- How to Leverage the Health Benefits of Branched Chain Amino Acids
- What Are Branched Chain Amino Acids?
- Increases Muscle Growth
- Decreases Muscle Soreness and Fatigue
- Reduces Symptoms of Liver Disease
- Foods High in Branched Chain Amino Acids
- Which Whey?
- Branched-chain amino acids and muscle protein synthesis in humans: myth or reality?
- Muscle protein turnover and dietary protein intake
- Theoretical considerations
- BCAAs: The Many Benefits Of Branched-Chain Amino Acid Supplements
- How Dieting Can Cause Muscle Loss
- How BCAAs Help You Keep Your Muscles
- Increase Protein Synthesis
- Reduce Protein Breakdown
- Have Better Workouts
- BCAAs and Whey
- BCAAs and Glucose Levels
- Taking Branched-Chain Amino Acids Pre-Workout
- Supplement: BCAAs
- Supplement: Whey Protein
- Supplement: Creatine
- Supplement: Pre-workout
- Supplement: Weight Gainer
- The Difference Between Essential and Non-Essential Amino Acids
- Scientific Studies Prove the Effectiveness of BCAAs
- Wrapping Up
- Glossary of Terms
- 6-Reasons Why You Should Take BCAAs Today
- Why Do BCAAs Matter?
- What Makes Them ‘Essential’
- Six Reasons to Take BCAAs
- How to Take BCAAs
- The Take-Home Message
How to Leverage the Health Benefits of Branched Chain Amino Acids
The rise of high-protein diets and consumers’ perceptions that they need more protein is backed by science, with many studies indicating that a high-protein diet that contains branched chain amino acids can play a major role in weight loss and metabolic health.
It’s easier than ever for food and beverage manufacturers to leverage the power of branched chain amino acids in their formulations to appeal to those embracing the clean label movement, fitness enthusiasts and others who are concerned with promoting health.
What Are Branched Chain Amino Acids?
Let’s start with a short biology lesson.
Researchers are discovering that the human body is made up of thousands and potentially billions of different types of proteins, but there are only 21 different amino acids that form the building blocks.
You may find many outdated resources that only list 20 amino acids, however, researchers recently discovered Selenocysteine (Sec), the 21st amino acid in the genetic code.
Of those 21 amino acids, there are nine that the human body cannot make, which are identified as essential amino acids. These essential amino acids are just that — we can’t live without them — and they can only be obtained through the foods we eat.
Breaking it down even further, three of the nine essential amino acids — leucine, isoleucine and valine — are considered branched chain amino acids (BCAAs) and account for 35% of the essential amino acids in muscle proteins. They fill several metabolic and physiological roles and, because of their importance, people must eat a diet rich in branched chain amino acids for healthy muscle function.
Increases Muscle Growth
Leucine has been shown to stimulate muscle protein synthesis. In other words, it helps make muscles. Those who suffer from many chronic illnesses, cancer, infections or malnutrition — or are simply growing older — often experience muscle wasting, and BCAAs and other essential amino acids can help reduce or slow its progression.
Decreases Muscle Soreness and Fatigue
Experiencing muscle soreness and fatigue after a new workout is expected. In part, this is due to levels of BCAAs decreasing in muscles during exertion. But research suggests that muscle damage can be reduced and recovery time can be sped up by supplementing with BCAAs prior to exercising.
Reduces Symptoms of Liver Disease
BCAA had a beneficial effect on symptoms and signs of hepatic encephalopathy, which results when your liver is unable to adequately remove toxins from the blood.
The condition results in declining brain function and can cause personality changes, confusion, anxiety, seizures, shakiness and even coma in severe cases.
Taking BCAA supplements may also help protect against liver cancer for those with liver cirrhosis.
Foods High in Branched Chain Amino Acids
The health benefits of branched chain amino acids align with heightened consumer preferences for protein-rich diets.
High levels of BCAAs are found in high-protein foods such as beef, chicken and other meat products.
Perhaps one of the most efficient ways to boost BCAAs, however, is through the consumption of whey protein, which contains all the essential amino acids needed to build muscle.
One study indicated that people who drank 5.6 grams of BCAAs after a workout increased their muscle protein synthesis by 22% compared to those who had a placebo drink.
While whey protein isolate (WPI) has been a long-time, go-to nutritional supplement for fitness enthusiasts, this ingredient is now commonplace in everyday consumer products as well. Some examples include protein bars, clear RTD beverages, frozen desserts and ice cream, soups and practically any application where an enhanced protein level is desired.
Not only can consuming whey protein promote wellness in the ways mentioned above, it has been proven to offer many other health benefits, including anti-aging, weight loss, reduced risks of diabetes and other diseases linked to being overweight, including heart disease, stroke and certain types of cancer.
