Your Protein Requirements – COVERED | The Locker Room Your Protein Requirements – COVERED – The Locker Room
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Your Protein Requirements – COVERED


 

Earlier this week we brought some clarity to protein requirements when it comes to improving muscle mass and body composition. Now its time to explore the sources from which you can obtain this protein, in particular those most advantageous when choosing a supplement to support your nutrition from whole foods. Because unfortunately against what some would like you to believe all protein is not equal and their may be times when eating whole food is not convenient or possible.

Protein Quality

The quality of a protein is determined by its essential amino acid composition, the digestibility and bioavailability of its amino acids (FAO and WHO 2017). Several measures have been developed over the past 40years to allow for credible standards for the use in determining quality (IDG 2017); 1) Biological Value (BV), 2) Net Protein Utilization (NPU), 3) Protein Digestibility Corrected Amino Acid Score (PDCAAS). Protein Efficiency Ratio was once the ‘go to’ quality standard and still used by some outdated sources, in this account the use of such as has been discounted, as it uses Winstar rat models, that do not translate or correlate to human growth (Sarwar 2007)

The list below outlines 3 paramount protein sources using the 3 standardized scoring systems using literature review drawing specifically on reserch from FAO 2013, Moughan and Rutherfurd 2012, Lewis 2012, Gilani 2012 and Fuller 2012:

Native Whey: BV (159), NPU (92), PDCAAS (1.00)

Micellular Casein: BV (89), NPU (76), PDCAAS (1.00)

Egg white: BV (100), NPU (94), PDCAAS (1.00)

Protein Ranking Scales are determined on the biological values formulated via standards established by the FAO in 1991, and updated in 2016 in conjunctions with WHO and Sarwar, 1997.

Biological Value determines protein quality by measuring how efficiently the human body uptake the tested dietary protein. Specifically, BV measures the nitrogen that is retained in the body and used in tissue and muscle formation. Since BV is a function of how much protein is absorbed and how much ends up being utilized, the theoretical top score is 100. However, since whole egg (the best whole food source of protein content) was originally set as the protein digestibility standard, it is possible for processed protein sources like whey protein concentrate to exceed this value (Moughan and Rutherfurd SM 2012, FAO 2013).

Net Protein Utilization aims to determine the percentage of amino acids from the food source that are converted into protein and utilized by the body. To maximize NPU, dietary protein sources must be easy to digest and provide an effective ratio of EAA. NPU values are usually measured indirectly using protein intake vs. nitrogen excretion (Fuller 2012, FAO 2013).

Protein Digestibility Corrected Amino Acid Score (PDCAAS) measures protein quality based on human essential amino acid requirements and the ability of the human body to digest it. The protein tested is compared to a standard amino acid profile and is given a score from 0-1, with a score of 1.0 indicating maximum amino acid digestibility. PDCAAS is currently considered the most reliable score of protein quality for human nutrition (Gilani 2012, FAO 2013) .

 

Micellar Casein

Micellar casein is the result of whole milk, skimmed and separated from the whey. The kappa casein molecules located on the outer shell of the micelle is negatively charged. It is this property that maintains milk as a liquid as the particles repel one another preventing coagulation. Therefore, to separate the casein the enzyme rennet is added to naturalise the charge; this leaves the end of the protein chain negative and is removed along with the whey component (Hurt 2015). As the kappa proteins are no longer charged they begin to join together. This happens because the freshly cut kappa casein chain (now called para-kappa-casein) is sensitive to picking up minerals. Its cut end link with the phosphate and calcium minerals present in milk to form a bridge that joins the casein micelles together (Augustin 2013).

It was a study in 2003 by Boirie et al that was seen as the catalyst of a great deal of interested and research in to the properties of casein in muscle mass, MPS in athletes and bodybuilders. The study investigated undenatured micellar casein verses caseinates, denatured proteins (whey and casein) and single protein blends. The micellar casein which is isolated from milk by filtration was the main focus, rather than proteins exposed to acid or heat treatments. The filtration method and low temperature in micellar casein preserves the structural integrity of the protein, unlike heat and acids processes. The study assessed micellular caseins time released gastric emptying rate to that provides a prolonged supply of quality protein and amino acids with a high bio-availability rating (FAO 2013).

The results demonstrated that the micellular casein induced a highly significant anticatabolic response due to; 1) slowing down the digestive process to maximise MSP; 2) the high mineral and amino acid content within the micelles; 3) the high quality and bio-availability of protein and protein fractions within the micellar casein, and 4) immunoenhancing properties from the protein fractions (Boirie, 1997).

