The sleep and recovery practices of athletes. By Jill Corleone, RD Jill is a registered dietitian who's been learning and writing about nutrition for more than 20 years.

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Table of Contents View All. Table of Contents. What are BCAAs? What Does the Research Say? Are BCAAs Harmful? Best Ways to Boost BCAAs. Importance of Recovery. Supplements for Fitness. How to Improve Workouts. Jerlyn Jones, MS, MPA, RDN, LD, CLT Ditch the BCAA supplements and add these whole foods to your daily meals.

Meat, poultry, and fish Beans and lentils Cheese, yogurt, and milk Whey protein Tofu and tempeh Eggs Quinoa Nuts and seeds. Rest and Recovery After Exercise. Verywell Fit uses only high-quality sources, including peer-reviewed studies, to support the facts within our articles.

Read our editorial process to learn more about how we fact-check and keep our content accurate, reliable, and trustworthy. See Our Editorial Process. Meet Our Review Board. Share Feedback. Was this page helpful? Thanks for your feedback! What is your feedback?

Related Articles. You may accept or manage your choices by clicking below, including your right to object where legitimate interest is used, or at any time in the privacy policy page. BCAAs may offer health benefits for people with cirrhosis, a chronic disease in which the liver does not function properly.

While certain sugars and antibiotics are the mainstays of treatment for hepatic encephalopathy, BCAAs may also benefit people with this condition One review of 16 studies including people with hepatic encephalopathy found that taking BCAA supplements had a beneficial effect on the symptoms and signs of the disease, but had no effect on mortality Liver cirrhosis is also a major risk factor for the development of hepatocellular carcinoma, the most common form of liver cancer, for which BCAA supplements may also be useful 28 , 29 , Several older studies have shown that taking BCAA supplements may offer protection against liver cancer in people with liver cirrhosis 31 , As such, scientific authorities recommend these supplements as a nutritional intervention for liver disease to prevent complications BCAA supplements may improve the health outcomes of people with liver disease, while also possibly protecting against liver cancer.

BCAAs are found in foods and whole protein supplements. Getting BCAAs from complete protein sources is more beneficial, as they contain all the essential amino acids. Fortunately, BCAAs are available in a variety of food sources.

This makes BCAA supplements unnecessary for most, especially if you consume enough protein in your diet already Consuming protein-rich foods will also provide you with other important nutrients that BCAA supplements lack. The best food sources of BCAAs include 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 :.

Many protein-rich foods contain high amounts of BCAAs. If you consume enough protein in your diet, BCAA supplements are unlikely to provide additional benefits.

The branched-chain amino acids BCAAs are a group of three essential amino acids: leucine, isoleucine, and valine. BCAA supplements have been shown to build muscle, decrease muscle fatigue , and alleviate muscle soreness. They have also successfully been used in a hospital setting to prevent or slow muscle loss and to improve symptoms of liver disease.

However, because most people get plenty of BCAAs through their diet, supplementing with BCAA is unlikely to provide additional benefits. Our experts continually monitor the health and wellness space, and we update our articles when new information becomes available. BCAA stands for branched-chain amino acids.

These are essential amino acids with several benefits for muscle growth and performance. While pre-workout supplements may boost your exercise performance, you may be worried about side effects. Here are 5 side effects of pre-workout…. Glutamine is an important amino acid.

This article discusses the benefits, uses and side effects of glutamine supplements. Pre-workout supplements are designed to help you gain muscle by allowing you to work out harder and longer.

Here are the 10 best pre-workout…. This is a detailed article about whey protein and its health benefits. It can help you lose weight and gain muscle, while improving your overall…. Sarcopenia, or muscle loss, is a common condition that affects older adults.

This article explains what causes sarcopenia and how to fight it. Learn about the best pre-workout nutrition strategies. Crameri RM, Aagaard P, Qvortrup K, Langberg H, Olesen J, Kjaer M Myofibre damage in human skeletal muscle: effects of electrical stimulation versus voluntary contraction.