For food formulators and those who produce nutritional supplements, it’s important to distinguish between commodity WPIs and those specially formulated for use in food applications and RTD beverages. Not all WPIs exhibit the flavor, consistency and functionality necessary to appeal to manufacturers and consumers a.
This is especially true in clear, high-protein beverages, which need to remain shelf-stable without turbidity or sediment forming over time.
Compared with other leading WPIs in the industry, Grande Ultra exceeds commodity products in the areas of protein fortification combined with its ability to maintain great flavor and clarity in beverage applications.
The whitepaper below explores sports nutrition in whey protein further, so be sure to reference the resource for additional insights.
Then, learn the difference for yourself by requesting a consultation and sample. Contact one of our food scientists today.
Branched-chain amino acids and muscle protein synthesis in humans: myth or reality?
There are a total of twenty amino acids that comprise muscle protein. Nine of the twenty are considered essential amino acids (EAAs), meaning they cannot be produced by the body in physiologically significant amounts, and therefore are crucial components of a balanced diet.
Muscle protein is in a constant state of turnover, meaning that protein synthesis is occurring continuously to replace protein lost as a consequence of protein breakdown.
For synthesis of new muscle protein, all the EAAs, along with the eleven non-essential amino acids (NEAAs) that can be produced in the body, must be present in adequate amounts. The branched-chain amino acids leucine, isoleucine and valine are three of the nine EAAs.
Leucine is not only a precursor for muscle protein synthesis, but also may play a role as a regulator of intracellular signaling pathways that are involved in the process of protein synthesis (e.g., ).
The concept that the BCAAs may have a unique capacity to stimulate muscle protein synthesis has been put forward for more than 35 years. Data supporting this hypothesis have been obtained from studies of the responses of rats.
In 1981 Buse  reported that in rats the BCAAs may be rate limiting for muscle protein synthesis. Additional studies supported the concept of a unique effect of BCAAs on muscle protein synthesis in rats, although few have studied the response to oral consumption of only BCAAs.
Garlick and Grant showed that infusion of a mixture of BCAAs into rats increased the rate of muscle protein synthesis in response to insulin , but they did not measure the effects of BCAAs alone. The infusion of BCAAs alone into rats by Kobayashi et al.
 was shown to induce an increase in muscle protein synthesis, but the response was only transient. Presumably the rate of synthesis quickly became limited by the availability of the other EAAs.
Studies of muscle protein synthesis in rats have limited relevance to human responses. Skeletal muscle comprises a much smaller percentage of the total body mass in rats as compared to humans and regulation of muscle protein synthesis differs in many respects.
Thus, in their landmark book on protein metabolism Waterlow and associates concluded from available data that dietary amino acids do not stimulate muscle protein synthesis in rats .
While recent work challenges this assertion, the limited stimulatory effect of dietary amino acids on protein synthesis in the rat reflects the fact that under normal post-absorptive conditions there are excess endogenous amino acids available to enable an increase in protein synthesis if the activity of intracellular factors involved in the initiation of protein synthesis is stimulated. Expressed differently, muscle protein synthesis in the rat is apparently limited by the initiation process rather than the translation process. In contrast, as will be discussed below, that does not appear to be the case in humans. Another important distinction between studies investigating the effects of amino acids on muscle protein synthesis in humans and rats relates to the methodologies commonly used. The “flooding dose” technique  has usually been used in rat studies. This procedure involves measurement of the incorporation of an amino acid tracer into muscle protein over a very short time window, often as short as 10 min. This approach does not distinguish between a transient and a sustained stimulation of protein synthesis. Only a sustained stimulation of synthesis is relevant physiologically. Consumption of an imbalanced mixture of amino acids, such as the BCAAs, may transiently stimulate protein synthesis by utilizing endogenous stores of the other precursors of protein synthesis. However, endogenous stores of amino acids, such as those in plasma and free intracellular pools, are quite limited and may quickly become depleted. If the stimulation of protein synthesis cannot be sustained, there is little physiological significance. Consequently, the flooding dose technique commonly used to measure muscle protein synthesis in the rat produces results with uncertain relevance to human nutrition. Since BCAA dietary supplements are intended for human consumption, the focus of this short review will be research in human subjects.
The sale of BCAAs as nutritional supplements has become a multi-million dollar business. At the center of the marketing for these products is the widely-believed claim that consumption of BCAAs stimulates muscle protein synthesis, and as a result elicits an anabolic response. BCAAs may also be consumed for the purpose of improving “mental focus”, but we will not consider that application.
The primary purpose in this paper to evaluate the assertion that BCAAs alone are anabolic is adequately supported either theoretically or empirically by studies in human subjects. Implicit in our assessment will be the examination of whether or not the phosphorylation state of the eukaryotic initiation factors plays a rate-controlling role in the regulation of muscle protein synthesis in humans.
Muscle protein turnover and dietary protein intake
Muscle protein is in a constant state of turnover, meaning that new protein is continuously being produced while older proteins are being degraded.
