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Amino acids are the building blocks of proteins, and proteins are the building blocks of life. The human body is constantly assembling, breaking down and using proteins on a daily basis. In fact, 10 to 35% of caloric energy should come from good, high-quality protein.
Amino acids are vital for the body’s ability to function at an optimal level. Unlike fat and carbohydrates, the human body does not store excess amino acids for later use. Amino acids must be obtained from protein in the diet on a daily basis to meet the needs of the body. They are crucial and have wide-ranging roles, including the repair and maintenance of muscles, organs, nails, hair, skin, ligaments, connective tissues, glands, etc. Because amino acids are considered the building blocks of life, specifically protein, a deficiency in even one of them can have detrimental effects on one’s health and well-being.
There are twenty “standard” amino acids used by cells in protein biosynthesis. Of the 20+ amino acids, 9 are “essential” and are required in the diet, since the body cannot produce them. “Nonessential” amino acids, on the other hand, are produced in the body from other amino acids when given an adequate supply of nitrogen, carbon, hydrogen and oxygen. Yet, even some of these nonessential amino acids are necessary at certain life stages or during certain situations, which is why some are considered “conditionally essential”
In chemistry, an amino acid by definition is any molecule that contains both amine (amino) and carboxyl functional groups. All amino acids share this common chemical "backbone" that consists of a carbon atom to which four substituent groups are bonded: a nitrogen-containing amino group (NH2), a carboxyl group (COOH), a hydrogen (H+) atom and an "R" group.
The "R" group or side chain varies in electric charge, size, structure and solubility in water, giving each amino acid its distinct chemical properties. Since all amino acids (except glycine) contain at least one asymmetrical carbon atom, which produces a mirror image, they exist in nature as two forms (stereoisomers). The forms are designated as either D- or L-, depending on their structural relationship to a right- or left-handed reference point. While both forms are found in biological systems, all amino acids constituting proteins are composed of the L-form. DL-amino acids are a 50/50 mixture of both the D- and L- form of the molecule.
Everybody needs protein, but some need it more than others do. Particular lifestyles and at different life stages, human beings have special protein requirements. The growth and development of muscles, organs, and even the brain, all depend on the high-quality protein an infant receives from the diet. Additionally, since children grow so fast, and because healthy development in a child is critical to health in later life, meeting their daily protein requirements is crucial. Patients who have undergone trauma from surgery or an accident can benefit from protein supplementation. Consumption of high-quality (complete) protein is directly related to the rehabilitation and normal rate of repair of damaged muscle and tissue. While the amount of protein required does not increase over the age of 65, older adults need fewer calories, they tend to eat less than younger adults and sometimes they wear dentures, all of which can decrease adequate consumption of protein-rich foods. As a result, they often consume too little protein. High-quality protein is important for seniors because it is essential in the maintenance of muscle tissue, proper organ function and metabolism.
The concept of “fast” and “slow” acting proteins was first described in the literature by Boirie et al. in 1997. Whey, a protein derived from milk, is considered fast-acting because unlike casein, its impact on postprandial (i.e., after eating) protein metabolism is fast, high (i.e., a lot of amino acids are available immediately) and transient. The amino acids derived from whey are typically associated with protein synthesis and oxidation and not in the inhibition of protein breakdown—so it’s great for muscle building, but not so much for muscle repair. These metabolic characteristics of whey are due in part because whey is not coagulated by the gastric juices of the gut, allowing its amino acids to be assimilated into the body easily. A rapid release of amino acids in the blood from the digestion of whey allows the amino acids to be used effortlessly for muscle enhancement. This is partly because whey’s amino acid profile is very similar to that of human muscle, making it the protein of choice for bodybuilders and athletes. Whey protein isolate is the more preferred form of whey over whey protein concentrate because of the high elemental amount of protein per serving—isolates provide 90% protein per gram of product—ensuring a high concentration of protein in a small dose.
Casein is the dominant protein found in milk, and unlike whey, it coagulates in the stomach—the protein then curdles, causing a delay in gastric emptying (i.e., the process of stomach contents passing into the small intestines for further digestion). This means that the release of amino acids into the blood will be slower, lower (i.e., not as many amino acids are available) and prolonged compared to how whey is metabolized. Therefore, with casein supplementation, although protein synthesis is slightly increased and oxidation is moderately stimulated, protein breakdown is markedly inhibited compared to whey. Casein’s slower absorption profile seems to better promote a positive protein balance in the body, which is an essential requirement for reconstructing broken down muscles. Therefore, casein is the preferred protein for prolonged hours of muscle rebuilding and repair and makes for a perfect partner to whey protein.
As previously mentioned, the digestion, absorption and metabolic response of whey and casein differ in the body. Whey protein primarily stimulates protein synthesis for muscle enhancement, whereas casein inhibits protein breakdown, allowing run-down muscles to rebuild and repair. The speed of absorption of dietary amino acids by the gut varies according to the type of dietary protein ingested. Whey protein produces a dramatic, but short increase of plasma amino acids; whereas, casein produces a delayed plateau of moderate amino acid availability due to its slow gastric emptying. Therefore, a combination of both proteins may be most appropriate for the athletically inclined or active individual since whey will provide immediate amino acid replenishment, while the addition of casein will help prolong the extent to which amino acids are available in the body for continual muscle support.
Everybody needs protein. Particular lifestyles and individuals at different life stages have special protein requirements. But, no one requires protein more than active individuals, athletes and weekend warriors who need strength, power and endurance. Since these individuals are constantly assembling, breaking down and using proteins on a daily basis, up to 35% (or 0.8 to 1.5 g/kg) of their caloric intake should come from high-quality, complete protein. Although variances and daily amounts of protein are dependent on weight and physical activity level, an ideal source of complete protein for those leading an active lifestyle is a formula that provides both fast-acting undenatured whey protein isolate and extended-acting undenatured micellar casein, like Bluebonnet’s 100% Natural Dual-Action Protein Powder.
Bluebonnet’s 100% Natural Whey Protein Isolate Powder is derived from free-roaming, grass-fed cows and is one of the purest undenatured whey protein products on the market providing 26 g of protein with no artificial flavors or sweeteners and is not treated with rBGH (recombinant bovine growth hormone) or antibiotics.
Whey protein has the high biological value (BV) of any protein on the market. Biological value refers to a protein that has all of the essential amino acids in adequate quantities to sustain growth and development. Additionally, whey protein is fast-acting, which means that its naturally occurring immunoglobulins and essential amino acids, such as BCAA and glutamic acid, are easily and readily available to the body for immediate use – an especially important consideration after exercising to optimize the recovery phase by supporting the immune system and quickly replenishing the body’s amino acid pool.
Unlike the common practice of using a heat-processed whey protein isolate that can denature (render useless) the protein and immunoglobulins, Bluebonnet employs a special low temperature method, which leaves the protein undenatured and immunoglobulins, which support the immune system, intact.
Plus, Bluebonnet’s 100% Natural Whey Protein Isolate Powder is microfiltered, removing 99% of the lactose. Most persons who are lactose intolerant are not deficient of lactase, the enzyme required to breakdown lactose, they just have a lower enzyme activity level. Therefore, persons who cannot normally tolerate milk products have little to no GI disturbance when supplementing with Bluebonnet’s 100% Natural Whey Protein Isolate Powder.
Moreover, Bluebonnet’s 100% Natural Whey Protein Isolate Powder is microfiltered, free of rBGH, antibiotics, added sugar and artificial flavors/sweeteners and is low in carbohydrate, cholesterol and sodium.