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Ajinopure® Instantized Branch Chain Amino Acids (2:1:1)
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Promotes fat loss & lean muscle growth
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Increases the post exercise Testosterone : Cortisol ratio
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The same ratio of BCAA’s found in human muscle
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Unmatched purity, taste, mixability and bio-availability
What is IBCAA?
IBCAA’s are Instantized
Branched Chain Amino Acids in a 2:1:1 ratio of L-leucine, L-isoleucine
and L-valine. Unlike regular BCAA’s found at other bulk supplement
stores, our Ajinopure IBCAA’s have been manufactured by Ajinomoto and
are recognized as the purest, best tasting, and most water soluble
BCAA’s available in the world.
Being that BCAA’s are essential amino
acids, they must be supplied by dietary or supplemental sources, since
the body cannot synthesize them. IBCAA’s are the perfect supplement to
any beverage or protein shake. At the average recommended dose of 2
servings per day, a bottle of IBCAA will last 20 days.
Why would I want to use BCAA’s?
Next week, when I begin my low carbohydrate diet for fat loss, I’ll be using 3-4 servings of BCAA’s every day.
Why you ask?
Because BCAA’s help burn off body fat and preserve muscle very efficiently –especially if you are on a ketogenic or low calorie diet (also referred to as therapeutic starvation).
Essentially, starvation is when the body must feed upon itself – so it is up to you to direct the body to feed upon the fat, rather than the muscle if
you want to sculpt out a chiseled physique. BCAA’s are quite possibly
the most important tool for making this happen. The science is a little
complex, but here is the basic idea –
1. The state of
starvation can be created by either burning more calories than you
consume, or consuming less calories than you burn. Either way, it’s
called a calorie deficit, and you must be in a calorie deficit in order to burn off fat.
2.
During a normal calorie deficit, blood glucose is used up as an energy
source. When blood glucose gets too low, cortisol is released which
causes the breakdown and conversion of muscle to glucose (This is bad
for fat loss). (1)
3. BCAA supplementation helps prevent muscle breakdown by sparing glucose as an energy source and instead encouraging the release of ketones, which can be used as an alternative source of energy. (7)
4.
Ketones are a byproduct of fat metabolism. When ketones are present,
this means fat is being used as an energy source. Ketones also have the
ability to prevent protein breakdown and catabolism of muscle tissue.
(This is good for fat loss) (8-10)
The anti-catabolic fat loss effects of
BCAA’s were clearly demonstrated in a 21-day study with a group of
hikers trekking through the Peruvian Andes. (4) One group received
15gm/day of BCAA’s, while the other group received a placebo. At the
end of the 21 days, the BCAA group actually gained lean muscle and lost more bodyfat than the placebo group which had a significant reduction in muscle mass and strength.
The researchers noted -
“From the differences in lean body
mass one may conclude that on the whole the placebo group was
catabolizing, whereas the BCAA group was synthesizing muscle tissue.”
Which group would you rather be in?
So there it is folks, the secret to fat
loss. Encourage your body to use fat (ketones) for fuel, save the
muscle from breakdown, and get ripped. Just know that if you want to
get truly ripped, your calories (and preferably your carbohydrates)
need to be low enough.
Will IBCAA help if I’m not dieting?
If you already consume 400-500 grams of
animal based protein everyday you probably won’t notice additional
benefits from BCAA supplementation since you probably get plenty of
BCAA’s from your dietary protein – however, most normal humans have a
hard time consuming this much protein each day – and this is where
BCAA’s come in to fill the gap.
Can’t find time to grill up some protein? Or don’t want consume a sugar loaded protein bar?
This would be a perfect time to slam down a quick mix of IBCAA’s.
In fact researchers found that
supplementing with ~15gm/day of BCAA’s increased protein retention just
as much as a 200lb individual increasing total protein from 54gm to
90gms/day. (2-3) By increasing protein retention, BCAA’s can help
retain and increase theavailability of circulating amino acids and
promote muscle growth through stimulation of protein synthesis.
(12-20) The L-Leucine in IBCAA is especially important for this purpose
as it’s been shown to have a direct effect on protein synthesis through
mTOR signaling and AMPK activation. (21-24)
An additional benefit of BCAA’s was
demonstrated in a study with a group of runners. (25) The first group
received a milk protein mixture with 10 grams of BCAA’s. The second
group received a milk protein mixture without BCAA’s. Both groups
consumed the beverage 90 minutes before the run test. In the BCAA
group, testosterone stayed the same during the exercise, and increased
during the recovery period, while testosterone declined in the non-BCAA
group. This shows an additive effect of BCAA’s when consumed with
dietary protein.
