What are EAAs and why should I take them?

Just in time for the release of our new Premium EAA flavor peach iced tea, we would like to explain to you in the following blog post what EAAs are all about and why it can make sense to take EAAs.

The abbreviation EAA stands for Essential Amino Acids.

Proteins, which are among other things the basic substance of our muscles, consist of individual amino acids that are connected to each other via so-called peptide bonds. Amino acids are therefore the building blocks of proteins. Although there are several hundred different amino acids that have a function in the human body, not all of these amino acids are actually used to build proteins. Depending on the literature source, there are 20 (or 21 with selenocysteine) so-called proteinogenic amino acids, which means that these amino acids are used to build proteins.

The proteinogenic amino acids can be further divided into essential and non-essential amino acids. Essential amino acids, as the name suggests, cannot be synthesized independently by the human organism and must therefore be supplied through food (Wolfe 2017). According to the World Health Organization (WHO) and the European Food Safety Authority (EFSA), the nine amino acids L-leucine, L-isoleucine, L-valine (the three branched chain amino acids; BCAA), L-lysine, L-methionine, L-tryptophan, L-threonine, L-histidine and L-phenylalanine are classified as essential (WHO 2007; EFSA 2015).

The availability of amino acids plays a particularly important role in muscle protein metabolism, since the synthesis of new muscle protein requires a sufficient availability of free amino acids (Tipton et al. 1999). After the training stimulus or during the recovery phase, the rate of muscle protein synthesis is regulated by the concentration of essential amino acids in the blood plasma (Jäger et al. 2017). According to current data, 10-12 g EAAs, of which 1-3 g L-leucine, are considered an adequate dosage to stimulate muscle protein synthesis and ensure a positive nitrogen balance (Jäger et al. 2017).

As mentioned above, L-leucine is one of the well-known BCAAs, which are characterized by their branched side chain in their chemical structure. L-leucine stimulates the so-called mTor signaling pathway (mammalian target of rapamycin) and thus myofibrillar protein synthesis, which is why the amino acid plays a key role as a signaling molecule.

Over the course of life, muscles are subject to constant building and breakdown processes (“muscle protein breakdown”). An increase in (skeletal) muscle mass is based on a positive ratio of muscle protein building (muscle protein synthesis) to muscle protein breakdown, which can be achieved, for example, through strength training and a protein-rich diet (Tipton et al. 2004; Phillips and van Loon 2011; Wolfe 2017). This positive ratio, or anabolic (building) state, can be achieved on the one hand by stimulating muscle protein synthesis and on the other hand by inhibiting muscle protein breakdown (Wolfe 2017).

Both resistance training (strength training) and the intake of dietary protein have been shown to result in an acute stimulation of muscle protein synthesis (Jäger et al. 2017). In addition, it has been shown that these effects exhibit synergism, which means that the combination of resistance training and sufficient protein intake increases muscle protein synthesis more than either individual intervention (Jäger et al. 2017). Since resistance training increases muscle protein synthesis for up to 24 hours, sufficient protein intake within this time window plays a crucial role in optimizing body composition (body composition; ratio of fat-free mass to body fat) (Jäger et al. 2017).

Numerous studies show that protein supplementation improves physical performance and recovery and increases muscle growth, muscle strength and lean body mass (Stark et al. 2012).

If all nine essential amino acids are not available in sufficient quantities, muscle protein synthesis is limited and cannot be increased to its maximum (Wolfe 2017). Taking BCAAs alone can improve the efficiency of amino acid recycling by reusing the amino acids released by muscle breakdown to build new proteins through BCAA-induced stimulation of muscle protein synthesis.

Due to the lack of additional building blocks, taking BCAAs alone cannot lead to muscle growth, as protein buildup cannot exceed protein breakdown. Muscle growth is only possible if all nine essential amino acids are supplied to the body.