J Physiol — Article CAS PubMed PubMed Central Google Scholar. Cruzat VF, Krause M, Newsholme P Amino acid supplementation and impact on immune function in the context of exercise. J Int Soc Sports Nutr Nat Commun Dorneles GP, Dos Passos AAZ, Romao PRT, Peres A New insights about regulatory T cells distribution and function with exercise: the role of immunometabolism.

Curr Pharm Des — Dorrell HF, Gee TI The acute effects different quantities of branched-chain amino acids have on recovery of muscle function. Sports Nutr Therapy —5.

Duan Y et al Effect of branched-chain amino acid ratio on the proliferation, differentiation, and expression levels of key regulators involved in protein metabolism of myocytes.

Nutrition — Elango R, Chapman K, Rafii M, Ball RO, Pencharz PB Determination of the tolerable upper intake level of leucine in acute dietary studies in young men.

Am J Clin Nutr — Estoche JM et al Branched-chain amino acids do not improve muscle recovery from resistance exercise in untrained young adults. Amino Acids — Fedewa MV, Spencer SO, Williams TD, Becker ZE, Fuqua CA Effect of branched-chain amino acid supplementation on muscle soreness following exercise: a meta-analysis.

Int J Vitam Nutr Res — Foure A, Bendahan D Is branched-chain amino acids supplementation an efficient nutritional strategy to alleviate skeletal muscle damage? A systematic review. Article PubMed PubMed Central Google Scholar. Foure A et al Effects of branched-chain amino acids supplementation on both plasma amino acids concentration and muscle energetics changes resulting from muscle damage: a randomized placebo controlled trial.

Clin Nutr — Gee TI, Deniel S Branched-chain aminoacid supplementation attenuates a decrease in power-producing ability following acute strength training. Greer BK, Woodard JL, White JP, Arguello EM, Haymes EM Branched-chain amino acid supplementation and indicators of muscle damage after endurance exercise.

Int J Sport Nutr Exerc Metab — Higgins JPT, Thomas J, Chandler J, Cumpston M, Li T, Page MJ, Welch VA eds Cochrane handbook for systematic reviews of interventions, 2nd edn.

Wiley, Chichester UK. Howatson G, Hoad M, Goodall S, Tallent J, Bell PG, French DN Exercise-induced muscle damage is reduced in resistance-trained males by branched chain amino acids: a randomized, double-blind, placebo controlled study. Hyldahl RD, Hubal MJ Lengthening our perspective: morphological, cellular, and molecular responses to eccentric exercise.

Muscle Nerve — Ikeda K et al Slc3a2 mediates branched-chain amino-acid-dependent maintenance of regulatory T cells. Cell Rep — Ishikura K, Miyazaki T, Ra S-G, Ohmori H The ameliorating effect of branched-chain amino acid ingestion on different types of muscle soreness after swimming and full-marathon running.

Adv Exerc Sports Physiol — Jackman SR, Witard OC, Jeukendrup AE, Tipton KD Branched-chain amino acid ingestion can ameliorate soreness from eccentric exercise.

Med Sci Sports Exerc — Jackman SR, Witard OC, Philp A, Wallis GA, Baar K, Tipton KD Branched-chain amino acid ingestion stimulates muscle myofibrillar protein synthesis following resistance exercise in humans. Front Physiol Kamei Y, Hatazawa Y, Uchitomi R, Yoshimura R, Miura S Regulation of skeletal muscle function by amino acids.

Kephart WC et al Post-exercise branched chain amino acid supplementation does not affect recovery markers following three consecutive high intensity resistance training bouts compared to carbohydrate supplementation. Kirby TJ, Triplett NT, Haines TL, Skinner JW, Fairbrother KR, McBride JM Effect of leucine supplementation on indices of muscle damage following drop jumps and resistance exercise.

Koo GH, Woo J, Kang S, Shin KO Effects of supplementation with BCAA and L-glutamine on blood fatigue factors and cytokines in juvenile athletes submitted to maximal intensity rowing performance. J Phys Ther Sci — Kurpad AV, Regan MM, Raj T, Gnanou JV Branched-chain amino acid requirements in healthy adult human subjects.

J Nutr SS. Leahy DT, Pintauro SJ Branched-chain amino acid plus glucose supplement reduces exercise-induced delayed onset muscle soreness in college-age females ISRN.

