- When you are looking to build and maintain muscle, to help recover from exercise and to cut fat then you need to think about supplementing with BCAAs.
If you are looking for a supplement that will help you to build and repair new muscle, to help you reduce muscle soreness and and maintain metabolic recovery then look no further than the BCAAs (branched chain amino acids) to help here.
Any serious sportsperson, fitness enthusiast, bodybuilder, weight or strength trainer will make it quite clear why they take BCAAs as a supplement. They want to be back in the gym soon after a serious work-out.
Amino-acids are needed for protein synthesis. In the gym protein synthesis usually means muscle building/repair. Some amino-acids are more important than others when it comes to this intense exercise. So it is with the BCAAs or branched chain amino acids.
Of the 20 amino acids needed for protein manufacture, 11 can be produced in the body. But the other nine have to come from the diet or from supplements as they cannot be manufactured by the body. The nine essential amino acids are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.
What Are The BCAAs?
The BCAAs are leucine, isoleucine and valine. These three amino acids are used by muscle during exercise which gives them a unique position in energy metabolism compared to other amino-acids. It has also long been known that supplementation with BCAAs increases anabolism which is the growth and production of muscle proteins but also suppresses their catabolism too (Tipton et al., 1999; Wolfe, 2001; Jones et al., 2004).
In some cases, sports people supplement with just leucine but with vigorous exercise all these soon become depleted. It is worth stating from the outset that for many of us, if we are eating plenty of protein then the need for supplementing with BCAAs makes little sense. If not then a supplement purely based on just these three essential amino-acids is crucial. If you are vegetarian or vegan and a keen gym goer then supplementation may well be the answer.
In the next section you can see that all the protein foods mentioned are from non-vegetarian sources. It seems based on research evidence that plant foods provide enough BCAAs for people enjoying regular exercise but not for those working-out intensely.
What Are The Best Foods Which Are High In BCAA
Foods are always a great source of amino acids including the BCAAs. The reason supplements are taken is because athletes want something where the intake can be controlled, especially if a calorie-controlled diet is being followed.
Some of the best foods to consume for BCAAs are the following:-
Chicken: Per 170g; 36g protein, 6.6g BCAAs, 2.9g leucine, 1.8g isoleucine, 1.9g valine.
Cottage cheese: Per half- cup: 12 protein, 4.7g BCAAs, 1.7g leucine, 1g isoleucine, 1g valine.
Eggs: Per egg; 6.3g protein, 1.3g BCAAs, 0.54g leucine, 0.3g isoleucine, 0.4g valine.
Tinned tuna: Per 170g; 33g protein, 5.6g BCAAs, 2.5g leucine, 1.5g isoleucine, 1.6g valine.
Wild salmon: Per 170g; 34g protein, 5.9g BCAAs, 2.7g leucine, 1.5g isoleucine, 1.7g valine.
What Does The Clinical Evidence Say?
The European Food Safety Authority looked at BCAAs in a review of claims which they published in 2010 with regards to their cause and effect in a number of instances and did not find any. In a nutshell that might have proved highly problematic for the supplement industry. However continued support for BCAAs where people were conducting intense exercise and the possibility that vegetarians probably need to take in certain amounts have led to heightened interest.
BCAAs also have quite a track record of use and were seriously considered from the late eighties onwards (Lemon, 1991). The whole subject of BCAA biochemistry in metabolism has been reviewed very recently (Zhang et al., 2017) where they give a very good account of how BCAAs impact in all sorts of human physiology (worth checking out !)
The Role Of Leucine
Leucine is probably the most important amino acid in the muscle building set. As we exercise, the level of leucine drops off which means it has to be replaced through the diet. It might be considered to act like a hormone as it activates muscle protein synthesis directly (Norton and Layman, 2006). In fact these three amino acids are key to regulating protein metabolism as well as having a key role in protein synthesis and its regulation.
Oral consumption of amino acids is followed by an increase in their blood levels, which immediately increases the rate of muscle protein synthesis. This is partly through the activation of what is known as (mTOR mammalian target of rapamycin) signaling (Ge et al., 2009). Leucine is certainly known to activate the mTOR signaling pathway and has a key role in initiating muscle protein synthesis (Buse & reid, 1975; Anthony et al., 2000).
