- The 9 essential amino acids are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine.
- Amino acids are organic compounds that join together to create proteins, which are essential for building and repairing tissues in the body, as well as providing us with energy.
- Free-form essential amino acids may be more useful than protein in certain cases, as they are absorbed more quickly and provide a high concentration of amino acids in the blood almost immediately.
What are the essential amino acids?
There are 9 amino acids that are essential for our body, which means that we cannot produce them ourselves and must obtain them from external sources, such as food.
It is necessary to consume these essential amino acids regularly through a healthy and balanced diet.
| Amino acids | Chicken | Evoeaas | Soy |
| Leucine | 1,8 | 27,3 | 2,4 |
| Isoleucine | 0,9 | 8,5 | 1 |
| Valine | 1 | 2,2 | 1 |
| Lysine | 2,2 | 13,9 | 3,1 |
| Methionine | 2 | 2,1 | 0,9 |
| Threonine | 1 | 8,5 | 0,8 |
| Tryptophan | – | 2,1 | 0,072 |
| Histidine | 0,7 | 2,2 | 1,6 |
| Phenylalanine | 0,8 | 2,1 | 1,62 |
Table I. Comparison of the amino acid profiles of chicken breast, soybeans and EvoEaas (expressed per 100g of product) (Bernard, Mahungu & Eric, 2018; Srinivas et al. 2015).
Functions of essential amino acids
Essential amino acids (EAAs) play a fundamental role in the human body, especially for athletes seeking to improve their performance and stay healthy. These are their main functions:
Protein synthesis
- Essential amino acids are the basic building blocks for protein synthesis in the body.
- Proteins are essential for muscle repair and growth, as well as for athletes seeking to increase muscle mass, recover from injuries or improve their strength and endurance.
Stimulation of anabolic hormone synthesis
- Some EAAs, such as leucine, are key to activating the mTOR pathway, which stimulates protein production and anabolic hormones such as insulin and IGF-1.
- These hormones are essential for muscle growth and tissue repair.
Improved muscle recovery
- EAAs, especially leucine, help reduce muscle breakdown and speed up recovery after exercise.
Increased endurance and reduced fatigue
- Some essential amino acids, such as isoleucine and valine, are known as branched-chain amino acids (BCAAs) and may help improve endurance and reduce fatigue during prolonged exercise.
- BCAAs may reduce the concentration of tryptophan in the brain, which in turn reduces serotonin production and delays the onset of fatigue.
Strengthening the immune system
- Essential amino acids also play a role in strengthening the immune system.
- EAAs can help maintain a healthy immune system, which is essential for preventing illness and maintaining optimal athletic performance.
When is it advisable to take essential amino acid supplements?
It is an ideal sports supplement for:
- Breaking a fast and quickly supplying amino acids, especially if you train in the morning.
- As a pre-workout to ensure the rapid release of amino acids into the bloodstream.
- As an intra-workout to supply amino acids while exercising, a time when splanchnic blood flow is reduced by up to 80% (Qamar, 1987, cited in De Oliveira, Burini & Jeukendrup, 2014), causing our digestive capacity to decrease drastically during this period.
It may also be useful for:
- People with irritable bowel syndrome (IBS), small intestinal bacterial overgrowth (SIBO), or other conditions characterised by intestinal permeability, as consuming free-form amino acids eliminates the enzymatic activity required for protein breakdown.
- People following fasting protocols to improve digestive symptoms generally resulting from a bulking phase with a high calorie intake.
What is the best time to take them?
Essential amino acids can be consumed at any time of day, as they are absorbed very quickly and, for practical purposes, act in the same way as a protein.
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Bibliographic Sources
- de Oliveira, E. P., Burini, R. C., & Jeukendrup, A. (2014). Gastrointestinal complaints during exercise: prevalence, etiology, and nutritional recommendations. Sports Medicine (Auckland, N.Z.), 44 Suppl 1(Suppl 1), S79-85.
- Gorissen, S. H. M., Burd, N. A., Hamer, H. M., Gijsen, A. P., Groen, B. B., & van Loon, L. J. C. (2014). Carbohydrate coingestion delays dietary protein digestion and absorption but does not modulate postprandial muscle protein accretion. The Journal of Clinical Endocrinology and Metabolism, 99(6), 2250–2258.
- Gorissen, S. H. M., Burd, N. A., Kramer, I. F., van Kranenburg, J., Gijsen, A. P., Rooyackers, O., & van Loon, L. J. C. (2017). Co-ingesting milk fat with micellar casein does not affect postprandial protein handling in healthy older men. Clinical Nutrition (Edinburgh, Scotland), 36(2), 429–437.
- Hoffman, J. R., & Falvo, M. J. (2004). Protein – Which is Best? Journal of Sports Science & Medicine, 3(3), 118–130.
- MacDonald, A., Singh, R. H., Rocha, J. C., & van Spronsen, F. J. (2019). Optimising amino acid absorption: essential to improve nitrogen balance and metabolic control in phenylketonuria. Nutrition Research Reviews, 32(1), 70–78.
- Oloo, B., S., M., Kahi, A., & Amonsou, E. (2018). Quantity and Functionality of Protein Fractions Isolated from 3 Ecotypes of Indigenous Chicken in Kenya. Food Science and Nutrition Studies, 2, 70.
- Rayaprolu, S., Hettiarachchy, N., Horax, R., Satchithanandam, E., Chen, P., & Mauromoustakos, A. (2015). Amino Acid Profiles of 44 Soybean Lines and ACE-I Inhibitory Activities of Peptide Fractions from Selected Lines. Journal of the American Oil Chemists’ Society, 92(7), 1023–1033.
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