Beta Alanine is a non-essential amino acid. It is naturally occurring and not found in proteins. It is used for the synthesis of the vitamin panthothenic acid, and has some potential ergogenic (enhance physical performance, stamina, or recovery from exercise) effects.
Alanine Needs and Exercise
When you exercise, alanine is released into circulation by your skeletal muscle in direct proportion to the intensity of the exercise.1 This provides much needed energy but this catabolism (breakdown) of BCAAs and cellular protein is detrimental. Losing amino acids is counterproductive because they are used to increase or maintain skeletal muscle mass. Studies have shown that taking alanine before and during lengthy exercise conserved carbohydrates and increased protein metabolism.2 Alanine also leads to a positive nitrogen balance during workouts.
Protein synthesis can be increased when large amounts of a single amino acid is consumed, despite the amino acid being considered non-essential. Alanine is taken up by muscle and is used as fuel directly without going to the liver first to be converted to glucose. Additionally, alanine reduces ketogenesis 3, 4 (the production of ketone bodies as a result of fatty acid breakdown) because it reduces the need to have ketones as fuel.
Alanine is present in high levels in many foods including beef, lamb, milk products, corn meal, peas, and potatoes. However, many foods including chicken, fish, eggs, and bacon have low levels of alanine. Remember that chicken, fish and eggs are the staple of many bodybuilding diets. Bodybuilders are usually on restrictive diets which include only large amounts of these three foods for many months and many will this type of diet throughout the entire year. Even non-competing bodybuilders can find it hard to get enough dietary alanine. Low fat diets are recommended to decrease saturated fat intake so it is important to decrease the consumption of beef, lamb, and milk products. As a result, overall alanine intake may be low. Calorie restricted diets are usually alanine deficient so a high quality protein and/or alanine supplementation is necessary.
If there is a deficiency of or need for any amino acid, your body will break down body proteins to supply the amino acid for protein synthesis of needed proteins and enzymes or for gluconeogenesis (the generation of glucose from amino acids). Thus, supplementing with alanine before and after exercise will reduce the breakdown of proteins into smaller amino acids and increase the availability of amino acids for protein synthesis.
It’s been shown that alanine can affect insulin and glucogen and raises plasma glucose concentrations in diabetics 5, and can produce glucose recovery from hypoglycemia.6 Alanine decreases the breakdown of proteins into smaller amino acids 7 and is a potent stimulus for protein synthesis, energy levels 8 or an increase in cellular hydration. Alanine also helps increase cell volume.9
Supplementing with alanine decreases the need for the catabolism (breakdown) of muscle, and creates protein synthesis, as well as providing extra energy for anaerobic muscle contraction by allowing BCAAs to be oxidized and by providing an increase in glucose availability within the cells.
A diet low in alanine should be supplemented with protein foods that are rich in alanine or supplements, such as Beta Alanine. Supplements consisting of amino acids are necessary for protein synthesis and the maintenance of lean body mass. Because of its anabolic and anticatabolic effects, alanine supplementation in beneficial for all athletes wishing to maximize lean body mass and performance, regardless of their intake of dietary alanine.
Beta Alanine is known to have liver protection effects. In one study, supplementing with Beta Alanine can result in elevated cysteine levels,10 which are used for the production of taurine and GSH (Glutathione – an important antioxidant), both known to have an important role in the maintenance of normal liver function. The enhanced availability of cysteine accounts for the liver protective effects of Beta Alanine against toxin-induced liver injury.
Beta Alanine was also shown to provide cardio protection from reperfusion injury 11, to decrease the toxic effects of Beta Amyloid, 12 and to reduce the bacterial liver toxicity 13, suggesting that this supplement might reduce oxidative damage.
Several studies have found that Beta Alanine supplementation increases muscle carnosine levels, and with or without creatine, resulted in improvements in exercise performance. 14-19
Supplementing with Beta Alanine can lower taurine levels in the body because it inhibits taurine uptake.20 As a result, it’s wise to add taurine with beta alanine to make an effective nutritional supplement formulation.
1. Amino acid metabolism in exercising man.
Felig, P. and Wahren, J., J. Clin Invest., 1971 Dec;50(12):2703-14.
2. Differential metabolic fate of the carbon skeleton and amino-N of [13C]alanine and [15N]alanine ingested during prolonged exercise.
Korach-André M, Burelle Y, Péronnet F, Massicotte D, Lavoie C, Hillaire-Marcel C., J Appl Physiol (1985). 2002 Aug;93(2):499-504.
3. Post-exercise ketosis in post-prandial exercise: effect of glucose and alanine ingestion in humans.
Koeslag JH, Levinrad LI, Lochner JD, Sive AA., J Physiol. 1985 Jan;358:395-403.
4. The effects of alanine, glucose and starch ingestion on the ketosis produced by exercise and by starvation.
Koeslag JH, Noakes TD, Sloan AW., J Physiol. 1982 Apr;325:363-76.
5. Glycemic actions of alanine and terbutaline in IDDM.
Wiethop BV, Cryer PE., Diabetes Care. 1993 Aug;16(8):1124-30.
6. Alanine and terbutaline in treatment of hypoglycemia in IDDM.
Wiethop BV, Cryer PE., Diabetes Care. 1993 Aug;16(8):1131-6.
7. Multiphasic control of proteolysis by leucine and alanine in the isolated rat hepatocyte.
Venerando R, Miotto G, Kadowaki M, Siliprandi N, Mortimore GE., Am J Physiol. 1994 Feb;266(2 Pt 1):C455-61.
8. Effects of aminooxyacetate, alanine and other amino acids on protein synthesis in isolated rat hepatocytes.
Seglen PO, Solheim AE., Biochim Biophys Acta. 1978 Oct 24;520(3):630-41.
9. Role of amino acid-induced changes in ion fluxes in the regulation of hepatic protein synthesis.
Rivas T, Urcelay E, González-Manchón C, Parrilla R, Ayuso MS., J Cell Physiol. 1995 May;163(2):277-84.
10. Effect of beta-alanine administration on carbon tetrachloride-induced acute hepatotoxicity.
Lee SY, Kim YC., Amino Acids. 2007 Sep;33(3):543-6. Epub 2006 Nov 9.
11. Taurine depletion, a novel mechanism for cardioprotection from regional ischemia.
Allo SN, Bagby L, Schaffer SW., Am J Physiol. 1997 Oct;273(4 Pt 2):H1956-61.
12. Toxic effects of beta-amyloid(25-35) on immortalised rat brain endothelial cell: protection by carnosine, homocarnosine and beta-alanine.
Preston JE, Hipkiss AR, Himsworth DT, Romero IA, Abbott JN., Neurosci Lett. 1998 Feb 13;242(2):105-8.
13. Attenuation of bacterial lipopolysaccharide-induced hepatotoxicity by betaine or taurine in rats.
Kim SK, Kim YC., Food Chem Toxicol. 2002 Apr;40(4):545-9.
14-19. The absorption of orally supplied beta-alanine and its effect on muscle carnosine synthesis in human vastus lateralis.
Harris RC, Tallon MJ, Dunnett M, Boobis L, Coakley J, Kim HJ, Fallowfield JL, Hill CA, Sale C, Wise JA., Amino Acids. 2006 May;30(3):279-89. Epub 2006 Mar 24.
20. Characteristics of taurine transport system and its developmental pattern in mouse cerebral cortical neurons in primary culture.
Kishi M, Ohkuma S, Kimori M, Kuriyama K., Biochim Biophys Acta. 1988 Apr 22;939(3):615-23.