Clinical studies showed that when compared to a placebo, a daily intake of 20g of BCAAs with half taken in the morning and then evening for a week before intensive exercising helped reduce muscle soreness by 30%. Markers for muscle damage were also reduced by 22% and there was improved muscle performance during the recovery phase (Howatson et al., 2012). There are studies showing that a leucine-enriched amino-acid supplement can help improve muscle recovery in untrained men doing eccentric muscle exercises (Matsui et al., 2019).
Dosing & Timing
Consume at least 2.5g of leucine per meal on average four times per day. This promotes a better weight loss, more fat loss and improved retention of muscle performance in the recovery phase. Similar studies show a high leucine content in the diet impacts on better control of blood glucose levels (Zhang et al., 2007).
BCAAs are best used in a pre-workout drink like a protein shake although we know of some who take these alone when they don’t want protein as well. The feeling is that it is easier to deal with being a much lighter softer load before intense exercise. Understood!
Endurance athletes can certainly be helped using BCAAs. Apparently there is plenty of clinical and anecdotal evidence suggesting back packers, marathon runners or anybody involved with prolonged exercise who benefits from supplementation. Cyclists for example were shown to benefit from high levels of BCAA ingestion when they were engaging in sprints during endurance racing (Kephart et al., 2016). This was a study into performance at the School of Kinesiology in Auburn University, USA. BCAAs also appear to ‘blunt’ the neutrophil response to intense cycling training. This suggests an immune function benefit when they are involved in a long cycling season. We have already commented on the benefits for basketball players.
Getting Over Sore Muscles
- Research suggests BCAAs reduce muscle soreness after a hard workout.
Any exercise however strenuous can leave you feeling sore in the muscles and this lasts usually for a couple of days at least. The level of soreness often diminishes with repetition of the same type of exercise.
Muscle soreness comes from delayed onset muscle soreness (DOMS). It develops about 12 hours after exercise and can persist for up to 72 hours (Costello et al., 2016). DOMS is still being investigated but it appears to be due to microtearing of the muscle fibres which occur after any type of exercise. If BCAAs are associated with reducing muscle damage it is highly likely by association that the duration of DOMS and its severity will also be curtailed.
Limiting The Effects Of Tiredness And Fatigue
Various pieces of research that have looked at the association of BCAA supplementation with tiredness. It suggests they can help reduce the effect of fatigue. Whilst there are many other factors that contribute to tiredness of muscles such as intensity, duration and fitness levels, BCAAs can ameliorate this.
In biochemical terms, BCAAs help return the levels of tryptophan in the brain to its normal level. Tryptophan in the brain is converted to serotonin during exercise which causes fatigue. There is one research study which showed that participants who supplemented with BCAAs had improved mental focus during exercise.
Burning Off Fat
BCAAs and leucine in particular could help with fat burning. If it is combined with glutamine, then supplementation can help those who are overweight following a hypocaloric diet. It is claimed to help reduce excess fat but also reduce a marker of metabolic problems by helping to normalise visceral fat.
What about protein containing BCAAs ? There is some evidence that if we increase our protein intake and reduce our carbohydrate intake at the same time, we can enhance weight loss, lose more body fat without sacrificing muscle or rather lean body mass (Layman et al., 2003; Noakes et al., 2005).
It is not a stretch of the imagination to look at BCAAs as a useful way of reducing obesity in the same way protein ingestion might and in that same way also control diabetes by minimising insulin resistance or controlling glucose tolerance (Kainulainen et al., 2013). All these additional benefits help with improving general health and fitness.
Looking For Lean Muscle Mass?
One study by Stoppani et al.,(2009) found that BCAA supplementation could help improve lean muscle mass and also decrease the percentage of body fat in the process. That study involved 36 strength training men who had been doing resistance training for over 2 years. These gents did an 8-week resistance training program and the researchers randomly assigned them to three groups. Each received either 14 grams of BCAAs, or 28 grams of whey protein, or 28 grams of carbohydrates in a sports drink. In that study, those men who took the BCAA supplement had a better reduction in body fat with a greater increase in lean mass compared to the other study groups.
Bulk Powders Offering Instant BCAAs
N.B. This article contains links to our affiliate marketing partner. Please read our affiliate disclosure. To purchase any of the products highlighted, click on the ‘BUY THIS PRODUCT’ link.
