Highest Quality Protein to Rebuild the Body:
Healthy lean body tissue depends upon an adequate supply of high quality protein. The protein acts to repair damaged muscle tissue and provide growth factors that improve muscle fiber growth and rejuvenation (1). Although the quantity of protein consumed is important it is much more important to consider the quality of protein.
High quality protein is completely whole and non-denatured. It contains essential vitamins, minerals, enzymes and other natural co-factors. These components are very important for overall amino acid utilization and energy production. Protein by nature digests to form an acidic ash. These co-factors help provide alkaline substances that maintain normal acid/base balance.
Processing Damages the Protein:
There is a tremendous amount of processing that takes place to produce a protein isolate. It is completely unnatural. This processing strips out the natural proteolytic enzymes, minerals & anti-oxidants. This reduces overall bioavailability and creates a highly acidic and inflammatory food product.
The branched chain amino acids (BCAA’s) leucine, isoleucine and valine are especially important for building muscle. Many research trials have shown that BCAA’s improve red blood cell count, hemoglobin, hematocrit, serum albumin, fasting glucose levels, increased glycogenesis and rapid improvement in muscular inflammation (2, 3, 4) . These attributes make optimizing BCAA content extremely important for overall health and performance.
Branched Chain Amino Acids:
The BCAA leucine is the only amino acid that helps to stimulate muscle cell DNA to increase muscle protein synthesis. Muscle cells contain an inhibitory enzyme named 4E-binding protein 1 (4E-BP1). Leucine stimulates the cellular phosphorylation of 4E-BP1, effectively removing it. The removal of 4E-BP1 allows for greater activation of factors involved with muscle protein synthesis (5, 6, 7) .
The best food sources for BCAA’s such as leucine are found in high quality dairy products. Raw cheese, raw milk and non-denatured whey protein are the most bioavailable forms of these critical nutrients. These BCAA’s should always be consumed as whole foods and not as synthetically derived supplements which are of inferior quality.
The Daily Leucine Consumption:
The daily leucine consumption should be 1-3 grams per day to maintain body protein. To optimize the anabolic pathways one would need between 8-16 grams daily. Optimizing anabolic pathways enhances muscle repair, growth, & rejuvenation. This is desirable for a healthy physique, anti-aging and maximal performance (8).
Non-denatured whey protein concentrate from grass-fed cows is one of the elite superfoods for human consumption. It provides the best profile of essential amino acids and conditionally essential amino acids. It is by far the most bioavailable form of leucine (9).
Fast Assimilating Proteins During the Day:
Fast assimilating proteins such as raw, grass-fed whey protein work best to have during daytime hours. This is very easy on the digestive system and move into muscle tissue and initiate the repair process immediately.
High quality whey protein mixed with organic coconut milk is strikingly similar to mothers milk. The coconut milk provides an incredible array of medium chain triglycerides. The whey protein provides the complete protein as well as bioactive immunosupportive compounds. These include lactoferrin, alpha-lactoglobulins, immunoglobulins, bovine serum albumin, & conjugated linoleic acid (CLA).
These sources should ideally be replenished with another 20 grams of protein every 3-4 hours to maximize muscle recovery. During the daytime hours this should be in a low calorie form to reduce digestive stress and maintain high cognitive and kinetic energy.
Slow Release Proteins at Night:
Slow release proteins are better to have at night as they digest over time and move into muscle tissue and form enzymes in the body slowly. This maintains optimal protein synthesis and positive nitrogen balance during sleep while the body is in a fasting state.
Slow release proteins are found in healthy meat sources such as grass-fed beef, bison, buffalo & deer. Raw, grass-fed cheese is an amazing slow release protein. Free range turkey, chicken, & eggs as well as wild-caught fish are good. When cooking these proteins be sure to add phytonutrient rich vegetables, fresh lemon & apple cider vinegar to balance the acids and free radicals formed during the cooking process. They also provide proteolytic enzymes and microorganisms to enhance the protein assimilation process.
Non-Dairy Protein Powders:
Many people have food sensitivities to all dairy including grass-fed whey. With these individuals, I recommend either a collagen protein or a pea protein base with added nutrients to reduce gut inflammation. I formulated a specific protein powder that is especially good for individuals with leaky gut or autoimmunity.
This product is called gut healing protein that contains a powerful array of anti-oxidant compounds that reduce inflammation, it is completely sugar-free and has 5 grams of L-glutamine in it to support healing leaky gut. Check it out here
Sources For This Article Include:
- Rieu I, Balage M, Sornet C, Debras E, Ripes S, Rochon-Bonhomme C, Pouyet C, Grizard J, Dardevet D. Increased availability of leucine with leucine-rich whey proteins improves postprandial muscle protein synthesis in aging rats. Nutrition. 2007 Apr;23(4):323-31. PMID: 17367997
- Ohtani M, Sugita M, Maruyama K. Amino Acid Mixture Improves Training Efficiency in Athletes Link Here
- Takeshita S, Ichikawa T, Nakao K, Miyaaki H, Shibata H, Matsuzaki T, Muraoka T, Honda T, Otani M, Akiyama M, Miuma S, Ozawa E, Fujimito M, Eguchi K. A snack enriched with oral branched-chain amino acids prevents a fall in albumin in patients with liver cirrhosis undergoing chemoembolization for hepatocellular carcinoma. Nutr Res. 2009 Feb;29(2):89-93. PMID: 19285598
- Matsumoto K, Koba T, Hamada K, Sakurai M, Higuchi T, Miyata H. Branched-chain amino acid supplementation attenuates muscle soreness, muscle damage and inflammation during an intensive training program. J Sports Med Phys Fitness. 2009 Dec;49(4):424-31. PMID: 20087302
- Yoshizawa F, Hirayama S, Sekizawa H, Nagasawa T, Sugahara K. Oral administration of leucine stimulates phosphorylation of 4E-bP1 and S6K 1 in skeletal muscle but not in liver of diabetic rats. J Nutr Sci Vitaminol (Tokyo). 2002 Feb;48(1):59-64. PMID: 12026190
- Anthony JC, Reiter AK, Anthony TG, Crozier SJ, Lang CH, MacLean DA, Kimball SR, Jefferson LS. Orally administered leucine enhances protein synthesis in skeletal muscle of diabetic rats in the absence of increases in 4E-BP1 or S6K1 phosphorylation. Diabetes. 2002 Apr;51(4):928-36. PMID: 11916909
- Anthony JC, Anthony TG, Kimball SR, Jefferson LS. Signaling pathways involved in translational control of protein synthesis in skeletal muscle by leucine. J Nutr. 2001 Mar;131(3):856S-860S. PMID: 11238774
- Mero A. Leucine supplementation and intensive training. Sports Med. 1999 Jun;27(6):347-58. PMID: 10418071
- Bukhari SS, Phillips BE Atherton, Wilkinson DJ, Limb MC, Rankin D, Mitchell WK, Koboyashi H, Greenhaff PL, Smith K, Atherton PJ. Intake of low-dose leucine-rich essential amino acids stimulates muscle anabolism equivalently to bolus whey protein in older women, at rest and after exercise. Am J Physiol Endocrinol Metab. 2015 Mar 31:ajpendo.00481.2014. PMID: 25827594