Nutrition —5. Lee JH et al Anti-inflammatory and anti-genotoxic activity of branched chain amino acids BCAA in lipopolysaccharide LPS stimulated RAW Food Sci Biotechnol — Lewis PB, Ruby D, Bush-Joseph CA Muscle soreness and delayed-onset muscle soreness.

Clin Sports Med — Lysenko EA, Vepkhvadze TF, Lednev EM, Vinogradova OL, Popov DV Branched-chain amino acids administration suppresses endurance exercise-related activation of ubiquitin proteasome signaling in trained human skeletal muscle.

J Physiol Sci — Matsumoto K, Koba T, Hamada K, Sakurai M, Higuchi T, Miyata H Branched-chain amino acid supplementation attenuates muscle soreness, muscle damage and inflammation during an intensive training program.

Mizumura K, Taguchi T Delayed onset muscle soreness: involvement of neurotrophic factors. Mohamad-Panahi P, Aminiaghdam S, Lofti N, Hatami K Effects of two different dosage of BCAA supplementation on serum indices of muscle damage and soreness in soccer players.

Pedagog Psychol Med-Biol Probl Phys Train Sports — Mueller-Wohlfahrt HW et al Terminology and classification of muscle injuries in sport: the Munich consensus statement. Br J Sports Med — Murase S et al Bradykinin and nerve growth factor play pivotal roles in muscular mechanical hyperalgesia after exercise delayed-onset muscle soreness.

J Neurosci — Murase S et al Upregulated glial cell line-derived neurotrophic factor through cyclooxygenase-2 activation in the muscle is required for mechanical hyperalgesia after exercise in rats.

Nicastro H, da Luz CR, Chaves DF, Bechara LR, Voltarelli VA, Rogero MM, Lancha AH Jr does branched-chain amino acids supplementation modulate skeletal muscle remodeling through inflammation modulation? Possible mechanisms of action.

The authors also confirmed that oral taurine administration in rats reduces exercise- and drug-induced oxidative stress [ 17 , 18 ]. Interestingly, a multi-nutrient supplement containing BCAA and taurine as well as some vitamin B and plant extracts improved inflammation and joint pain in middle-age individuals [ 19 ].

Therefore, we hypothesized that taurine might enhance the beneficial effect of BCAA on DOMS and muscle damage induced by exercise.

In the present study, we investigated by means of a randomized, placebo-controlled, double-blind trial whether a combination of BCAA and taurine supplements can provide an effective nutritional strategy for attenuating DOMS and muscle damage induced by high-intensity exercise in humans.

This randomized, placebo-controlled, double-blind trial was conducted with 36 male college volunteers who did not have any musculoskeletal disorders and had not partaken in any regular resistance training prior to the study Table 1.

The study was carried out in accordance with the Declaration of Helsinki and was approved by the Human Subjects Committee of the University of Tsukuba. All subjects provided written informed consent. Subjects were orally administered two sachets containing a combination of BCAA or placebo-1 and taurine or placebo-2 after every meal for two weeks prior to exercise Table 1 and Figure 1.

We chose this timeframe because previous studies showed a significant increase in muscular taurine concentration following two weeks of taurine administration in rats [ 18 , 20 ], but not after one week in humans [ 21 ]. Since the present study was designed as a double-blind trial, the duration of BCAA supplementation prior to exercise was matched to the two-week duration of taurine supplementation.

All subjects were instructed to fill out a supplemental checklist after every meal. The BCAA and taurine sachets contained 3. The daily doses of BCAA and taurine were based on the doses used in previous studies, which examined the effectiveness of BCAA supplementation on DOMS [ 9 , 22 ] and plasma taurine levels [ 23 ].

The daily doses per body weight of BCAA and taurine were The placebo-1 and -2 supplements were compounded to the same volume and color as the BCAA and taurine supplements, respectively, by using similar proportions of starch for the double-blind method Table 1.

Supplementation was continued in a double-blind manner until dinner on the third day after exercise. Evaluation using a visual analogue scale VAS and by assessing muscle damage markers was completed on the morning of the fourth day after exercise.

