Key learnings:
|
What if whey protein could not only help you gain muscle and get stronger, but also protect your cells, enhance detoxification and improve gut and immune function? Here’s what you need to know about non-denatured native whey, other popular processing methods and the effects of processing on its nutritional benefits.
Whey protein is a popular health food supplement derived from cow’s milk. Originally, whey was thought of as a useless by-product of the cheese making process, and discarded. Nowadays, that has changed drastically. Whey was popularised in bodybuilding and athletic communities due to its ease of digestion, complete amino acid profile, high protein content and subsequent effects on increasing muscle mass (1, 2). You’d be hard pressed to find a health food or supplement store not selling whey protein these days.
However, whey is so much more than just another source of protein; it can have a positive effect on our health, but the source and processing of your whey matters.
Not all whey is created equally
First off, let’s consider the difference between 100% grass fed and grain fed whey.
Cows, being ruminate animals, are adapted to eating a diet based on grasses. A healthier cow makes healthier milk leading to healthier whey. Grass fed whey, when compared to grain fed, contains a more favourable profile of omega-3 to omega-6 fatty acids, as well as higher levels of conjugated linoleic acid, and potentially increased levels of amino acids.
Processing diminishes the quality
The majority of whey on the market is produced as a by-product of cheese or casein manufacturing. Rennet, other acids or enzymes are added to heated milk, splitting the solids from the whey. The whey is then pasteurized, dried, may undergo microfiltration, packaged and sold to consumers as whey concentrate. It contains 30-80% protein, some sugar as lactose, and fat.
The high levels of heat, oxidation, enzymatic/acidic treatment and filtration used in processing whey cause irreversible changes to the structure of the proteins in whey, known as denaturation.
Non-denatured native whey is NOT a by-product of cheese manufacturing. It is processed in a way that maintains nutrient levels, keeps protein structures intact and increases bioavailability of other nutrients. Put simply, it has more of what you want, in a way that your body can use.
Encouraging the body to produce glutathione
As explained in this article, glutathione is the body’s ‘master antioxidant.’ Unlike other antioxidants, which work outside the cell, glutathione exerts its effect inside the cell. This enables it to restore cellular damage and protect the mitochondria directly. Mitochondria are the powerhouses of the cell, producing adenosine triphosphate (ATP), our energy currency. Dysfunction of the mitochondria is implicated in many chronic diseases.
Glutathione is also an incredibly important molecule in detoxification processes. It is utilized in both phase I and phase II liver detoxification and is essential for healthy elimination of endogenous and exogenous toxins.
On top of these crucial uses, glutathione can also improve workout recovery time, decrease inflammation and much more (4, 5).
There are a multitude of factors depleting glutathione within the body, including (6, 7):
- Poor sleep
- Stress
- Exposure to environmental toxins such as heavy metals and mould
- Certain medications
- Intense physical exercise
- Anything else that increases oxidative stress
Whey doesn’t contain any glutathione itself, but has ample amounts of the building blocks: cysteine, glutamate and glycine. By consuming these precursors present in whey protein, the body is able to facilitate the production of glutathione when required.
Cysteine and Cystine
Improving cellular levels of cysteine, is believed to be one of the most effective ways of increasing glutathione levels. It is said to be the rate limiting step to producing glutathione, without it, production is severely limited. However, cysteine is broken down in the gut and bloodstream before it can reach the cells. This is where the molecule cystine shines. Cystine is known as a dimeric amino acid, composed of two cysteine molecules covalently bound together. Cystine passes through the gut and bloodstream intact and upon entering the cell, the bond is broken, allowing the 2 cysteine molecules into the cell, to enhance glutathione production. Undenatured whey protein contains higher levels of cystine than denatured whey (8).
Branch Chain Amino Acids (BCAAs)
Whey is also a fantastic source of the BCAAs, leucine, isoleucine and valine. BCAAs are the largest collection of amino acids in the body and, similar to whey, they have been popularized in the bodybuilding and athletic communities.
BCAAs have been found to boost protein synthesis which leads to increased muscle growth, reduced fatigue, improved athletic performance and less muscle soreness (9, 10, 11). Undenatured whey contains more BCAAs per gram than denatured whey.