So what do you need to look for when choosing a BCAAs containing powder?
- It contains what it says it should and there may be some other added minerals and vitamins too.
- It does what it claims to do!
- It tastes right – flavour is often underrated but when you’re drinking lots of the stuff it shouldn’t make it a throat-struggle.
- Dissolves easily in water and milk. Most powder formulations are designed for easy dissolution. Water is often the preferred solution.
Most suppliers of BCAA in powder recommend 7g per serving and in virtually all cases the ratio is 2:1:1 of leucine:isoleucine:valine. A few suppliers offer ratios of 4:1:1 and some also do 10:1:1 which makes them virtually leucine powders with a bit of other added branched chain amino acid.
We suggest you start by taking a look at Optimum Nutrition Gold Standard BCAA produced by Glanbia Performance Nutrition. The product comes packed with not only BCAAs but also vitamin C, minerals such as zinc and magnesium and other important electrolytes.
Vitamin C is a nutritional necessity because it is such a powerful antioxidant so protects cell functions at all sorts of levels. It works alongside zinc in helping to maintain the immune system at its peak performance level whilst you reach your fitness goals. Magnesium is needed for energy management in all our cells and ensuring the muscles get enough ‘power juice’ when it needs it most. All three are there to help get through intense workout sessions. It means that you can train much longer than usual because they reduce your level of tiredness and muscle fatigue.
Product details for Optimum Nutrition Gold Standard BCAA:
A 266g pack of 28 servings. Each serving contains 9.5g of the following – 31kcal of energy, 5g BCAA which includes 2.6g leucine, 1.2g isoleucine and 1.2g valine. The ratio is a typical level of 2:1:1 for these amino acids.
The range comes in various exciting and easy to get down flavours:
|apple & pear||BUY THIS PRODUCT|
|raspberry & pomegranate||BUY THIS PRODUCT|
|peach & passionfruit||BUY THIS PRODUCT|
|strawberry kiwi||BUY THIS PRODUCT|
Product details for XTEND Original BCCA Powder:
The XTEND brand from Scivation also offer BCAA containing powders which comes in a similarly positioned set of funky flavours like:
|blackcurrant||BUY THIS PRODUCT|
|blue raspberry ice||BUY THIS PRODUCT|
|Italian blood orange||BUY THIS PRODUCT|
|Knockout fruit punch||BUY THIS PRODUCT|
|lemon lime squeeze||BUY THIS PRODUCT|
|mango madness||BUY THIS PRODUCT|
|smash apple||BUY THIS PRODUCT|
|strawberry kiwi splash||BUY THIS PRODUCT|
|watermelon explosion||BUY THIS PRODUCT|
Their offer is 30 servings and they claim to have in a serving 7g of BCAAs, magnesium for electrolyte support, 2.5g of L-glutamine and 550mg of L-citrulline which the Optimum Nutrition products are not offering in their particular BCAAs product. All well and good we say!
We like Grenade Defend for its Green Apple flavour!
Iron labs Nutrition, who have been producing food supplements since 2009 have a product called BCAA Power which not only includes BCAAs in the ratio of 10:1:1 (L-leucine:L-isoleucine:L-valine) but also magnesium (100mg per regular serving) and pantothenic acid (5mg per regular serving). The flavour is Berry Blast!
Another well known supplier is USN. They offer USN BCAA Power Punch Tangerine.
Supplements made in the UK or European Community are regulated and safe to use. Do always check the label and purchase from a reputable brand. Overseas suppliers might not be so secure as regulations for such products are different. The supplements from the USA are fine but always check if buying on-line whether they include ingredients which are not permitted in Europe.
Are There Any BCAA Side Effects ?
As far as anyone can ascertain from the research there is little to worry about when it comes to BCAA supplementation if conducted properly. Follow the manufacturer’s instructions and take BCAAs responsibly. These should not induce weight gain because a typical 10 serving of BCAAs will contain about 40kcal. It is felt that 0.03-0.05g of BCAA per kg of bodyweight per hour is appropriate. During exercise, it increases to 2-4g per hour.