Other research has shown that BCAA’s can
enhance the anabolic (muscle building) effect of insulin. (11) The
effect was summarized here by Maria et al –
“We can speculate that the amino
acid-mediated [BCAA] enhancement of sensitivity and responsiveness of
the tissues to the actions of insulin on suppressing proteolysis may be
partly related to increased binding of insulin to its receptors, as
well as to associated improvements in postreceptor function”
In laymen’s terms, BCAA’s could be
considered a “growth optimizer” that help drive the amino acids into
muscle tissue, encourage connection of individual amino acids into
proteins than constitute the structural muscle – aka protein synthesis – and support further anabolic effect by supporting post exercise testosterone levels.
In summary, BCAA’s can offer the following benefits for muscle growth –
Promoting a positive protein balance
Increased muscle protein synthesis
Increase the post exercise testosterone : cortisol ratio
Increased insulin sensitivity
Are BCAA’s safe?
When used at the maximum recommended 20
gm daily dose, BCAA’s have been proven to be safe for long-term
supplementation. (26-27)
References
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Pedro Del Corral, et al.
J Appl Physiol, Mar 1998; 84: 939 - 947.
2. Branched-chain amino acid supplementation during bed rest: effect on recovery
T. P. Stein, et al.
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3. Effect of dietary protein on bed-rest-related changes in whole-body-protein synthesis
CA Stuart, et al.
Am. J. Clinical Nutrition, Sep 1990; 52: 509 - 514.
4. Branched-chain amino acid
supplementation during trekking at high altitude. The effects on loss
of body mass, body composition, and muscle power.
F Schena, et al.
Eur J Appl Physiol Occup Physiol, Jan 1992; 65(5): 394-8.
5. Acute response of net muscle protein balance reflects 24-h balance after exercise and amino acid ingestion
Kevin D. Tipton, et al.
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Elisabet Břrsheim, Kevin D. Tipton, Steven E. Wolf, and Robert R. Wolfe
Am J Physiol Endocrinol Metab, Oct 2002; 283: E648 - E657
7. Partial oxidation of leucine in skeletal muscle.
TN Palmer, S Gossain, and MC Sugden
Biochem Mol Biol Int, Feb 1993; 29(2): 255-62.
8. Effect of ketone infusions on amino acid and nitrogen metabolism in man.
RS Sherwin, RG Hendler, and P Felig
J Clin Invest, June 1, 1975; 55(6): 1382-90.
9. 3-Hydroxybutyrate to conserve protein during therapeutic starvation.
Lancet, Feb 1983; 1(8321): 409.
10. The effect of ketone bodies on nitrogen metabolism in skeletal muscle.
JR Thompson and G Wu
Comp Biochem Physiol B, January 1, 1991; 100(2): 209-16.
11. Role of insulin and branched-chain amino acids in regulating protein metabolism during fasting.
Frexes-Steed M, et al.
Am J Physiol. 1990 Jun;258(6 Pt 1):E907-17.
12. Increase in anterior tibialis
muscle protein synthesis in healthy man during mixed amino acid
infusion: studies of incorporation of [1-13C]leucine.
13. The effect of amino acid infusion on leg protein turnover assessed by L-[15N]phenylalanine and L-[1-13C]leucine exchange.
WM Bennet, et al.
Eur J Clin Invest, Feb 1990; 20(1): 41-50.
14. Euglycemic hyperinsulinemia augments amino acid uptake by human leg tissues during hyperaminoacidemia
W. M. Bennet, et al.
Am J Physiol Endocrinol Metab, Aug 1990; 259: E185 - E194
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Scot R. Kimball et al.
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ME May and MG Buse
Diabetes Metab Rev, May 1989; 5(3): 227-45.
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Padden-Jones D, et al.
Am J Physiol Endocrinol Metab. 2004 Mar;286(3):E321-8.
18. Effects of prolonged administration of branched-chain amino acids on body composition and physical fitness
N Candeloro, et al.
Minerva Endocrinol, Dec 1995; 20(4): 217-23
19. Postexercise net protein synthesis in human muscle from orally administered amino acids
Kevin D. et al
Am J Physiol Endocrinol Metab, Apr 1999; 276: E628 - E634.
20. Contractile and nutritional regulation of human muscle growth.
Rasmussen BB, et al.
Exerc Sport Sci Rev. 2003 Jul;31(3):127-31.
21. Leucine supplementation improves muscle protein synthesis in elderly men independently of hyperaminoacidaemia.
Rieu, Isabelle. et al
J. Physiol. 2006;575;305-15.
22. Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise.
Norton LE and Layman DK.
J Nutr. 2006; 136(2):533S-537S.
23. Leucine and protein synthesis: mTOR and beyond. Nutrition Reviews.
Stipanuk, et al.
2007;Mar;Vol. 65, No. 3:122-9.
24. Orally administered leucine
stimulates protein synthesis in skeletal muscle of postabsorptive rats
in association with increased eIF4F formation.
Anthony, et al.
J Nutr 130: 139-145, 2000.
25. Changes in the exercise-induced hormone response to branched chain amino acid administration.
G Carli, et al.
Eur J Appl Physiol Occup Physiol, Jan 1992; 64(3): 272-7.
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Michael Gleeson et al
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27. An approach to defining the upper safe limits of amino acid intake.
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