No significant differences in physical parameters measured a week before starting supplementation were noted between the groups Table 1. All subjects were sedentary men who were non-athletes.

They were instructed to continue their normal activities and to abstain from any strenuous exercise for at least one month before the experiment. Moreover, they were instructed to continue their usual food intake, not to change the amount or frequency of dietary meat or seafood intake, and not to use any dietary supplements, anti-inflammatory drugs, or anything else that could affect muscle soreness and damage until the end of the study.

They were also instructed to abstain from stretching or massage therapy during the experimental period. A schematic illustrating the experimental protocol and time course of the present study.

Participants were supplied with two kinds of sachets consists of combination of BCAA or placebo of BCAA and taurine or placebo of taurine from 2 weeks before exercise to the end of the experiment.

Participants were performed elbow extension as part of ECC in the non-dominant arm using dumbbell weight. Muscle soreness and damage were then monitored for 4 days after ECC. Figure 1 outlines the experimental protocol, including the time course corresponding to amino acid supplementation, exercise, and parameter measurement.

On the day of exercise, all subjects assembled at our laboratory at after fasting overnight. Following blood sampling, they ingested their assigned supplements 15 min prior to performing ECC.

The exercise protocol, designed to induce soreness in the elbow flexors, was modified from a previously published method of voluntary ECC [ 25 ].

During the week prior to initiating amino acid supplementation, the maximal voluntary strength of isometric contraction MVC in the non-dominant arm of each subject was measured at 1. For the ECC protocol, subjects were seated on a bench with their arm positioned in front of their body and resting on a padded support, such that their shoulder was secured at a flexion angle of 0.

Subjects performed six sets of five repetitions of elbow extension from the flexed position at 90° to the fully extended position slowly over 5 s, while maintaining a constant speed of movement by following a verbal metronome provided by the investigator.

After each extension, the investigator returned the dumbbell to the starting position 90° to prevent excess muscle activation induced by the weight. Subjects were permitted to rest for 3 s between repetitions and for 2 min between sets. The subjects also required verbal encouragement from the investigator to maintain constant speed.

Blood samples were collected from the antecubital vein at seven different time points: prior to amino acid supplementation, before exercise, immediately after exercise, at one to four days after exercise Day1—4 Figure 1. On the day of exercise, blood was collected before supplement intake, and exercise was started thereafter.

Immediately after exercise, blood was collected again. In the four days following exercise, blood was collected at before breakfast and amino acid intake. Serum was centrifuged for 30 min after the formation of a solid clot, and the plasma was immediately separated.

The serum activities of creatine kinase CK , lactate dehydrogenase LDH , and aldolase were analyzed and used as parameters of muscle damage, as described in the Japan Society of Clinical Chemistry consensus methods. Serum levels of 8-hydroxydeoxyguanosine 8-OHdG , a marker of oxidative stress-induced DNA damage, were measured before exercise and on Day 2 after exercise by competitive enzyme-linked immunosorbent assay Highly Sensitive 8-OHdG Check ELISA kit; Japan Institute for the Control of Aging, Fukuroi, Japan after purification with a kDa filter Nanosep®; Pall Corporation, NY, US.

Plasma albumin concentrations were analyzed by the bromocresol green method Albumin II-HA test Wako; Wako Pure Chemicals, Osaka, Japan. VAS scores were measured before exercise and on Days 1—4 with the arm in the extended position.

Specifically, the exercised arm was placed on a table in the seated position and the investigator passively extended the elbow joint to test the perception of soreness. Because the degree of soreness in the extended arm position was influenced by the technique of the investigator, the same investigator performed all measurements to avoid inter-investigator measurement error.

The test-retest reliability determined using an intraclass correlation coefficient ICC was 0. The upper arm circumference CIR was used as an indirect marker of muscle damage and measured before exercise, after exercise, and on Days 1—4 Figure 1. CIR was measured at five points 3, 5, 7, 9, and 11 cm proximal to the elbow joint on a relaxed arm in the standing position using a constant-tension tape.

To avoid daily variations in the measurement position, these sites on the upper arm were marked with a semi-permanent ink pen during the first testing session. CIR was measured in duplicate and the mean value of each point was used for analysis. The values immediately after exercise and on Days 1—4 were presented as the differences from the values before exercise.