When high quality whey and micellar casein are combined, the athletes in the Borie 1997 study, reaped the benefits of both proteins. Almost after this study was published, mixing casein and whey became the “cutting edge” in protein formulation, yet many manufactures still opt for profit over quality by using caseinate.

The pivotal element lies with the caseins unique micelle itself. Its spherical structure enables casein to be suspended within milk. However, when heat or acid is used to separate casein out of milk, the micelle’s structures are altered, resulting in a loss of its high bio-available status, biological properties and digestibility (Fox and Brodkorb 2008). The micellar structure is specifically and naturally designed to be digested over a prolonged period of time for optimal absorption, to provide complete nutrition to the mammals’ offspring (Goldberg 2014). The processing is the difference as undenatured casein contains cholecystokinin (CKK) that has the ability to halt catabolism by preserving muscle tissue. CKK is released post dietary ingestion of proteins and fats to facilitate the transit and absorption of the protein such as lactoferrin and lactoperoxidase (Burrington 2014).

Therefore, micellar casein holds intact protein fractions that provides so much more than just a source of amino acids, such as providing an abundance of biologically active proteins that have direct immune and physiological benefits that aren’t provided by heat treated proteins, animal tissue protein sources or vegetable proteins. To maintain the entirety of the micellar caseins biological functions, the casein must be as undamaged as possible. This is the crucial difference between micellar casein inferior caseinates (Zimet, Rosenberg and Livney, 2011). Caseinate is produced by acid or heat. Casein does not dissolve in water, and therefore in caseinates is made more soluble by heating/acid treating to react with inorganic base compounds such as calcium hydroxide where the micelles are damaged, digestive enzymes adversely altered and factions rendered as denatured. Caseinates are also stripped of naturally occurring chelated minerals (Lu 2016).

 

WPC & Isolate

Whey protein concentrate and Whey protein isolate within ProPeptide are derived from the filtration of the liquid whey, separated in the rennet process. Hydolate whey is particularly beneficial to those who have intolerances as the protein have been partly broken down to remove the lactose content (Schaafsma 2012). The capacity of whey protein supplementation to provide a significant benefit to persons engaged in resistance exercise training has been widely accepted in both laboratory and observational studies. Whey concentrate and isolates have been highly effective with athletes and bodybuilders in rapidly gaining lean muscle mass while reducing body fat (Sousa et al. 2012). Whey protein isolate is high in branched-chain amino acids and considered to be fast-acting, and is effective in promoting muscle growth, with enhanced results when whey protein is in combination with the amino acids glutamine and BCAA to enhance MPS and reduce fatigue (Tsuchita H et al.). Studies have also shown that the regular intake of native whey has resulted in a significant reduction in abdominal adiposity in trained and untrained individuals and significantly higher rates of MPS to that of non-native whey products (Le Ruyet and Le Goër, 2010).

Many whey powders are acid treated that rendered the fractions denatured and ineffective, similarly to that of micellar casein.

Native Whey

Native whey is made in one continuous process, unlike many whey powders that are derived from sweet dairy whey that is acid and heat treated, bought by whey processors where a secondary process of pasteurization is required by law that further denatures the EAA, enzymes and protein factions within whey (Hendriks et al., 2012). Native whey protein is not a by-product of cheese, but a superior product produced by the filtration of unprocessed raw milk giving it unique functional and compositional properties compared to traditional acid and heat-treated cheese whey (Shon and Haque, 2007). The native whey process therefore protects the properties of the protein, its minerals and protein fractions, preventing the denaturing that occurs when subjected to acids used in the production of cheese (Burrington 2014). This method of production protects the inherently higher concentrations of BCAA’s; particularly L-Leucine that is proven to have the most positive effect on stimulating protein synthesis and repair due to Leucine being the substrate for the mTORC1 complex triggering the anabolic leading to increased muscle mass and body strength (Sudsa 2012).

Research into native whey dietary proteins have shown to elicit a wide range of metabolic and physiologic functions, that are far beyond their traditional role as sources of energy and indispensable amino acids. Native whey protein intakes play a significant role in the regulation of appetite, food intake, body weight, and body composition (Holt et al 2017). Their role in the regulation of blood pressure, glucose and lipid metabolism, bone metabolism, and immune system is also shown. The role of native whey protein as the most satiating macronutrient in regulation of food intake, body weight and body composition is well-studied. The direct interaction between dietary proteins and the GIT via endogenous satiety signals and the vagus nerve in addition to their effects on protein synthesis are major underlying mechanisms (Frestedt et al., 2017). The interaction of proteins with the GI tract can be elucidated by their effect on gastric emptying rate, communication via the gut-brain axis, and more recently by their effect on gut microbiota (Caron et al., 2017).