The anabolic state has no specific definition, but generally refers to the circumstance in which the rate of muscle protein synthesis exceeds the rate of muscle protein breakdown. The results in a gain of muscle mass.
Conventionally the anabolic state is considered to be driven by a stimulation of muscle protein synthesis, but theoretically could also result from an inhibition of muscle protein breakdown.
The overriding metabolic goal of consuming BCAA supplements is to maximize the anabolic state. It is widely asserted that BCAAs induce an anabolic state by stimulating muscle protein synthesis. An abundant availability of all EAAs is a requisite for a significant stimulation of muscle protein synthesis .
Muscle protein synthesis will be limited by the lack of availability of any of the EAAs, whereas a shortage of NEAAs can be compensated for by increased de novo production of the deficient NEAAs .
In the post-prandial state following a meal containing protein, all of the EAA precursors required for new muscle protein synthesis can be derived from either the elevated plasma concentrations resulting from digestion of the consumed protein or from recycling from protein breakdown.
In this circumstance of abundant availability of EAAs the rate of muscle protein synthesis exceeds the rate of breakdown, thereby producing an anabolic state. In the post-absorptive state the plasma EAA levels fall below the post-prandial values because amino acids are no longer being absorbed.
As a result, EAAs are no longer taken up by muscle, but rather released by muscle into plasma . This catabolic state of muscle protein in the post-absorptive state enables continued availability of EAAs for other tissues to maintain the rate of protein synthesis at the expense of muscle protein, which can be considered to play a role as the reservoir of EAAs for the rest of the body to draw upon.
Since EAAs cannot be produced in the body and there is a net release of EAAs from muscle, in the post-absorptive state the only source of EAA precursors for muscle protein synthesis is intracellular EAAs derived from muscle protein breakdown .
In addition to being reincorporated into muscle protein via synthesis, some EAAs released from muscle protein breakdown may be partially oxidized within muscle, thereby making them unavailable for reincorporation into muscle protein.
EAAs released from muscle protein breakdown that are not reincorporated into muscle protein or oxidized within muscle tissue are released into plasma, whereupon they can either be taken up by other tissues as precursors for protein synthesis or irreversibly oxidized .
Thus, the rate of muscle protein synthesis will always be lower than the rate of muscle protein breakdown in the post-absorptive state, owing to the net flux of EAAs from protein breakdown into plasma and to oxidative pathways.
Expressed differently, it is impossible for muscle protein synthesis to exceed the rate of muscle protein breakdown when the precursors are derived entirely from protein breakdown, and thus an anabolic state cannot occur in the absence of exogenous amino acid intake.
All EAA precursors for muscle protein synthesis in the post-absorptive state are derived from muscle protein breakdown. It has been consistently reported that in normal post-absorptive humans the rate of muscle protein breakdown exceeds the rate of muscle protein synthesis by approximately 30% . Consumption of BCAAs alone (i.e.
, without the other EAAs) can only increase muscle protein synthesis in the post-absorptive state by increasing the efficiency of recycling of EAAs from protein breakdown back into protein synthesis, as opposed to either being released in to plasma or oxidized.
This is because all 9 EAAs (as well as 11 NEAAs) are required to produce muscle protein, and EAAs cannot be produced in the body. If only 3 EAAs are consumed, as is the case with consumption of BCAAs, then protein breakdown is the only source of the remaining EAAs required as precursors for muscle protein synthesis.
It is therefore theoretically impossible for consumption of only BCAAs to create an anabolic state in which muscle protein synthesis exceeds muscle protein breakdown.
If the generous assumption is made that BCAA consumption improves the efficiency of recycling of EAAs from muscle protein breakdown to muscle protein synthesis by 50%, then this would translate to a 15% increase in the rate of muscle protein synthesis(30% recycled in basal state X 50% improvement in recycling = 15% increase in synthesis).
Further, a 50% reduction in the release of EAAs into plasma from muscle would also reduce the plasma and intracellular pools of free EAAs. Figure Fig. 1 schematically illustrates these principles.
Since a 50% improvement in recycling efficiency would be about the reasonable maximal limit, this means that the maximal stimulation of muscle protein synthesis could not exceed 15%. This would correspond to an increase in the fractional synthetic rate of muscle from a basal value of about 0.050%/h in the basal state to 0.057%/h, and this difference in the fractional synthetic rate (FSR) of protein would be difficult to accurately measure .
Schematic representation of the recycling of essential amino acids (EAAs) from muscle protein breakdown into muscle protein synthesis in the post-absorptive state. Arbitrary units are used for simplicity and are measured rates of each pathway in post-absorptive human subjects .
a Normal circumstance in the post-absorptive state. Approximately 70% of EAAs from muscle protein breakdown are recycled into protein synthesis .