The test-retest reliability determined using an ICC for CIR was 0. Data are expressed as means ± SE. The values of CK, LDH, aldolase, VAS, and CIR are presented as raw values and as the area under the curve AUC during the experimental period. The AUC was calculated as the sum of four or five trapezoid areas separated by each measurement time point.

Analysis was conducted using SPSS software version Figure 2 shows the plasma concentrations of taurine, total BCAA, and individual BCAAs prior to amino acid supplementation, before exercise, and on Days 1 and 4.

Prior to supplementation, there were no significant differences in plasma taurine concentration among the groups Figure 2 A. Before exercise and on Days 1 and 4, the plasma taurine concentration in the TAU and COMB groups was significantly increased compared with that in the PLCB and BA groups Figure 2 A.

No significant differences in the plasma concentrations of total BCAA and individual BCAAs valine, leucine, or isoleucine were observed among the groups at any time points Figure 2 B-E.

Plasma taurine A , BCAA B , valine C , leucine D and isoleucine E concentrations. Data are expressed as means ± S. The plasma albumin concentration 4.

Figure 3 A shows the VAS scores for subjective DOMS assessment. The VAS scores in all groups were significantly higher on Day 1 compared with before exercise. The VAS scores in the BA and COMB groups peaked on Day 1 while those in the PLCB and TAU groups peaked on Day 2. The increased VAS scores in all groups declined by Day 4.

In the COMB group, the VAS scores on Day 2 were significantly lower than in the PLCB group. VAS score A and CIR B throughout the experiment. VAS score was used as subjectively assessment of muscle soreness in the exercised arm.

CIR value as an indirect marker of muscle damage is presented as differences from the respective BEx. Both parameters were also shown as the AUC from BEx to Day4. Abbreviations : VAS , visual analog scale; AUC , area under the curve; CIR , upper arm circumference. CIR as an indirect marker of muscle damage is shown in Figure 3 B.

CIR differences increased significantly and immediately after exercise in all groups and declined by Day 1. Thereafter, the CIR differences in all groups increased significantly until the end of the experimental period. In the COMB group, the CIR differences were lower than in the other groups throughout the experimental period, with significant differences on Days 2 and 3 compared with the PLCB group.

Additionally, the AUC of the CIR differences in the COMB group was significantly lower than in the PLCB group.

No significant differences in CIR were observed among the PLCB, BA, or TAU groups throughout the experimental period. The serum enzyme activities throughout the experimental period of CK, LDH, and aldolase, which serve as blood parameters of muscle damage, are presented in Figure 4. All serum markers remained unchanged in all groups until Day 1 and then increased from Day 2 to Day 4.

Serum activities of CK A , LDH B , and aldolase C throughout the experimental period. The AUC of these parameters calculated through the experimental period was also shown.

Serum CK activity in the PLCB, BA, and TAU groups was significantly higher on Days 3 and 4 compared with before exercise Figure 4 A. In the COMB group, a significant difference in CK activity compared with before exercise was found only on Day 4.

Statistically significant differences among all groups was not found at any points throughout the experiment due to the large variance between individuals. Serum LDH activity from Day 1 to Day 3 and the AUC were significantly lower in the COMB group than in the PLCB group Figure 4 B.

Similarly, serum aldolase activity in the COMB group was lower than in other groups, and a significant difference was noted only before exercise on Day 4 Figure 4 C. The AUC of aldolase was significantly lower in the COMB group than in the PLCB group.

Figure 5 shows serum 8-OHdG levels before exercise and on Day 2. Before exercise, there was no significant difference in serum 8-OHdG levels between any groups.

Serum 8-OHdG levels in the PLCB, BA, and TAU groups were significantly increased on Day 2 compared with before exercise.

On Day 2, 8-OHdG levels were significant lower in the COMB group than in the PLCB and BA groups. Serum 8-OHdG level at BEx and Day2. Abbreviations : 8-OHdG , 8-hydroxydeoxyguanosine; BEx , before exercise; Day2 , 2nd day after exercise. Data are shown as means ± S. Numerous studies have confirmed the effectiveness of BCAA supplementation on DOMS and muscle damage [ 4 , 7 — 11 ].

