am J Physiol Regul Integr Comp Physiol. URL: http://www.ncbi.nlm.nih.gov/pubmed/17581840.

[10] Gualano et al. (2011): Branched-chain amino acids supplementation enhances exercise capacity and lipid oxidation during endurance exercise after muscle glycogen depletion. In: J Sports Med Phys Fitness. URL: http://www.ncbi.nlm.nih.gov/pubmed/21297567.

[11] Wisnik et al. (2011): The effect of branched chain amino acids on psychomotor performance during treadmill exercise of changing intensity simulating a soccer game. In: Appl Physiol Nutr Metab. URL: http://www.ncbi.nlm.nih.gov/pubmed/22050133.

[12] Blomstrand et al. (1997): Influence of ingesting a solution of branched-chain amino acids on perceived exertion during exercise. In: Acta Physiol Scan. URL: http://www.ncbi.nlm.nih.gov/pubmed/9124069.

[13] Portier et al. (2008): Effects of branched-chain amino acids supplementation on physiological and psychological performance during an offshore sailing race. In: Eur J Appl Physiol. URL: http://www.ncbi.nlm.nih.gov/pubmed/18704484.

[14] Shimomura et al. (2010): Branched-chain amino acid supplementation before squat exercise and delayed-onset muscle soreness. In: Int J Sport Nutr Exerc Metab. URL: http://www.ncbi.nlm.nih.gov/pubmed/20601741.

[15] Bigard et al. (1996): Branched-chain amino acid supplementation during repeated prolonged skiing exercises at altitude. In: Int J Sport Nutr. URL: http://www.ncbi.nlm.nih.gov/pubmed/8876349.

[16] Blomstrand et al. (1991): Administration of branched-chain amino acids during sustained exercise–effects on performance and on plasma concentration of some amino acids. In: Eur J Appl Physiol Occup Physiol. URL: http://www.ncbi.nlm.nih.gov/pubmed/1748109.

[17] van Hall et al. (1995): Ingestion of branched-chain amino acids and tryptophan during sustained exercise in man: failure to affect performance. In: J Physiol. URL: http://www.ncbi.nlm.nih.gov/pubmed/7473239.

[18] Shimizu et al. (2012): Energy expenditure during 2-day trail walking in the mountains (2,857 m) and the effects of amino acid supplementation in older men and women. In: Eur J Appl Physiol. URL: http://www.ncbi.nlm.nih.gov/pubmed/21744005.

[19] Blomstrand et al. (1991): Effect of branched-chain amino acid supplementation on mental performance. In: Acta Physiol Scan. URL: http://www.ncbi.nlm.nih.gov/pubmed/1962526.

[20] Falvigna et al. (2012): Effects of diets supplemented with branched-chain amino acids on the performance and fatigue mechanisms of rats submitted to prolonged physical exercise. In: Nutrients. URL: http://www.ncbi.nlm.nih.gov/pubmed/23201847.

[21] Stoppani et al. (2009): Consuming a supplement containing branched-chain amino acids during a resistance-training program increases lean mass, muscle strength and fat loss. In: J Int Soci Sport Nutr. URL: http://www.jissn.com/content/6/S1/P1.

[22] Anthony et al. (2000): Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. In: J Nutr. URL: http://www.ncbi.nlm.nih.gov/pubmed/11015466.

[23] Drummond et al. (2009): Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis. In: J Physiol. URL: http://www.ncbi.nlm.nih.gov/pubmed/19188252.

[24] Dreyer et al. (2006): Resistance exercise increases AMPK activity and reduces 4E-BP1 phosphorylation and protein synthesis in human skeletal muscle. URL: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1890364/.

[25] Kubica et al. (2004): Resistance Exercise Increases Muscle Protein Synthesis and Translation of Eukaryotic Initiation Factor 2Bϵ mRNA in a Mammalian Target of Rapamycin-dependent Manner. In: J Biol Chem. URL: http://www.jbc.org/content/280/9/7570.abstract.

[26] Blomstrand et al. (2006): Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise. In: J Nutr. URL: http://www.ncbi.nlm.nih.gov/pubmed/16365096.

[27] Louard, RJ. / Barett, EJ. / Gelfand, RA. (1990): Effect of infused branched-chain amino acids on muscle and whole-body amino acid metabolism in man. In: Clin Sci. URL: http://www.ncbi.nlm.nih.gov/pubmed/2174312.

[28] Liu et al. (2001): Branched chain amino acids activate messenger ribonucleic acid translation regulatory proteins in human skeletal muscle, and glucocorticoids blunt this action. In: J Clin Endocrinol Metab. URL: http://www.ncbi.nlm.nih.gov/pubmed/11344218.

Search terms: BCAA intake, BCAA dosage, How to take bcaa, do you need bcaa, bcaa protein synthesis, bcaa anti catabolic, bcaa glycogen sparing, best bcaa ratio, bcaa muscle.     


Share this article:

Related Articles

    Sorry, no posts were found.

No Comments

No Comments Yet!

You can be first one to write a comment

Leave a comment