There is a net efflux of approximately 85% of EAAs released from protein breakdown, which can either be taken up and incorporated into protein in other tissues or oxidize. About 15% of EAAs from protein breakdown are partially oxidized in muscle and unavailable for protein synthesis.
The figures for outward flux and intracellular oxidation of EAAs are averages, since some EAAs, such as phenylalanine, are not oxidized at all in muscle. b Representation of a 50% increase in efficiency of recycling of EAAs from muscle protein breakdown into protein synthesis.
In this example there would be an increase in synthesis from 70 to 80 units, or 20%. Protein synthesis can never exceed protein breakdown in the post-absorptive state, since protein breakdown is the only source of EAAs
BCAAs have been administered intravenously in the only studies determining the response of muscle protein metabolism in human subjects to BCAAs alone.
While the infusion of BCAAs is not the conventional manner in which a dietary supplement would be consumed, intravenously infused and orally-ingested amino acids have been shown to elicit comparable effects on muscle protein synthesis in other circumstances .
Consequently, it is reasonable to evaluate the papers in which the response of muscle protein synthesis to the intravenous infusion of BCAAs in human subjects.
Louard et al.  used the forearm balance method to quantify the response to the intravenous infusion of a mixture of BCAAs for 3 h in 10 post-absorptive subjects. The forearm balance method involves the measurement of the uptake and release of individual EAAs (leucine and phenylalanine in this case) and their isotopically-labelled counterparts.
Rates of disappearance (Rd) and appearance (Ra) of phenylalanine and leucine are calculated. With the assumption that the balance across the muscle of leucine and phenylalanine is representative of all EAAs, Rd. of phenylalanine is taken to be a reflection of muscle protein synthesis, since protein synthesis is the only fate of phenylalanine taken up by muscle from plasma. The Rd.
of leucine cannot be interpreted with regard to protein synthesis, as leucine taken up by muscle can be oxidized as well as incorporated into protein. The 3 h infusion of BCAAs increased plasma concentrations of all 3 BCAAs four-fold, while the concentrations of other EAAs decreased .
Rather than being stimulated by the BCAA infusion, muscle protein synthesis decreased from 37+/− 3 to 21 +/− 2 nmol/min/100 ml leg (statistically significant, p
BCAAs: The Many Benefits Of Branched-Chain Amino Acid Supplements
In recent years, branched-chain amino acid supplements have made a comeback in the bodybuilding and fitness communities, and with good reason. There's more research that supports the use of BCAAs than most other supplements on the market.
While BCAA supplementation may be useful for gaining skeletal muscle (the kind that makes you swole), BCAAs are especially helpful for maintaining mass while on a calorie-deficit diet. They're particularly useful for bodybuilding competitors who take their physiques to the lean extreme.
Although dieting down makes you look awesome onstage, on the beach, and to your friends, it can also take a chunk your muscle mass.
How Dieting Can Cause Muscle Loss
Dieting is catabolic, which means it can lead to muscle breakdown, for several reasons. The leaner a body gets, the more ly it is to lose skeletal muscle as the body tries harder and harder to hold on to body fat stores. In doing so, a side effect is that the body will turn to muscle to satisfy its energy needs. Bad news for anyone interested in a hard body.
On the molecular level, muscle loss occurs because the body increases protein breakdown (catabolism) in order to liberate muscle amino acids for metabolic fuel. If this isn't bad enough, muscle loss is compounded by the fact that levels of muscle protein synthesis will also decrease due to reduced energy intake.
The basic equation for muscle mass is: Muscle mass = rate of protein synthesis – rate of protein breakdown.
When the rate of synthesis equals the rate of breakdown, you don't gain or lose muscle. If the rate of synthesis is higher than the rate of breakdown, you get muscle growth. When the rate of breakdown is higher than the rate of synthesis, you lose muscle. If you're dieting, you may be burning the candle at both ends: raising muscle breakdown and lowering protein synthesis.
Working out compounds the metabolic effects of dieting. The leaner you get, the more lethargic you can become. Decreased energy intake and glycogen storage make for some rough training sessions. If you're too tired or weak to lift as heavy as your body is used to, your muscles will adapt, and they won't use as much energy to get the work done.
That leads to two metabolic problems: You won't increase skeletal muscle, and your body could use the lean muscle you do have for energy because you aren't using it to lift a heavy load.
How BCAAs Help You Keep Your Muscles
Here are the ways branched-chain amino acids can help you stay swole when you're dieting.
Increase Protein Synthesis
Branched-chain amino acids (which are the essential amino acids valine, isoleucine, and leucine) stimulate muscle protein synthesis, potentially more than a normal protein on its own. Protein synthesis is the metabolic process when your body makes new muscle protein, also known as gains.
Reduce Protein Breakdown
Increased BCAA levels also work in your favor by reducing the rate of protein breakdown. They do this by decreasing the activity of the protein breakdown pathway, and also by decreasing the expression of several complexes involved in protein breakdown. (They decrease the amount of mRNA produced from the gene that codes for these components.)