With regard to nutrient timing, current scientific evidence shows that the intake of protein or amino acids before, during and after training increases muscle protein synthesis (Kerksick et al. 2008). At all three intake times, the effect of dietary protein on muscle protein synthesis can be increased beyond the normal level by the intake of carbohydrates (Kerksick et al. 2008).

Beelen and his colleagues investigated the effect of protein intake during exercise and concluded that protein stimulates muscle protein synthesis even when the protein is consumed during physical exercise (Beelen et al. 2008).

The experts of the International Society of Sports Nutrition (ISSN) state that although it is certainly possible to cover the increased protein requirements of athletes through the daily diet, protein supplementation is an adequate and practical means of ensuring the intake of high-quality protein while maintaining low calorie intake (Jäger et al. 2017).

A study by Børsheim and colleagues concluded that non-essential amino acids do not contribute to an increase in muscle protein synthesis (Børsheim et al. 2002). The scientists compared the effect of 6 g of EAAs with that of a mixture of 3 g of EAAs and 3 g of non-essential amino acids and were able to show that the administration of pure EAA was actually twice as effective in stimulating muscle protein synthesis as the administration of mixed amino acids (Børsheim et al. 2002). This study confirms previous observations by Tipton and colleagues published in 1999 in the Journal of Nutritional Biochemistry (Tipton et al. 1999).

According to scientific studies, between three and four grams of L-leucine are needed to optimally stimulate muscle protein synthesis, with positive effects already being achieved at lower doses starting from 700 mg (Stark et al. 2012; Jäger et al. 2017).

In 2011, Pasiakos and colleagues published the results of a study in which they investigated the importance of the L-leucine content in an EAA drink (Pasiakos et al. 2011). The scientists found that a high content of L-leucine (3.5 g) is able to increase muscle protein synthesis in the recovery phase after physical activity more significantly (+33%) than a lower L-leucine content (1.87 g) (Pasiakos et al. 2011). The authors concluded that the intake of an EAA supplement with a high L-leucine content during exercise results in a greater increase in muscle protein synthesis in the subsequent recovery phase (Pasiakos et al. 2011).

Another study by Churchward-Venne et al. was able to confirm that added L-leucine can increase the effect of a low-protein supplement on muscle protein synthesis (Churchward-Venne et al. 2014). By adding L-leucine to about 6 g of protein, the muscle protein synthesis induced by it could be increased to the level of 25 g of complete whey protein (Churchward-Venne et al. 2014).

The working group of scientist M. Moberg found that the anabolic effect of the amino acid L-leucine is potentiated beyond the normal level by the addition of the remaining EAAs (Moberg et al. 2016). In the regularly published "Position Stand" of the International Society for Sports Nutrition, a high L-leucine content is also recommended to maximize the protein effect (Jäger et al. 2017). The authors recommend 700-3000 mg L-leucine or a relatively high L-leucine content, combined with the other eight essential amino acids (Jäger et al. 2017). With regard to the protein source, the expert panel states that rapidly digestible proteins with a high EAA content and an appropriate dosage of L-leucine are most effective if the aim is to maximize muscle protein synthesis (Jäger et al. 2017).

So far so good, but why does taking EAAs make sense in practice?

As mentioned before, a protein-rich diet supports muscle growth. Proteins are made up of amino acids - and the essential ones are particularly important because they are the crucial building blocks for building muscle proteins. EAAs are therefore well suited to promote muscle building!

Free EAAs have the advantage over complete proteins that they do not have to be broken down for absorption. This means that EAAs are quickly available and well tolerated, which is why they are ideal for taking around or during training.

An EAA drink feels less heavy in the stomach than, for example, a milk-based protein shake, which makes the free amino acids the ideal pre- or intra-workout drink.

Many athletes prefer the refreshing, fruity taste during training over the milky, creamy taste of protein shakes.

Convinced? Then enjoy our delicious premium EAAs during your workout and give your muscles the building blocks they need to regenerate and grow!