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The human body's thousands of distinct proteins are made up of 20 different amino acids.
Because of their potential to enhance muscle regeneration, Branched Chained Amino Acids have become a mainstay for athletes all over the world. Leucine, isoleucine, and valine are the three primary amino acids in our BCAA Gummies. Together, they serve as essential building blocks in the fight against muscle loss and protein breakdown.
Out of the 20 different amino acids, 9 of the 20 amino acids are deemed essential, which means they can't be synthesized by your body and must be received through food.
The branched-chain amino acids (BCAAs) are three of the nine essential amino acids: leucine, isoleucine, and valine.
The molecular structure of BCAAs, which are present in protein-rich foods including eggs, meat, and dairy products, is referred to as "branched-chain." They're also a well-liked dietary supplement that comes in powder form.
BCAAs make up roughly 35% of your body's muscle protein, which is why eating adequate BCAAs is so important for effective muscle building and maintenance.
The three branched chain amino acids (BCAAs), named for their nonlinear ("branched") carbon atom structure, are leucine, isoleucine, and valine. Proteins, as you surely know, are made up of amino acids, which are the building blocks of proteins. Amino acids are either manufactured by the body (referred to as "non-essential") or must be obtained from food (referred to as "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. BCAAs provide an additional fuel source for working muscle, as BCAA breakdown for energy increases during prolonged exercise. They also play an important role in overall protein turnover, and regulate whether the body is in a recovery or breakdown state.
Bacillus Calmette-like amino acids (BCAA) are important for a number of reasons, including the fact that they bypass liver breakdown and provide an additional fuel source for working muscle. BCAAs also play an important role in overall protein turnover and regulate whether the body is in a recovery (tissue building) or catabolic state - i.e. whether it needs extra energy to maintain its protein turnover levels.
Of the BCAAs, leucine has been shown to initiate muscle protein synthesis (building) and inhibit protein breakdown (reduction). 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.
One of the many advantages of BCAAs is their role in the development and maintenance of lean muscle mass. According to a study published in the Journal of Nutrition, BCAAs, specifically Leucine, have anabolic effects on protein metabolism by increasing the rate of muscle protein synthesis and decreasing the rate of protein degradation, or breakdown. [1]
The metabolic process that describes the incorporation of amino acids into bound skeletal muscle proteins is known as muscle protein synthesis (MPS). Muscle proteins are divided into two groups: contractile myofibrillar proteins (such as myosin, actin, tropomyosin, and troponin) and energy-producing mitochondrial proteins.
Muscle protein synthesis occurs as a result of intense physical stress, which is caused by micro-tears and mini-trauma to the muscle tissue during training. By taking BCAAs before or during your workout, you will stimulate protein synthesis, which will aid in the development of lean muscle mass and strength.
In one study, people who drank a drink containing 5.6 grams of BCAAs after a resistance workout had a 22% higher increase in muscle protein synthesis than those who drank a placebo drink. [2]
However, this increase in muscle protein synthesis is approximately 50% lower than what was observed in other studies where people consumed a whey protein shake containing a comparable amount of BCAAs. [3,4]
Although, we understand there are several factors, including workout intensity, duration, and fitness level, that can contribute to fatigue during intense periods of exercise. According to research, BCAAs can help to delay muscle fatigue by restoring tryptophan levels, a chemical that converts to serotonin, which can cause fatigue.
One mechanism that has been proposed as a potential factor in fatigue is the level of 5-hydroxytryptamine (5-HT). Tryptophan crosses the blood-brain barrier during exercise, where it is converted to 5-hydroxytryptamine (5-HT), or serotonin. Higher serotonin levels during exercise alert the brain that your body is fatigued, resulting in less muscle endurance.
The amount of tryptophan and other available amino acids, including BCAAs, which are transported along the same carrier pathway, influence 5-HT transport. While BCAAs and tryptophan compete to cross the blood-brain barrier, BCAAs almost always win. [5]
It's not uncommon to feel sore a day or two after a workout, especially if you're starting a new exercise routine. This is known as delayed onset muscle soreness (DOMS). Delayed-onset muscle soreness (DOMS) is muscle pain that begins after you’ve worked out. It normally starts a day or two after a workout. You won’t feel DOMS during a workout and it occurs 12 to 24 hours after exercise and can last up to 72 hours.
While the exact cause of DOMS is unknown, researchers believe it is caused by tiny tears in the muscles after exercise. BCAAs have been shown to reduce muscle damage, which may help to shorten the duration and severity of DOMS. Several studies have found that BCAAs reduce protein breakdown during exercise and lower levels of creatine kinase, an indicator of muscle damage. [6,7,8]
BCAAs can aid in the prevention of muscle wasting or breakdown.
Muscle proteins are constantly broken down and rebuilt (synthesized). The amount of protein in muscle is determined by the balance of muscle protein breakdown and synthesis When protein breakdown exceeds muscle protein synthesis, muscle wasting or breakdown occurs.