Legal Disclaimer Concerning Products On This Web-Site
The products and the information provided about specific products on or through this site have not been evaluated by the United States Food and Drug Administration or by any other national regulatory body and are not intended to diagnose, treat, cure or prevent disease. The information provided on this site is for informational purposes only and is not intended as a substitute for advice from your physician/doctor or other health care professional or any information contained on or in any product label or packaging. You should not use the information on this site for diagnosis or treatment of any health problems or for prescription of any medication or other treatment. You should consult with a healthcare professional before starting any diet, exercise or supplementation program, before taking any medication or if you suspect you might have a health problem.
Anthony, J.C., Yoshizawa, F., Anthony, T.G., et al. (2000) Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. J Nutr., 130: pp. 2413–2419 (Article)
Buse, M.G., Reid, S.S. (1975) Leucine. A possible regulator of protein turnover in muscle. J. Clin. Invest., 56: pp. 1250–1261 (Article).
Costello, J.T., Baker, P.R., Minett, G.M., Bieuzen F, Stewart I.B., Bleakley, C. (2016) Cochrane review: Whole-body cryotherapy (extreme cold air exposure) for preventing and treating muscle soreness after exercise in adults. J. Evid. Based Med. Feb;9(1) pp. 43-44. doi: 10.1111/jebm.12187. Epub 2016 Jan 14. PMID: 26779801.
Ge, Y., Wu, A.L., Warnes, C., et al. (2009) mTOR regulates skeletal muscle regeneration in vivo through kinase-dependent and kinase-independent mechanisms. Am. J. Physiol. Cell Physiol., 297: C1434–C1444 (Article)
Howatson, G., Hoad, M., Goodall, S., Tallent, J., Bell, P. G., & French, D. N. (2012). Exercise-induced muscle damage is reduced in resistance-trained males by branched chain amino acids: a randomized, double-blind, placebo controlled study. Journal of the International Society of Sports Nutrition, 9(1), 20
Kainulainen, H., Hulmi, J.J., Kujala, U.M. (2013) Potential role of branched-chain amino acid catabolism in regulating fat oxidation. Exerc. Sport Sci. Rev. 41 pp. 194–200.
Kephart, W.C., Wachs, T.D., Mac Thompson, R., Mobley, C.B., Fox, C.D., McDonald, J.R., et al. (2016) Ten weeks of branched-chain amino acid supplementation improves select performance and immunological variables in trained cyclists. Amino Acids. 48 pp. 779–89
Layman, D.K., Boileau, R.A., Erickson, D.J., Painter, J.E., Shiue, H., Sather, C., et al. (2003) A reduced ratio of dietary carbohydrate to protein improves body composition and blood lipid profiles during weight loss in adult women. J. Nutr. 133 pp. 411–7.
Lemon, P.W. (1991) Protein and amino acid needs of the strength athlete. Int. J. Sport Nutr. 1 pp. 127–45
Noakes, M., Keogh, J.B., Foster, P.R., Clifton, P.M. (2005) Effect of an energy-restricted, high-protein, low-fat diet relative to a conventional high-carbohydrate, low-fat diet on weight loss, body composition, nutritional status, and markers of cardiovascular health in obese women. Am. J. Clin. Nutr. 81 pp. 1298–306.
Norton, L.E., Layman, D.K. (2006) Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. J. Nutr. 136:533S–7S.
Paddon-Jones, D., Sheffield-Moore, M., Zhang, X.J., et al. (2004) Amino acid ingestion improves muscle protein synthesis in the young and elderly. Am J Physiol Endocrinol Metab. 286 E321–E328 (Article)
Stoppani, J., Scheett, T., Pena, J., Rudolph, C., Charlebois, D. (2009) Consuming a supplement containing branched-chain amino acids during a resistance-training program increases lean mass, muscle strength and fat loss. J. Int. Soc. Sports Nutr. 6(Suppl. 1) , p1 https://doi.org/10.1186/1550-2783-6-S1-P1
Tipton, K.D., Ferrando, A.A., Phillips, S.M., et al. (1999) Post exercise net protein synthesis in human muscle from orally administered amino acids. Am. J. Physiol., 276 E628–E634 (Article)
Wolfe, R.R. (2001) Effects of amino acid intake on anabolic processes. Can. J. Appl. Physiol., 26: S220–S227 (Article)