If we revisit our original equation for muscle mass, it's plain to see that increasing synthesis and decreasing breakdown will equate to muscle gain or maintenance.
Have Better Workouts
Amino acid supplementation could also help you get a more intense workout. Branched-chain amino acids compete with the amino acid tryptophan for entry into the brain, where tryptophan can be converted to the neurotransmitter serotonin.
During exercise, serotonin levels rise and can make you feel more fatigued, meaning you won't be able to push as hard.
BCAA supplementation reduces the amount of tryptophan that gets through the blood-brain barrier, and therefore reduces the amount of serotonin produced. This might allow you to work harder, longer, and get more gains.
BCAAs and Whey
Despite all these benefits of BCAA supplementation, there are many skeptics who say branched-chain amino acids are overpriced and you can just get them from whey protein. While proteins whey are naturally rich in BCAAs, this isn't the most effective strategy for muscle growth or fat loss.
The BCAAs in whey are peptide-bound to other amino acids. In order to raise BCAA levels in your body, they must be liberated through digestion and then absorbed into the bloodstream. Even though whey protein is relatively fast digesting, it still takes several hours for all the amino acids to be broken down and absorbed into the plasma.
Branched-chain amino acids in supplement form, however, are free-form, require no digestion, and are rapidly absorbed into the bloodstream.
They spike blood amino acid levels more quickly and to a much greater extent than peptide-bound aminos in proteins.
Even a few grams of free-form BCAAs will spike BCAA plasma levels way more than 30 grams of whey protein. They can start working right away.
BCAAs and Glucose Levels
Branched-chain amino acids play an important role in regulating glucose. They are continuously released from the liver and other internal organs to skeletal muscles to maintain blood sugar levels. Having enough of these amino acids in the body can help improve glucose uptake and insulin sensitivity in healthy people.
These essential amino acids are responsible for a large portion of blood sugar production during workouts. This is important to note if you work out in a fasted state or if you're on a calorie restricted diet.
When you have a balanced carbohydrate, high-protein, and amino acid beverage during and post-exercise, this can induce an insulin response.
The insulin response helps transport aminos into cells to repair muscle damage and build muscle tissue.
You're basically replenishing the anabolic building blocks that your body needs to repair itself post-workout and reduce delayed onset muscle soreness.
Taking Branched-Chain Amino Acids Pre-Workout
BCAA supplementation should also be a regular part of your pre-workout routine.
Since these amino acids bypass the liver and gut and go directly into your blood plasma, they can be used as an immediate energy source during high-intensity workouts.
Valine and isoleucine are glucogenic amino acids, meaning they can be converted to glucose to give you energy. That can help you fight fatigue during your muscle-building workouts.
- Use: Replenish amino acids to build and maintain muscles, avoid fatigue
- Timing: Pre-workout, intra-workout, post-workout, throughout the day
- How Much to Take: 5-7 grams
Supplement: Whey Protein
- Use: Increase protein synthesis for muscle building and repair
- Timing: Pre-workout, post-workout, throughout the day
- How Much to Take: 20-30 grams
- Use: Assist muscle growth and pump, delay fatigue
- Timing: Once daily
- How Much to Take: 3-5 grams
- Use: Get extra energy and focus for hard efforts
- Timing: Pre-workout
- How Much to Take: Depends on formula
Supplement: Weight Gainer
- Use: Provide protein, fat, and carbs to build and retain mass
- Timing: Post-workout, throughout the day
- How Much to Take: Depends on formula
The Difference Between Essential and Non-Essential Amino Acids
Essential amino acids include all the amino acids that cannot be made by the body, including BCAAs. You must get them from protein foods. There are nine essential amino acids: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, tryptophan, and valine. Your body can make non-essential amino acids by itself from vitamins and other amino acids.
The term “non-essential” can be misleading since all amino acids are essential for proper metabolism and certain non-essential amino acids, such as glutamine, become very essential during illness or trauma. The 13 non-essential amino acids are alanine, arginine, aspartic acid, cysteine, cystine, glutamic acid, glutamine, glycine, hydroxyproline, proline, serine, and tyrosine.
So how do branched-chain amino acids factor in with your diet and other supplements? The standard dosage for isoleucine is 48-72 milligrams per kilogram of body weight and the recommended dosage for leucine is between 2-10 grams. This equals about 20 grams of combined amino acids with a balanced ratio of leucine and isoleucine.
This would be the equivalent of consuming natural sources of protein such as meat and eggs at a ratio of 1-1.5 grams of protein per kilogram of body weight per day. But remember, to get the immediate effects of branched-chain amino acids on your plasma BCAA levels, take them on their own instead of just getting them from foods.
Monitor your dosage accurately. Excessive amounts of BCAA supplements can overstimulate insulin signals causing insulin resistance.