2017 Hamarsland et al studied native whey in resistance trained athletes, compared to non- native whey powder alternatives. The study found highly significant results of increased blood concentrations of leucine in those participants ingesting the native whey. Leucine is the anabolic trigger working as the mTORC1 substrate signalling to initial MPS, leading to increased muscle mass and body strength. The study concluded that the native whey induced larger increases in blood concentrations of EAA and leucine, greater phosphorylation of p70S6K, and higher rates of MPS. Native whey also contents higher concentrations of the amino acids, tryptophan and cysteine. Tryptophan increases serotonin, which helps support energy out-put of intensive exercise (Richards et al,. 2009).

Native Whey Protein is only pasteurised once avoiding unnecessary secondary heat treatments that can denature valuable cystine rich peptides. Native Whey Protein is up to 240% higher in cystine (than heat/acid treated whey) which is a very fragile peptide and easily damaged by heat (it’s comprised of two cysteine molecules joined by a disulphide bridge) (Hamarsland et al., 2017). Cystine plays an essential role as a pre-cursor to the powerful antioxidant Glutathione.

 

Egg White Albumen

Egg white albumen is a highly bio-available, complete protein containing all of the essential amino acids and BCAA’s. The main proteins contained within egg white are albumins, mucoproteins and globulins. However, egg white contains 148 individual protein fractions, suspended in an alkaline solution; all of which have been credited to enhance MPS (Jahan and Mihan 2017). With a high protein content, zero fat, nil cholesterol and very low carbohydrate content, bodybuilders have taken advantage of egg white albumens muscle enhancing properties (Kewich et al 2010). Egg white proteins provide an intermediate release of protein, with a gastric emptying rate in-between that of native whey and micellular casein proteins.

Research on the use of egg white albumen protein supplementation is vast and highly substantial in its health and MPS attributes (Moughan 2012). Evidence is conclusive that the use of egg white protein has many positive benefits as a blend and a standalone protein powder source to the increase fat free mass (FFM), 1RM strength and serum free amino acids in resistance trained athletes (Hida et al 2012).

Several studies have reported the efficacy of egg white albumen in the initiation of MPS. Kewich et al (2010) evaluated the effect of albumen protein supplementation on muscle strength during a 10-week period; reporting significant increases in 1rep max bench press and leg press muscle strengths.

Previous studies have evaluated changes in blood amino acids concentrations following a long-term energy intake and found that serum concentrations change temporarily, yet significantly post ingestion stimulates increased MPS due to egg albumens high bio-availability (Hida et al 2012)

Hasegawa et al., 2008, studied the relationship between dietary whey protein and egg white albumen intake on serum metabolites (urea and citrulline) when on a low kilocalorie diets, low in carbohydrates. The 8-week study observed strong correlations in both groups that increased daily protein intake (1.2g/kg) on protein metabolites, compared to those on a placebo supplement. The study also showed that serum cortisol concentrations post-exercise increased after the 8-week regime in the protein groups. Cortisol increases hepatic lipolysis and proteolysis to fuel hepatic gluconeogenesis, suggesting that egg white protein supplementation and whey inhibits muscle damage when following a low carbohydrate, calories restricted diet. This in turn results in decreased myoglobin concentrations (Hasegawa et al., 2008) Egg albumen supplementation demonstrated an ability to further stimulate the process of MPS, when subjected to resistance exercise, increased levels of exercise-induced endogenous anabolic hormones; growth hormone and insulin-like growth factors where seen (Hasegawa et al., 2008). In addition, egg albumen also presented a positive change in urinary composition and nitrogen excretion.

 

Conclusion

It has never been more crystal clear what we need to look for when our aim is to get the very best from a protein based supplement. We can see just how deep the research goes into the various types of protein and how each has its own repertoire of benefits. It is with this information we decided to formulate Pro Peptide. Pro Peptide is and always has been CNP’s flagship product for athletes across the board, no corners where cut, no fillers used and no protein spiking.

The protein within Propeptide is bovine derived undenatured casein, native undenatured whey and egg albumin as they are the favoured protein powder source, for the high BA, PER, NPU and essential amino acids content as shown by the PDCAAS (Schaafsma 2012), so ultimately only the best.

Making Peptide a premium priced product but this being a good indicator of what you are getting. The high-quality for the best results physically possible.

 

 

 

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