BCAA Structured Peptides

250% Greater Muscle Growth!

Structured Peptides are absorbed faster, utilized better, and produce 250 percent greater muscle growth than free-form amino acids.

BIOTEST® Leucine and BCAA Structured Peptides are produced from peptide enhanced whey-protein isolate, utilizing a three-step process:

1. Whey-protein isolate is hydrolyzed into very small peptide forms using a combination of selective enzymes (aminopeptidases and proteases) to break apart targeted leucine peptide and BCAA-peptide bonds.
2. Afterward, small peptide formations are extracted from the hydrolyzed whey by passing the mixture through a series of filters, ending with nanofiltration.
3. Next, the nano-mixture undergoes a final reaction phase to further enhance its total leucine and BCAA content.

The end result is a highly refined mixture of leucine and BCAA di- and tripeptides that provides the body with the greatest effects from leucine/ BCAA supplementation.

Di- and Tripeptide Science

• Unlike regular (free-form) amino acids, the uptake of di- and tripeptides is achieved through a very specific, high-capacity intestinal transporter (PEPT-1), which can lead to a larger and more rapid spike in blood levels of these crucial anabolic signals.

BCAA Science

• The branched-chain amino acids (BCAA) consist of the essential amino acids leucine, isoleucine, and valine.
• BCAA account for approximately 35% of the essential amino acids in muscle.
• In contrast to most essential amino acids that are metabolized in the liver, BCAA are unique because they are metabolized primarily in skeletal muscle. This fact also explains why BCAA are used to help patients with liver failure retain their lean mass. BCAA are also used in the management of tardive dyskinesia, amytrophic lateral sclerosis (ALS), hepatic encephalopathy, and phenylketonuria.
• Numerous studies have demonstrated the anti-catabolic effects of (free form) BCAA administration, i.e., a reduction in muscle protein breakdown during clinical conditions of wasting (e.g., starvation, post-surgery, burns, liver disease, etc.).
• BCAA have been theorized to act as a metabolic fuel during exercise, particularly during intense and/or prolonged physical activity. This effect "spares" muscle glycogen during training, at least when BCAA are taken pre-exercise.
• BCAA also donate nitrogen (via transamination) to non-essential amino acids. This phenomenon explains why not all amino acids are necessary to stimulate protein synthesis.
• Proponents of BCAA supplementation maintain that BCAA may blunt the increase in serotonin, thus reducing perceived effort and mental fatigue during prolonged exercise, and here's why:

BCAA contribute to the synthesis of neurotransmitters. As such, supplementing with BCAA during prolonged exercise could, in theory, increase the mental effort necessary to maintain (or extend) higher performance levels. This conclusion is based on the well-known "Central Fatigue Hypothesis," which suggests that prolonged exercise decreases BCAA and increases fatty acids in circulating blood, resulting in elevated tryptophan levels. And tryptophan is the amino-acid precursor to serotonin, a neurotransmitter that causes feelings of sleepiness and (in excess) depression.

• A few recent studies have shown that men and women who ingest approximately 10 to 15 grams of BCAA per day (comprised of 5-7 g leucine, 3-4 g isoleucine, and 3-4 g valine) for at least four-weeks increase their lean mass more than matched control subjects. This effect appears to be the result of a BCAA-induced increased protein synthesis during the recovery period following resistance exercise.
• Another interesting aspect of BCAA that has only recently been explored is the potential effect on weight loss. During moderate protein intake (1.5 grams/kg of body weight per day) and a lower carbohydrate (100-200 grams/day) diet, an increased intake of BCAA is thought to have positive effects on muscle protein synthesis, insulin signaling, and sparing of glucose use by stimulation of the glucose-alanine cycle. This may lead to more fat loss and a greater sparing of lean tissue compared to a calorically-matched, higher carbohydrate diet.

BCAA References

Blomstrand E, Ek S, Newsholme EA.

Influence of ingesting a solution of branched chain amino acids on plasma and muscle concentrations of amino acids during prolonged submaximal exercise. Nutrition 1996;12:485-490.

Blomstrand E, Hassmen P, Ek S, et al.

Influence of ingesting a solution of branched chain amino acids on perceived exertion during exercise. Acta Physiol Scand. 1997;159:41-49.

Blomstrand E, Hassmen P., et al.

Administration of branched chain amino acids during sustained exercise-effects on performance and plasma concentration of some amino acids. Eur J Appl Physiol 1991;63:83-88.

Blomstrand E, Saltin B.

BCAA intake affects protein metabolism in muscle after but not during exercise in humans. Am J Physiol Endocrinol Metab. 2001 Aug;281(2):E365-74.

Candeloro N, Bertini I, Melchiorro G, DeLorenzo A.

Effects of prolonged administration of branched chain amino acids on body composition and physical fitness. Minerva Endocrinol 1995;20(4):217-223.

Layman DK, Baum JI.

Dietary protein impact on glycemic control during weight loss. J Nutr. 2004 Apr;134(4):968S-73S.

Madsen K, Maclean DA. Et al.

Effects of glucose, glucose plus branched chain amino acids, or placebo on bike performance over 100 km. J Appl Physiol. 1996;81:2644-2650.

Mourier A, Bigard AX, deKerviler E, et al.

Combined effects of caloric restriction and branched chain amino acid supplementation on body composition and selected performance parameters in elite wrestlers. Int J Sports Med. 1997;18:47-55.

Shimomura Y, Murakami T, Nakai N, Nagasaki M, Harris RA.

Exercise promotes BCAA catabolism: effects of BCAA supplementation on skeletal muscle during exercise. J Nutr. 2004 Jun;134(6 Suppl):1583S-1587S.