Muscle wasting is a sign of malnutrition and can occur as a result of chronic infections, cancer, fasting periods, or as a natural part of the aging process. BCAAs account for 35% of the essential amino acids found in muscle proteins in humans. They supply 40% of the total amino acids required by your body. [9]
First, we have to understand what Peak performance power is and why it is important.
Peak power is defined as the maximum output or production of work in a given amount of time. Peak power is an important metric for endurance athletes and powerlifters because it accounts for a combination of strength, velocity, force, and neuromuscular adaptations when performed at 90-100 percent of maximum heart rate capacity for a short period of time.
More peak power is directly related to improved athletic performance. You'll be able to improve time trials, sprint performance, load, and outperform the competition if you can generate more power during a max effort.
A quick study from Auburn University's School of Kinesiology conducted took a time frame of 10-weeks to conduct a randomized double-blind controlled study with trained cyclists to examine the effects of BCAA supplementation on select body composition, performance, and immune health over a 10-week training season. 18 trained cyclists were given 12g of BCAAs or a maltodextrin placebo daily. Peak power performance and average power increased by 19%, according to the results. This study thus concluded again that more peak power is linearly related to a direct increase in athletic performance. [10]
In conclusion, the branched-chain amino acids (BCAAs) are a class of three essential amino acids that include leucine, isoleucine, and valine. They are essential, which means that your body cannot produce them and must obtain them from food. BCAA supplements have been shown to increase muscle mass, decrease fatigue, and reduce muscle soreness in athletes.
[1] Eva Blomstrand, Jörgen Eliasson, Haåkan K. R. Karlsson, Rickard Köhnke, Branched-Chain Amino Acids Activate Key Enzymes in Protein Synthesis after Physical Exercise, The Journal of Nutrition, Volume 136, Issue 1, January 2006, Pages 269S–273S, https://doi.org/10.1093/jn/136.1.269S
[2] Jackman, S. R., Witard, O. C., Philp, A., Wallis, G. A., Baar, K., & Tipton, K. D. (2017). Branched-Chain Amino Acid Ingestion Stimulates Muscle Myofibrillar Protein Synthesis following Resistance Exercise in Humans. Frontiers in physiology, 8, 390. https://doi.org/10.3389/fphys.2017.00390
[3] Churchward-Venne, T. A., Burd, N. A., Mitchell, C. J., West, D. W., Philp, A., Marcotte, G. R., Baker, S. K., Baar, K., & Phillips, S. M. (2012). Supplementation of a suboptimal protein dose with leucine or essential amino acids: effects on myofibrillar protein synthesis at rest and following resistance exercise in men. The Journal of physiology, 590(11), 2751–2765. https://doi.org/10.1113/jphysiol.2012.228833
[4] Witard, O. C., Jackman, S. R., Breen, L., Smith, K., Selby, A., & Tipton, K. D. (2014). Myofibrillar muscle protein synthesis rates subsequent to a meal in response to increasing doses of whey protein at rest and after resistance exercise. The American journal of clinical nutrition, 99(1), 86–95. https://doi.org/10.3945/ajcn.112.055517
[5] Blomstrand E. A role for branched-chain amino acids in reducing central fatigue. J Nutr. 2006 Feb;136(2):544S-547S. doi: 10.1093/jn/136.2.544S. PMID: 16424144.
[6] MacLean, D. A., Graham, T. E., & Saltin, B. (1994). Branched-chain amino acids augment ammonia metabolism while attenuating protein breakdown during exercise. The American journal of physiology, 267(6 Pt 1), E1010–E1022. https://doi.org/10.1152/ajpendo.1994.267.6.E1010
[7] 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, 20. https://doi.org/10.1186/1550-2783-9-20
[8] Coombes, J. S., & McNaughton, L. R. (2000). Effects of branched-chain amino acid supplementation on serum creatine kinase and lactate dehydrogenase after prolonged exercise. The Journal of sports medicine and physical fitness, 40(3), 240–246.
[9] 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 Suppl), 1583S–1587S. https://doi.org/10.1093/jn/134.6.1583S
[10] Kephart WC, Wachs TD, Thompson RM, Brooks Mobley C, Fox CD, McDonald JR, Ferguson BS, Young KC, Nie B, Martin JS, Company JM, Pascoe DD, Arnold RD, Moon JR, Roberts MD. Ten weeks of branched-chain amino acid supplementation improves select performance and immunological variables in trained cyclists. Amino Acids. 2016 Mar;48(3):779-789. doi: 10.1007/s00726-015-2125-8. Epub 2015 Nov 9. Erratum in: Amino Acids. 2018 Oct;50(10):1495. Mac Thompson R [corrected to Thompson RM]. PMID: 26553453.
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