However, the attenuating effects of BCAA on the DOMS and muscle damage were occasionally limited, especially in case of intensive exercise.

Consequently, more effective nutritional strategies need to be discovered. In the present study, the effects of BCAA supplementation combined with taurine on a highly intense ECC-induced DOMS and muscle damage were investigated via a randomized, placebo-controlled, and double-blind trial, because taurine was reported to decrease oxidative stress induced by ECC [ 16 ].

In ECC-induced DOMS and muscle damage, subjective and objective parameters including VAS scores, CIR, and serum levels of LDH and 8-OHdG were significantly improved by the combination of BCAA and taurine supplementation. This combined supplementation also tended to improve serum CK and aldolase activities, but not significantly.

These parameters, especially serum CK activity, have a high degree of individual biological variability, and it is difficult to demonstrate a statistically significant difference between the small number of subjects [ 3 ].

Overall, the present study demonstrated that combined supplementation with BCAA and taurine is beneficial for reducing ECC-induced DOMS and muscle damage. However, it was impossible to determine whether the combined effects were due to the synergistic effect of both BCAA and taurine or the sum of the individual effects.

Compared with the effectiveness of BCAA supplementation on exercise-induced muscle soreness and damage reported in previous studies [ 4 , 7 , 9 , 22 , 25 ], BCAA supplementation alone was not sufficient to effectively inhibit muscle soreness and damage in the present study.

This discrepancy might be due to differences in the exercise protocol intensity and type and the supplemental regimen duration and dose. In a previous study by Shimomura et al. The present findings with this higher intensity suggest that a combination of BCAA and taurine taken during high-intensity exercise may prevent severe muscle soreness and damage that cannot be attenuated by BCAA alone.

In addition to exercise intensity, the amount of oral BCAA intake is one of the important factors for preventing exercise-induced muscle soreness and damage. The BCAA dose in the present study should be sufficient because daily BCAA supplementation at 9.

Furthermore, the overall BCAA intake was probably sufficient because amino acid supplementation was from two weeks before to three days after exercise throughout the whole experimental period. Therefore, both the amount per body mass and the duration of BCAA supplementation in the present study might be sufficient for attenuating DOMS and muscle damage.

However, plasma BCAA concentrations were not altered by the BCAA supplementation in the present study. The two-week duration of BCAA supplementation prior to exercise was used to match the duration of taurine supplementation because this study was a double-blind trial.

Hamada et al. reported that the plasma BCAA concentration in healthy humans significantly and rapidly increased and peaked at 30 min after a single BCAA dose; however, the plasma concentration returned to the basal level within 1—2 h [ 28 ] because of transport to the skeletal muscle [ 24 ].

Since blood sampling in the present study was done before each BCAA supplementation, the plasma BCAA concentration should have already returned to the basal level by the sampling time. Taurine content in the skeletal muscle is also thought to be important for preventing muscle damage; however, neither the optimal duration nor the total dose of taurine has been clarified.

We previously confirmed in rats that two weeks of oral taurine administration significantly increases taurine concentration in both the skeletal muscle and plasma in a dose-dependent manner [ 20 , 26 ].

In the present study, oral taurine administration at 6. Therefore, we suggest that the taurine concentration in the skeletal muscle in the present study might have been increased in line with the plasma level. However, a previous study with humans reported that seven days of oral taurine supplementation 5.

This discrepancy between the present results and those of previous studies with humans might be due to differences in the supplemental protocol. Therefore, an effective protocol for taurine supplementation, including dose and duration, to increase muscle taurine concentration as well as plasma level should be clarified in the future.

Interestingly, Galloway et al. Available Now! Click Here. Don't Forget:. Left Right. Check out. Start shopping. Search Shop Ingredients About Us Articles Contact Us. Account Search Cart. Rapid Recovery. Shop Toggle menu Action Grape Action Lemon Rapid Recovery Accessories.

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Do BCAAs Break A Fast? Mango Ginger Recovery Smoothie Green Goddess Recovery Smoothie Tropical Bliss Recovery Smoothie Berry Blast Protein Smoothie Peanut Butter Banana Recovery Smoothie.