Scientific Studies Prove the Effectiveness of BCAAs
Many studies have been conducted to monitor the safety and effectiveness of branched-chain amino acids.
- A study at Leeds Metropolitan University in the UK found that supplementing with leucine during a resistance training program enhanced strength performance.
- A team of researchers from the University of Orleans in France found that during a long endurance trial, athletes who took high levels of mixed branched-chain amino acid supplements (including valine, leucine, and isoleucine) reported feeling less tired. Athletes who took the placebo reported feeling more tired and having more memory errors.
- Other reports found that proteins involved in muscle catabolism (exercise-induced muscle breakdown) appeared to be suppressed following BCAA supplementation. The researchers think this is an indirect function of muscle protein synthesis.
- The Graduate School of Bioagricultural Sciences at Nagoya University in Japan also tested the effects of BCAA supplementation. Their findings show that taking BCAA supplements before and after exercise is effective for reducing post-exercise muscle soreness.
Whether your goal is muscle building or weight loss, supplementing with branched-chain amino acids (leucine, isoleucine, and valine) can support the metabolic processes that make it happen. They can also make your gym workouts more effective.
You can get these amino acids from foods, but dietary BCAAs won't hit your blood plasma as fast as BCAA supplements. Add a BCAA supplement to your routine! You can take it before, after, and/or during your workout. You can also sip on these amino acids between meals to stay in an anabolic state as much as possible.
Forget other supplements that are long on promises but short on results. Instead, check out the power of BCAAs.
Glossary of Terms
Amino acids: Amino acids are the compounds that are the building blocks of protein. There are essential amino acids and non-essential amino acids. You get them from eating protein, and they are what your body uses to build muscle protein.
Branched-chain amino acids (BCAAs): BCAAs are a class of essential amino acids that the body can use for energy and muscle synthesis. The branched-chain amino acids include leucine, isoleucine, and valine.
Catabolism/Catabolic: Catabolism is another name for muscle tissue breakdown. This is what happens when your body dismantles muscle tissue to use as fuel. Being in a catabolic state means this is how your body is getting energy.
Glucose: Glucose is the form of sugar that is in our blood, also known as blood sugar. You get this from eating carbs, but the branched-chain amino acids isoleucine and valine can also be converted into glucose.
Insulin: Insulin is a hormone made in the pancreas that helps the body turn glucose into energy.
Protein synthesis: Protein synthesis is when your body makes new muscle protein, also known as gains.
- Ispoglou, T., King, R. F., Polman, R. C., & Zanker, C. (2011). Daily L-leucine supplementation in novice trainees during a 12-week weight training program. International Journal of Sports Physiology and Performance, 6(1), 38-50.
- Portier, H., Chatard, J. C., Filaire, E., Jaunet-Devienne, M. F., Robert, A., & Guezennec, C. Y. (2008). Effects of branched-chain amino acids supplementation on physiological and psychological performance during an offshore sailing race. European Journal of Applied Physiology, 104(5), 787-794.
- Borgenvik, M., Apró, W., & Blomstrand, E. (2011). Intake of branched-chain amino acids influences the levels of MAx mRNA and MuRF-1 total protein in resting and exercising human muscle. American Journal of Physiology-Endocrinology and Metabolism, 302(5), E510-E521.
- Shimomura, Y., Inaguma, A., Watanabe, S., Yamamoto, Y., Muramatsu, Y., Bajotto, G., … & Mawatari, K. (2010). Branched-chain amino acid supplementation before squat exercise and delayed-onset muscle soreness. International Journal of Sport Nutrition and Exercise Metabolism, 20(3), 236-244.
6-Reasons Why You Should Take BCAAs Today
accessibility mode: off
Skip to content
What is the big deal with BCAAs anyway? You may have heard a thing or two about them from your supplement-savvy training partner, but unless you have a background in biochemistry, you might not know why they matter or how to incorporate them into your training and nutrition regimen.
Why Do BCAAs Matter?
Leucine, isoleucine, and valine are the three branched chain amino acids (BCAAs), so named because of their nonlinear (“branched”) carbon atom configuration.
Amino acids are the building blocks of proteins, and proteins, as you probably know, make up the structure of the body.
Amino acids are either produced in the body (termed, “nonessential”), or they must be supplied from the diet (termed, “essential”).
What Makes Them ‘Essential’
BCAAs are essential amino acids, meaning they are not made in the body, yet they constitute more than one third of the protein found in human muscle tissue! Rich dietary sources of BCAAs include dairy, egg, meat, poultry and fish.
Supplemental BCAAs are also widely available and often used within the context of sports nutrition. BCAAs are unique because, un most other amino acids, they are primarily metabolized within the muscle itself, as opposed to being broken down by the liver.
