Amino acids are organic compounds that combine to form proteins, which are often referred to as the ‘building blocks’ of life.1
There is a total of 20 amino acids that comprise muscle protein; 9 of which are considered to be ‘essential’, meaning they cannot be produced by the body in physiologically significant amounts, and therefore must be consumed through diet. For synthesis of new muscle protein, all 20 amino acids must be present in adequate amounts.2 Physiological regulation of skeletal muscle mass is determined and maintained, in large, by dietary protein intake.
A growing body of research suggests that increasing dietary protein consumption beyond currently recommended amounts, can aid in the regulation of skeletal muscle mass and optimise tissue reconditioning in response to exercise, as noted in healthy participants and elderly.3
A study conducted in 20 resistance trained, healthy young males found that mycoprotein stimulated resting and post-exercise muscle protein synthesis rates, and to a greater extent compared with milk protein.
What does the science say about mycoprotein?
A study investigated the impact of mycoprotein ingestion in 12 healthy young males on the levels of amino acids and insulin in the blood and found that mycoprotein resulted in slower but more sustained rise in levels of insulin and amino acids compared with milk protein. These results demonstrate that mycoprotein, if consumed in sufficient quantities, can support skeletal muscle growth and reconditioning and therefore have utility in muscle health in a variety of populations.3
Milk proteins are a typical animal source of dietary protein, particularly for those who take part in intense exercise and/or resistance training and interestingly, mycoprotein ingestion results in amino acid and leucine availability similar to that following milk protein consumption. A study conducted in 20 resistance trained, healthy young males found that mycoprotein stimulated resting and post-exercise muscle protein synthesis rates to a greater extent than milk protein. These data suggest mycoprotein’s potential as an effective alternative dietary protein source to support post exercise muscle tissue synthesis.6
Incorporating mycoprotein into a dietary plan
In recent years, a growing body of work has suggested that protein intakes above current guidelines could assist with healthy ageing.4 Age is associated with progressive loss of muscle mass, known as sarcopenia, and can increase the risk of injury and disability. A decline in intake of dietary protein is thought to be a contributing factor. There are some data to suggest that excess leucine may be able to overcome this age-related challenge,7 thus, Quorn® products may be a beneficial addition to the diets of older individuals who are looking to manage or prevent loss of muscle mass by increasing dietary protein intake. As such, current and future research is looking to investigate the effects of mycoprotein on healthy ageing in larger sample sizes and diverse populations.
There is also evidence to suggest that skeletal muscle turnover is not only a concern in the aging population, but also the younger more sedentary population.8 Because of their high protein and low fat content, Quorn products may be used as a meat-alternative to supplement the diets of these individuals to ensure they are meeting the requirements for protein intake, whilst avoiding a high caloric intake.
Research and evidenceExplore all research and evidence
- MedlinePlus. Amino acids. Available at: https://medlineplus.gov/ency/article/002222.htm. Accessed December 2019.
- Wolfe RR. J Int Soc Sports Nutr. 2017;14:30.
- Dunlop MV, et al. Br J Nutr. 2017;118:673–85.
- Quorn. Protein Guidelines. Why the time is right for an update. Available at: https://www.mycoprotein.org/files/Protein_White_Paper_140619.pdf. Accessed December 2019.
- Edwards DG, Cummings JH. Proceedings of the Nutrition Society, 69(OCE4), E331. doi:10.1017/S0029665110001400.
- Monteyne AJ, et al. Abstract presented at ECSS 2019.
- Fujita S, Volpi E. J Nutr. 2006;136(1 Suppl):277S–80S.
- McGregor RA, Poppitt SD. Nutr Metab (Lond). 2013;10:46.