Guide: Best Times to Drink BCAAs. Do BCAAs Help with Muscle Soreness? How Much BCAAs Do I Need to Help with Muscle Soreness?

When to Take BCAA Supplements for Muscle Soreness As mentioned above, studies 2 have shown that BCAAs are most effective for helping with muscle soreness when taken immediately before your workout, generally within half an hour of starting.

Share Facebook Share on Facebook Twitter Share on Twitter Pinterest Pin it. July 30, — amino VITAL. These results were corroborated by an earlier study in Japan 3 which demonstrated that BCAA supplements can both lower muscle damage incurred during exercise and also boost muscle protein synthesis.

For experienced trainers who engage in intensive exercise we recommend a dose of between 0. Essential amino acid formulas, casein hydrolysate Peptopro or Whey Protein Hydrolysate can all be used in place of BCAA supplements as they contain high amounts of BCAAs as well as other benefits.

Like our article? Let us know on Facebook and be sure to check out our other articles for more great reads! Howatson et. al : Exercise-induced muscle damage is reduced in resistance-trained males by branched chain amino acids: a randomized, double-blind, placebo controlled study.

Matsumoto K et. al : Branched-chain amino acid supplementation attenuates muscle soreness, muscle damage and inflammation during an intensive training program. Shimomura Y et.

When strength-training, ISSN says you may need at least 1. Adding protein to your diet is easy. Make your oatmeal with milk, add beans and nuts to your grilled chicken salad, and snack on hard-boiled eggs and low-fat yogurt. It gives your muscles the time it needs to repair and strengthen in between workouts, adapt to the stress, and replenish energy stores.

So you may not need to take BCAAs to recover from your workouts. What you do need is proper nutrition , rehydration, and adequate sleep. At Verywell Fit, we aim to provide the facts behind the fads, especially when it comes to products and health habits that are popular but may not be entirely rooted in science.

When it comes to supplements, including items like BCAAs, be a cautious consumer. While there are some purported health benefits of BCAA supplements, the science is limited.

Instead of reaching for a product that may not provide everything the label claims, we suggest looking to adequate fiber and hydration, balanced nutrition, good sleep hygiene, daily movement, and other positive lifestyle factors to ensure you feel your best.

If you do choose to supplement your diet with BCAAs, speak with a healthcare professional and registered dietitian nutritionist to decide which product and dosage is best for you.

VanDusseldorp TA, Escobar KA, Johnson KE, et al. Effect of branched-chain amino acid supplementation on recovery following acute eccentric exercise. National Institutes of Health.

National Library of Medicine. Amino acids. Holeček M. Branched-chain amino acids in health and disease: metabolism, alterations in blood plasma, and as supplements.

Nutr Metab Lond. Wolfe RR. Branched-chain amino acids and muscle protein synthesis in humans: myth or reality? J Int Soc Sports Nutr. Published Aug Office of Dietary Supplements. Dietary supplements for exercise and athletic performance.

Jäger, R. et al. International Society of Sports Nutrition Position Stand: protein and exercise. J Int Soc Sports Nutr 14, 20 Jackman SR, Witard OC, Philp A, Wallis GA, Baar K, Tipton KD. Branched-chain amino acid ingestion stimulates muscle myofibrillar protein synthesis following resistance exercise in humans.

Front Physiol. AbuMoh'd MF, Matalqah L, Al-Abdulla Z. Effects of oral branched-chain amino acids BCAAs intake on muscular and central fatigue during an incremental exercise. J Hum Kinet. National Organization for Rare Disorders. Maple syrup urine disease.

Doherty R, Madigan SM, Nevill A, Warrington G, Ellis JG. The sleep and recovery practices of athletes. By Jill Corleone, RD Jill is a registered dietitian who's been learning and writing about nutrition for more than 20 years.

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By Jill is a registered dietitian who's been writing about nutrition, health, and fitness for more than 20 years. Jill Corleone, RD. Learn about our editorial process. Learn more. Medical Reviewers confirm the content is thorough and accurate, reflecting the latest evidence-based research.