That has two important implications for performance:
- Rapidly Absorbed: BCAAs enter the bloodstream rapidly, bypass breakdown in the liver, and are readily taken up by active tissues (mainly muscle), and
- More Fuel: BCAAs provide an additional fuel source for working muscle, as BCAA breakdown for energy increases during prolonged exercise (Shimomura et al., 2006). BCAAs also play an important role in overall protein turnover, which is to say they help regulate whether the body is in a recovery (tissue building) or catabolic (tissue breakdown) state.
Of the BCAAs, leucine in particular has been shown to initiate muscle protein synthesis (building) and inhibit protein breakdown (Norton & Layman, 2006). This is key whether you are trying to build muscle, maintain lean body mass during caloric restriction, or simply reduce muscle breakdown during intense and/or long-duration exercise.
Six Reasons to Take BCAAs
1. BCAAs Delay Fatigue During Prolonged Exercise
BCAAs have been found to inhibit the onset of both central and peripheral fatigue during exercise, so you can go stronger for longer.
Peripheral fatigue (when your muscles get tired) is delayed because BCAAs are used as an additional energy source during prolonged exercise. Event after your body has used its glycogen stores, you can pull power from BCAAs in your muscles(Kainulainen, Hulmi, & Kujala, 2013; Gualano et al.
, 2011). Central fatigue (when your brain gets tired) may also be delayed by BCAAs that block the amino acid tryptophan from getting into the brain.
Tryptophan (the same tryptophan from your post-thanksgiving drowsiness) is a precursor to the neurotransmitter serotonin, a central fatigue substance which produces feelings of relaxation and sleepiness (Newsholme & Blomstrand, 2006).
BCAAs Improve Aerobic and Anaerobic Performance When Taken Regularly
Trained cyclists supplementing with 6 g BCAAs for a week leading up to a graded exercise test to exhaustion achieved a 4% higher VO2max, including 13% higher VO2 at the lactate threshold (LT) and 6% greater power output at LT compared to placebo (Matsumoto et al, 2009). As any athlete knows, a a small increase in performance can mean the difference between a podium finish…or not. In another study involving trained cyclists, researchers found that 10 weeks of BCAA supplementation (12 g/day) resulted in a 19% increase in all-out sprint peak power and 4% increase in average power relative to body mass when compared to placebo (Kephart et al., 2016). Importantly, the results of these studies indicate that BCAA supplementation can improve both aerobic exercise capacity and anaerobic performance!
3. BCAAs Fortify the Immune System
Intense, high volume training repeated over days and weeks can lead to fatigue, immune suppression, and overtraining if an athlete does not recover adequately between training bouts.
Chronic (long term) supplementation with 12 g BCAA daily has been shown to improve the immune response to several weeks of intense endurance training in cyclists (Kephart et al., 2016).
But how? Researchers have found that BCAAs can also be used by immune cells within the gut as a fuel source, which allows the immune system to regenerate itself more efficiently and protect against harmful pathogens (Zhang et al, 2017). A strong immune system aids in recovery and makes you less ly to get sick.
BCAAs Protect Lean Muscle (Insurance for your Muscles!)
BCAAs have been shown to preserve muscle mass under extremely catabolic conditions characterized by protein breakdown and muscle wasting, such as ultramarathons and high altitude mountaineering (Schena, Guerrini, Tregnaghi, & Kayser, 1992). During exercise, muscle protein breakdown, and in particular, BCAA breakdown for energy is increased (Shimomura et al., 2004). By providing supplemental BCAAs, the body is less ly to consume its own amino acid (protein) stores. Think of them as your muscle insurance policy!
5. BCAAs Promote Muscle Protein Synthesis
This is probably the number 1 reason weight lifters (aka meatheads) love BCAAs! As mentioned before, leucine is the most important of the three BCAAs for initiating muscle protein synthesis (MPS), which is necessary for muscle building.
A dose of 2-3 g leucine (depending on body weight) is generally considered effective to maximally stimulate MPS, and is often referred to as the leucine threshold (Norton & Layman, 2006). As a point of reference, one large egg contains about 0.5 g leucine, and 5-6 oz of most meat, poultry, or fish sources will provide the recommended 2-3 g amount.
Dairy products, and whey in particular, are high in BCAA content, which is why you’ll find whey protein in our Recovery Drink Mix!
BCAAs Reduce Exercise Induced Muscle Soreness and Damage
BCAA administration prior to and following exercise may reduce the severity and duration of delayed onset muscle soreness (DOMS), the painful sensation that lasts for several days after an intense or unaccustomed exercise bout (Shimomura et al.
, 2010). Furthermore, studies have shown that BCAA intake reduces muscle damage in response to both resistance training (Howatson et al., 2012) and endurance exercise (Coombes & McNaughton, 2000; Kim et al., 2013). That means you can bounce back faster and have less muscle soreness between challenging workouts.
