Whey Protein Stimulates Muscle Buildup More Effectively Than other Milk Proteins

 A recent study by Dutch scientists at the Maastricht University Medical Center, Maastricht, Netherlands, showed that whey protein stimulates muscle protein synthesis towards muscle gain more effectively than casein.

Recent data suggests that muscle protein synthesis depends on the quantity and the type of protein ingested. Previous reports indicated that whey protein ingestion results in greater postprandal (post-meal) protein retention than does casein ingestion. Casein is a "slow protein" that allows a long lasting release of amino acids to the muscle. In comparison, whey is a "fast protein" that releases amino acids to the muscle instantly and rapidly. The greater anabolic properties of whey are mainly attributed to its faster digestion and absorption kinetics. Whey yields a greater increase in circulating amino acid availability and thereby further stimulates muscle protein synthesis.

Higher Content of Leucine
Besides differences in protein absorption rates, whey protein and casein also markedly differ in their amino acid composition.

Whereas both proteins contain all amino acids required to stimulate muscle mass gain, whey protein has a considerably higher leucine content which further contributes to the greater anabolic properties of whey protein than of casein. The amino acid leucine has been identified as the main nutritional trigger of mTOR, the mechanism that stimulates muscle protein accretion.

Given all this, scientists were trying to figure out whether the greater anabolic properties of whey than of casein are attributed to faster absorption or simply to differences in amino acid composition. So they tested the anabolic effects of whey protein compared to hydrolyzed casein which has a fast absorption rate similar to whey.

Whey Protein vs. Hydrolyzed Casein

When intact casein is hydrolyzed (pre-digested), its protein matrix breaks down into smaller components – amino acids and peptides – forming a "fast protein" with substantially increased absorption rate, similar to that of whey protein. Yet, despite this, whey protein demonstrated a stronger anabolic impact, yielding greater protein synthesis in the muscle than hydrolyzed casein. 

The postprandal anabolic effect of whey on muscle protein deposit was correlated strongly with the rise in plasma leucine concentrations. The researchers observed a more rapid rise in plasma phenylalanine, leucine, and total essential amino acids after whey than after casein ingestion.

It has been concluded that whey protein is more effective than casein and casein hydrolysate at promoting postprandal muscle protein synthesis. These data are of great practical relevance to the use of effective nutritional strategies for supporting post-exercise muscle recovery, enhancing athletic performance, and particularly for preventing age-related muscle waste.

Areas to be Concerned With 

Beware of commercial casein powders  
Commercial casein is typically a protein isolate, extracted from ultra-pasteurized milk via extreme heat and acid treatment. The heat/acid processing is a cheap way to precipitate the casein from the milk and has been commonly used as a cost effective method in casein manufacturing. The commercial casein product is not the same as the original raw milk casein. The ultra heat processing of casein yields a degraded, less digestible product called thermolyzed casein which is constituted of broken proteins along with toxic compounds and unnatural amino acids that can markedly enhance metabolic toxicity and colon carcinogenesis.

Most bovine casein products are derived from A-1 milk 
A1 milk and related products from cattle belonging to the Bos Taurus subspecies which predominantly exist in the western hemisphere. The most popular cows in the U.S. are from Holstein and Fresian breeds which tend to produce mostly A1 milk. The casein product of A1 milk is A1 beta casein which is apparently associated with illness and disease. The digestion of A1 beta casein has been found to produce an opioid peptide byproduct (beta casomorphin) that can be very problematic for humans, especially for babies and infants. 

There's growing epidemiological evidence that link A1 beta casein and its opioid derivative with heart disease, autism, schizophrenia, type I diabetes and autoimmune disorders. This issue is still arguable and more studies need to be done to reach final conclusions. Nonetheless, it may be wise to avoid products containing A1 beta casein as a precautionary measure. Note that the A1 issue applies to milk and cheese products but does not apply to whey which is casein-free.
Raw milk cheese casein can benefit your muscle – 

Native non-denatured casein, as naturally occurring in raw milk cheese (from A2 cows, goats or sheep), is a viable source of protein, peptides and amino acids and can be highly effective in yielding long lasting anabolic impact. Casein forms a clot in the stomach which makes it very efficient in providing a sustained slow release of amino acids into the blood circulation, a process that can last for several hours. This provides better nitrogen retention and utilization by the body. Quality cheese, if eaten at dinner, can be effectively used to sustain muscle anabolism during the sleeping hours of the night.
Use only quality whey  

Your whey should be derived from raw milk of pasture fed cows, it should be supported by pasture-fed certification and an independent lab report proving that its fragile immuno peptides are intact. To avoid adverse side effects, make sure your whey protein is 100% chemical free, tested to be radiation safe, and made with no added sugar, no sugar alcohol and no fructose. Quality whey protein tastes naturally sweet and creamy and can be used for muscle nourishment during the day and particularly for muscle recovery after exercise. When using whey protein powders make sure they are whole food concentrates.