Lactoferrin
Lactoferrin is a natural peptide found in whey with an affinity for the gastrointestinal tract and immune system. One of its main actions is to bind to iron in the gut (12). This has the effect of reducing the growth of unwanted micro-organisms, such as bacteria and fungi, which feed on unbound iron. As you may have heard, over 80% of our immune system resides in the gut, thus improving health of the gut can have a positive impact on immune function (13).
Lactoferrin can also improve glucose tolerance, which is compromised in type II diabetics, and can improve cardiovascular health (14, 15). Lactoferrin is more abundant in undenatured whey protein when compared to standard high-heat processed products (16).
Serum albumin
Contains the compound glutamylcysteine, the amino acids cysteine and glutamate bound together. These are 2 of the 3 amino acids required for glutathione production. It also appears to have some breast cancer protective effects, though the mechanisms are not fully understood as yet (17).
Immunoglobulins
- Alpha-lactalbumin is a source of cysteine, the rate-limiting amino acid involved in glutathione production (17). It is also naturally high in the amino acid tryptophan, a precursor to the neurotransmitter serotonin, which is a precursor to melatonin, the hormone associated with sleep regulation. Beyond serotonin and melatonin production, tryptophan from alpha-lactalbumin can improve memory, cognitive performance, mood, sleep and depressive symptoms (18, 19, 20, 21).
Alpha-lactalbumin appears to have protective effects on gastric tissue, in addition to increasing the body’s production of antibacterial peptides against a range of micro-organisms including Escherichia coli, Klebsiella pneumoniae, Staphylococcus aureus, Staphylococcus epidermisand Candida albicans. It also prevents some pathogens from adhering to intestinal cells, potentially preventing infection from occurring at all (22).
- Beta-lactoglobulins are a large source of the branch chain amino acids (BCAAs) in whey. The BCAAs boost protein synthesis, increasing muscle growth, lowering fatigue and muscle soreness while improving athletic performance. The beta-lactoglobulins also have an effect on immune function, enhancing the immune response by stimulating cell proliferation. This effect is only significant of beta-lactoglobulin from an undenatured source (8).
Conclusion
To sum up, not all whey is created equally. If your only interest is in providing a rapid source of protein, most wheys will do. Undenatured, native whey may support athletic performance better than denatured whey, due to the higher levels of BCAAs, easier digestibility and bioavailability of glutathione precursors, which can improve recovery. Looking beyond athletic performance, to get most of the healthy aging support, detoxification, digestion and immune-enhancing effects of whey protein, undenatured and native is the first choice for informed, health-conscious consumers.
References
- Ha, E. and Zemel, M.B., 2003. Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people. The Journal of nutritional biochemistry, 14(5), pp.251-258.
- Hulmi, J.J., Lockwood, C.M. and Stout, J.R., 2010. Effect of protein/essential amino acids and resistance training on skeletal muscle hypertrophy: A case for whey protein. Nutrition & metabolism, 7(1), p.51.
- Hoffman, J.R. and Falvo, M.J., 2004. Protein–which is best?. Journal of sports science & medicine, 3(3), p.118.
- Aoi, W., Ogaya, Y., Takami, M., Konishi, T., Sauchi, Y., Park, E.Y., Wada, S., Sato, K. and Higashi, A., 2015. Glutathione supplementation suppresses muscle fatigue induced by prolonged exercise via improved aerobic metabolism. Journal of the International Society of Sports Nutrition, 12(1), p.7.
- Perricone, C., De Carolis, C. and Perricone, R., 2009. Glutathione: a key player in autoimmunity. Autoimmunity reviews, 8(8), pp.697-701.
- Krolow, R., Arcego, D.M., Noschang, C., Weis, S.N. and Dalmaz, C., 2014. Oxidative imbalance and anxiety disorders. Current neuropharmacology, 12(2), pp.193-204.
- Singh, T.D., Patial, K., Vijayan, V.K. and Ravi, K., 2009. Oxidative stress and obstructive sleep apnoea syndrome. Indian J Chest Dis Allied Sci, 51(4), pp.217-24.