How to Take BCAAs
Take between 4-20 g per day (that’s at least three BCAA capsules)
The exact dosage and ratio of leucine:isoleucine:valine is still a matter of debate in the literature, but most studies supplemented within a range of 4-20 g BCAAs per day, usually split into multiple doses.
Make it a habit – studies observe benefits after a week or more of supplementation
Favorable results have been seen with prolonged use, as it appears that the enzyme activity necessary to break down BCAAs increases in response to habitual intake. Many studies have observed benefits after a week or more of daily supplementation.
Use anytime – before, during, and after workouts
BCAAs can be taken before, during, and after workouts to rapidly increase amino acid levels in the bloodstream, promote protein synthesis, and prevent muscle protein breakdown.
They may also be taken between meals if you feel your diet is not providing adequate levels of BCAAs in the form of complete protein from meat, dairy, fish, eggs, etc. Supplemental BCAAs are sold encapsulated ( our Roctane BCAA Capsules), or in plain or flavored powder form, that can be mixed into liquid.
Keep in mind, however, plain (unflavored) BCAA powders are not everyone’s cup of tea, and can have a somewhat bitter taste.
The Take-Home Message
BCAAs are beneficial for athletes, individuals engaged in high volume or prolonged exercise, those on restrictive diets who many not get enough from whole food sources, or for anyone otherwise at risk of lean tissue breakdown.
Research has shown supplemental BCAA intake to be safe for healthy adults in doses of 4-20 g per day, with prolonged intake one week or more showing greater benefits than acute (short term) intake. Aim for 2-3 g leucine between meals, before, during or after workouts to maximize muscle protein synthesis.
Smaller amounts of BCAAs taken repeatedly over the course of a long training bout are ly beneficial for delaying the onset of fatigue and preventing muscle tissue breakdown.
Coombes, J. S., & McNaughton, L. S. (2000). Effects of branched-chain amino acid supplementation on serum creatine kinase and lactate dehydrogenase after prolonged exercise. Journal of sports medicine and physical fitness, 40(3), 240.
Gualano, A. B., Bozza, T., Lopes, D. C. P., Roschel, H., Dos Santos, C. A., Luiz, M. M., … & Herbert, L. J. A. (2011). Branched-chain amino acids supplementation enhances exercise capacity and lipid oxidation during endurance exercise after muscle glycogen depletion. The Journal of Sports Medicine and Physical Fitness, 51(1), 82-88.
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. Exercise and Sport Sciences Reviews, 41(4), 194-200.
Kephart, W. C., Wachs, T. D., Mac Thompson, R., Mobley, C. B., Fox, C. D., McDonald, J. R., … & Pascoe, D. D. (2016). Ten weeks of branched-chain amino acid supplementation improves select performance and immunological variables in trained cyclists. Amino Acids, 48(3), 779-789.
Kim, D. H., Kim, S. H., Jeong, W. S., & Lee, H. Y. (2013). Effect of BCAA intake during endurance exercises on fatigue substances, muscle damage substances, and energy metabolism substances. Journal of Exercise Nutrition and Biochemistry, 17(4), 169-180.
Matsumoto, K., Takashige, K. O. B. A., Hamada, K., Tsujimoto, H., & Mitsuzono, R. (2009).
Branched-chain amino acid supplementation increases the lactate threshold during an incremental exercise test in trained individuals. Journal of Nutritional Science and Vitaminology, 55(1), 52-58.
A., & Blomstrand, E. (2006). Branched-chain amino acids and central fatigue. The Journal of Nutrition, 136(1), 274S-276S.
Norton, L. E., & Layman, D. K. (2006). Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. The Journal of Nutrition, 136(2), 533S-537S.
, Guerrini, F., Tregnaghi, P., & Kayser, B. (1992). Branched-chain amino acid supplementation during trekking at high altitude.
European Journal of Applied Physiology and Occupational Physiology, 65(5), 394-398.
Shimomura, Y., Murakami, T., Nakai, N., Nagasaki, M., & Harris, R. A. (2004). Exercise promotes BCAA catabolism: effects of BCAA supplementation on skeletal muscle during exercise. The Journal of Nutrition, 134(6), 1583S-1587S.
Shimomura, Y., Yamamoto, Y., Bajotto, G., Sato, J., Murakami, T., Shimomura, N., … & Mawatari, K. (2006). Nutraceutical effects of branched-chain amino acids on skeletal muscle. The Journal of Nutrition, 136(2), 529S-532S.
Shimomura, Y., Inaguma, A., Watanabe, S., Yamamoto, Y., Muramatsu, Y., Bajotto, G., … & Mawatari, K. (2010). Branched-chain amino acid supplementation before squat exercise and delayed-onset muscle soreness. International Journal of Sport Nutrition, 20(3), 236.
Zhang, S., Zeng, X., Ren, M., Mao, X., & Qiao, S. (2017). Novel metabolic and physiological functions of branched chain amino acids: a review. Journal of Animal Science and Biotechnology, 8(1), 10.