Content is reviewed before publication and upon substantial updates. Medically reviewed by Jonathan Valdez, RDN, CDCES, CPT. Learn about our Medical Review Board. Table of Contents View All.

Table of Contents. What are BCAAs? What Does the Research Say? Are BCAAs Harmful? Best Ways to Boost BCAAs. Food Sci Biotechnol — Lewis PB, Ruby D, Bush-Joseph CA Muscle soreness and delayed-onset muscle soreness. Clin Sports Med — Lysenko EA, Vepkhvadze TF, Lednev EM, Vinogradova OL, Popov DV Branched-chain amino acids administration suppresses endurance exercise-related activation of ubiquitin proteasome signaling in trained human skeletal muscle.

J Physiol Sci — Matsumoto K, Koba T, Hamada K, Sakurai M, Higuchi T, Miyata H Branched-chain amino acid supplementation attenuates muscle soreness, muscle damage and inflammation during an intensive training program.

Mizumura K, Taguchi T Delayed onset muscle soreness: involvement of neurotrophic factors. Mohamad-Panahi P, Aminiaghdam S, Lofti N, Hatami K Effects of two different dosage of BCAA supplementation on serum indices of muscle damage and soreness in soccer players.

Pedagog Psychol Med-Biol Probl Phys Train Sports — Mueller-Wohlfahrt HW et al Terminology and classification of muscle injuries in sport: the Munich consensus statement.

Br J Sports Med — Murase S et al Bradykinin and nerve growth factor play pivotal roles in muscular mechanical hyperalgesia after exercise delayed-onset muscle soreness.

J Neurosci — Murase S et al Upregulated glial cell line-derived neurotrophic factor through cyclooxygenase-2 activation in the muscle is required for mechanical hyperalgesia after exercise in rats. Nicastro H, da Luz CR, Chaves DF, Bechara LR, Voltarelli VA, Rogero MM, Lancha AH Jr does branched-chain amino acids supplementation modulate skeletal muscle remodeling through inflammation modulation?

Possible mechanisms of action. J Nutr Metab Nikolaidis MG, Paschalis V, Giakas G, Fatouros IG, Koutedakis Y, Kouretas D, Jamurtas AZ Decreased blood oxidative stress after repeated muscle-damaging exercise.

Nosaka K, Clarkson PM Changes in indicators of inflammation after eccentric exercise of the elbow flexors. Nosaka K, Sacco P, Mawatari K Effects of amino acid supplementation on muscle soreness and damage.

Osmond AD et al The effects of leucine-enriched branched-chain amino acid supplementation on recovery after high-intensity resistance exercise. Int J Sports Physiol Perform — Owens DJ, Twist C, Cobley JN, Howatson G, Close GL Exercise-induced muscle damage: what is it, what causes it and what are the nutritional solutions?

Eur J Sport Sci — Pallottini AC, Sales CH, Vieira D, Marchioni DM, Fisberg RM Dietary BCAA intake is associated with demographic, socioeconomic and lifestyle factors in residents of Sao Paulo, Brazil. Paulsen G, Mikkelsen UR, Raastad T, Peake JM Leucocytes, cytokines and satellite cells: what role do they play in muscle damage and regeneration following eccentric exercise?

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Free Radic Biol Med — Download references. The authors would like to thank the Coordenação de Aperfeiçoamento de Pessoa de Nível Superior CAPES and Conselho Nacional de Pesquisa e Desenvolvimento tecnológico CNPq for the grant to TRA grant n.

Conselho Nacional de Pesquisa e Desenvolvimento tecnológico CNPq for the grant to TRA grant n. Research Group in Tissue Regeneration, Adaptation and Repair, State University of Londrina, Londrina, Brazil.

Research Group in Tissue Regeneration, Adaptation and Repair, Federal University of Jataí, Jataí, Brazil. Western São Paulo University, Presidente Prudente, Brazil. Department of Physics, State University of Londrina, Londrina, Brazil. Research Group in Tissue Regeneration, Adaptation and Repair, Center of Biological Sciences, State University of Londrina, Rodovia Celso Garcia Cid PR km, Londrina, Paraná, CEP: , Brazil.

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