- Bounous, G. and Gold, P., 1991. The biological activity of undenatured dietary whey proteins: role of glutathione. Clin Invest Med, 14(4), pp.296-309.
- Shimomura, Y., Murakami, T., Nakai, N., Nagasaki, M. and Harris, R.A., 2004. Exercise promotes BCAA catabolism: effects of BCAA supplementation on skeletal muscle during exercise. The Journal of nutrition, 134(6), pp.1583S-1587S.
- Gualano, A.B., Bozza, T., Lopes De Campos, P., Roschel, H., Dos Santos Costa, A., Luiz Marquezi, M., Benatti, F. and Herbert Lancha Junior, A., 2011. Branched-chain amino acids supplementation enhances exercise capacity and lipid oxidation during endurance exercise after muscle glycogen depletion. J Sports Med Phys Fitness, 51(1), pp.82-8.
- Shimomura, Y., Inaguma, A., Watanabe, S., Yamamoto, Y., Muramatsu, Y., Bajotto, G., Sato, J., Shimomura, N., Kobayashi, H. and Mawatari, K., 2010. Branched-chain amino acid supplementation before squat exercise and delayed-onset muscle soreness. International journal of sport nutrition and exercise metabolism, 20(3), pp.236-244.
- Adlerova, L., Bartoskova, A. and Faldyna, M., 2008. Lactoferrin: a review. Veterinarni Medicina, 53(9), pp.457-468.
- Vighi, G., Marcucci, F., Sensi, L., Di Cara, G. and Frati, F., 2008. Allergy and the gastrointestinal system. Clinical & Experimental Immunology, 153, pp.3-6.
- Zapata, R.C., Singh, A., Pezeshki, A., Nibber, T. and Chelikani, P.K., 2017. Whey Protein Components-Lactalbumin and Lactoferrin-Improve Energy Balance and Metabolism. Scientific reports, 7(1), p.9917.
- Kajikawa, M., Ohta, T., Takase, M., Kawase, K., Shimamura, S. and Matsuda, I., 1994. Lactoferrin inhibits cholesterol accumulation in macrophages mediated by acetylated or oxidized low-density lipoproteins. Biochimica et Biophysica Acta (BBA)-Lipids and Lipid Metabolism, 1213(1), pp.82-90.
- Nguyen, D.N., Sangild, P.T., Li, Y., Bering, S.B. and Chatterton, D.E., 2016. Processing of whey modulates proliferative and immune functions in intestinal epithelial cells. Journal of dairy science, 99(2), pp.959-969.
- Tsutsumi, R. and Tsutsumi, Y.M., 2014. Peptides and proteins in whey and their benefits for human health. Austin J Nutri Food Sci, 1(1), p.1002.
- Layman, D.K., Lönnerdal, B. and Fernstrom, J.D., 2018. Applications for α-lactalbumin in human nutrition. Nutrition reviews, 76(6), pp.444-460.
- Booij, L., Merens, W., Markus, C.R. and Van der Does, A.W., 2006. Diet rich in α-lactalbumin improves memory in unmedicated recovered depressed patients and matched controls. Journal of Psychopharmacology, 20(4), pp.526-535.
- Markus, C.R., Olivier, B. and de Haan, E.H., 2002. Whey protein rich in α-lactalbumin increases the ratio of plasma tryptophan to the sum of the other large neutral amino acids and improves cognitive performance in stress-vulnerable subjects. The American journal of clinical nutrition, 75(6), pp.1051-1056.
- Markus, C.R., Olivier, B., Panhuysen, G.E., Van der Gugten, J., Alles, M.S., Tuiten, A., Westenberg, H.G., Fekkes, D., Koppeschaar, H.F. and de Haan, E.E., 2000. The bovine protein α-lactalbumin increases the plasma ratio of tryptophan to the other large neutral amino acids, and in vulnerable subjects raises brain serotonin activity, reduces cortisol concentration, and improves mood under stress. The American journal of clinical nutrition, 71(6), pp.1536-1544.
- Tai, C.S., Chen, Y.Y. and Chen, W.L., 2016. β-lactoglobulin influences human immunity and promotes cell proliferation. BioMed research international, 2016.