Avoid whey products that are insoluble or have a funky acid aftertaste – 
Insolubility and an acid aftertaste are signs of protein degradation. A funky whey most likely contains waste byproducts of protein breakdown (toxic nitrogen soup). Even if the whey is soluble, you still need to check what kind of emulsifier is used to make it water soluble. Many whey proteins are instantized with GMO soy lecithin, often with chemical surfactants that are used in soap manufacturing.

To get maximum anabolic impact from your whey protein, use pulse feeding – 
To yield most effective and long lasting anabolic impact, feed your muscle frequently with small servings of quality whey protein (20-30g) with no sugar added throughout the day every 2-3 hours, and have your slow protein – cheese, fish or chicken protein – with your main meal at night. This will grant fast effective supply of amino acids and immuno supportive nutrients to grant muscle anabolism during the active hours of the day; followed by a slow steady release of amino acids to your muscle for protein retention and buildup during the sleeping hours of the night.. 
References

  • Volpi, E., Kobayashi, H., Sheffield-Moore, M., Mittendorfer, B., Wolfe, B.B. Essential amino acids are primarily responsible for the amino acid stimulation of muscle protein anabolism in healthy elderly adults. Am J Clin Nutr. 2003;78:250-8.
  • Koopman, R., Walrand, S., Beelen, M., et al. Dietary protein digestion and absorption rates and the subsequent postprandal muscle protein synthetic response do not differ between young and elderly men. J Nutr. 2009;139:1707-13.
  • Symons, T.B., Schutzler, S.E., Cocke, T.L., Chinkes, D.L., Wolfe, R.R., Paddon-Jones, D. Aging does not impair the anabolic response to a protein-rich meal. Am J Clin Nutr. 2007;86:451-6.
  • Tang, J.E., Phillips, S.M. Maximizing muscle protein anabolism: the role of protein quality. Curr Opin Clin Nutr Metab Care. 2009;12:66-71.
  • Dangin, M., Boire, Y., Guillet, C., Beaufrere, C., et al. Influence of the protein digestion rate on protein turnover in young and elderly subjects. J Nutr. 2002;132:3228S–33S.
  • Dangin, M., Guillet, C., Garcia-Redenas, C., et al. The rate of protein digestion affects protein gain differently during aging in humans. J Physiol. 2003;549:635-44.
  • Boirie, Y., Dangin, M., Gachon, P, Vasson, M.P., Maubois, J.L., Beaufrere, B. Slow and fast dietary proteins differently modulate postprandal protein accretion. Proc Natl Acad Sci USA. 1997;94:14930-5.
  • Dangin, M., Boirie, Y., Garcia-Rodenas, C., et al. The digestion rate of protein is an independent regulating factor of postprandial protein retention. Am J Physiol Endocrinol Metab. 2001;280:E340-8.
  • Bohe, J., Low, A., Wolfe, R.R., Rennie, M.J. Human muscle protein synthesis is modulated by extracellular, not intramuscular amino acid availability: a dose-response study. J Physiol. 2003;552:315-24.
  • Koopman, R., Crombach, N., Gijsen, A.P., et al. Ingestion of a protein hydrolysate is accompanied by an accelerated in vivo digestion and absorption rate when compared with its intact protein. Am J Clin Nutr. 2009;90:106–15.
  • Buse, M.G., Reid, S.S. Leucine. A possible regulator of protein turnover in muscle. J Clin Invest.1975;56:1250-61.
  • Katsanos, C.S., Kobayashi, H., Sheffield-Moore, M., Aarsland, A., Wolfe, R.R. A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. Am J Physiol Endocrinol Metab. 2006;291:E381–7.
  • Rieu, I., Balage, M., Sornet, C., et al. Leucine supplementation improves muscle protein synthesis in elderly men independently of hyperaminoacidemia. J Physiol. 2006;575:305-15.
  • Leenders, M., van Loon, L.J.C. Leucine as a pharmaconutrient to prevent and/or treat sarcopenia and type 2 diabetes. Nutr Rev. (in press).
  • van Loon, L.J., Boirie, Y., Gijsen, A.P., et al. The production of intrinsically labeled milk protein provides a functional tool for human nutrition research. J Dairy Sci. 2009;92:4812-22.
  • Pennings, B., Boirie, Y., Senden, J.M.G., Gijsen, A.P., Kuipers, H., van Loon, L.J.C. Whey protein stimulates postprandal muscle protein accretion more effectively than do casein and casein hydrolysate in older men. Am J Clin Nutr. 2011;93:997-1005.

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