Health Benefits of Whey Protein: A Review
Abstract
This paper views whey protein system in detail and shows that whey protein constitute 20% of
whole milk protein and have various different proteins, such as -lactalbumin (-LA), -
lactoglobulin (-LG), immunoglobulins (Igs), glycomacropeptide (GMP), lactoferrin (LF) and
lactoperoxidase. Whey protein has all 20 amino acids and so contains all essential nine amino
acids. It serves as rich and balanced source of sulfur amino acids which have main role as
antioxidants. Current studies regarding potential of whey proteins show they have numerous
health benefits elsewhere basic nutrition. Large number of researches of whey and whey
components from in vitro, experimental human and animal studies advise various beneficial
bioactivities. Similarly, supplements of whey protein have number of proven benefits.
Introduction
Milk has two proteins namely casein and whey. Whey protein may get separated from casein or
formed as a sub product in making of cheese. Whey protein is high quality, complete protein
consists of all essential amino acids. Moreover it is easily digestible and get absorbed from gut
rapidly in comparison to other protein types (Kosikowski, 1982).
Now we detail at whey protein system, we can see that whey protein, 20% of total milk
protein, consists of several different proteins, including -lactoglobulin (-LG), -lactalbumin
(-LA), the heavy-and light-chain immunoglobulins (Igs), bovine serum albumin (BSA),
lactoferrin (LF), lactoperoxidase, and glycomacropeptide (GMP) (De Wit, 1998).
It contains cysteine which has three to four times more bioavailability than other proteins.
Cysteine plays an important role in making of glutathione, which is a tripeptide having
anticarcinogen, antioxidant and immune stimulatory properties. It has also a key role in protein
metabolism regulation of whole body which causes changes in body composition (Bounous et
al., 1989). Leucine is mainly crucial for tissue repair and growth (Anthony, 2001). Valine,
leucine and isoleucine are considered important metabolic regulators for glucose and protein
homeostasis and lipid metabolism and thus have a role in weight control (Kimball et al., 2002).
1. Antimicrobial and Antiviral Activities
There are several biologically active proteins in milk proteins. Proteins and peptides of milk
particularly whey, exhibit antimicrobial and antiviral activities. Whey protein has certain
components which show protection against viruses, bacteria and toxins. These components may
include lactoperoxidase, lactoferricin, Igs, sphingolipids and GMP (Wakabayashi et al., 2003).
Moreover, antimicrobial peptides get produced when proteolysis of protein occurs in
gastrointestinal transit. Lactoferricin, -LA and -LG have been assessed against (HIV-1) human
immunodeficiency virus type-1. Specifically, -LG are potential agents to prevent genital
herpesvirus infection transmission along with spread of HIV (Kokuba et al., 1998). Lactoferrin
hinder a wide range of microorganisms such as gram-positive bacteria, gram-negative bacteria,
fungi, parasitic protozoa and yeast. It has also been considered to prevent the growth of injurious
foodborne pathogens including Listeria monocytogenes and E. coli (Floris et al., 2003).
Lactoferrin also shows considerable antiviral activity against HIV, (HCMV) human
cytomegalovirus, hepatitis C, herpes viruses, alphavirus and B and G viruses. Furthermore,
Lactoferrin is effective against various non-enveloped viruses including enterovirus, adenovirus,
enterovirus, rotavirus (Pan et al., 2006). Antibacterial activity of lysozyme also get enhanced by
it. Lactoferrin is of particular importance for intestinal function and for inhibition of
gastroenteric diseases as it counters intestinal microflora. As LF shows bactericidal activity
against pathogenic microbes like coliform, it also offers probiotic provision for benifical
microorganisms like Lactobacilli ssp and Bifidobacteria (Yamauchi et al., 2006). Since
Helicobacter pylori is considered causative agent in large number of duodenal ulcers, various
recent studies reported daily intake of LF effectively suppresses colonization of gut with
Helicobacter pylori (Collins et al., 2006).
Whey protein stimulates immune system and prevents infection. It also helps to inhibit
rotaviral diarrhea, that is a common infection which causes death of about 500,000 children per
anum. Current research has shown that infants who fed on whey protein (-Lactalbumin) had no
symptoms of diarrhea (Wolber et al., 2005).
The products containing lactoperoxidase have been approved clinically to prevent
injurious microbes related to oral irritation and gingivitis, and promote healing and curing of
bleeding gums and lowers inflammation and also counter both causes and effects associated with
halitosis (bad breath) (Tnevuo, 2002). One of a study shows that administration of particular
immunoglobulins in food product can increase the shelf life of that product whereas it also helps
in inhibiting oral infections and dental caries (Wei et al., 2002).
2. Immune Modulating Activity
Whey proteins and its components also contribute in immunity of host (Harper, 2003). Whey
consists of such bioactive compounds that can provide protection viruses and infections, some
cancers and also may enhance the immunity of the body. Mainly three whey peptides (LF and -
LA, -LG) are important for the enhancement of immune system by increaased production of
glutathione. IgF-I and IgF-II are known to be as growth factors promote gut health and healing of
wound (Bucci & Unlu, 2000).
Dietary whey protein has highest immune response. Immunomodulatory effects of bodys
immune system effect by certain whey proteins such as -LA, -LG, LF. Lactoferrin is produced
by neutrophils and boost up the growth of numerous cells of defense system such as
macrophages, monocytes, lymphocytes, antibody and humoral immune response (Wakabayashi
et al., 2003). During enzymatic digestion some immunomodulatory peptides of whey proteins
may get released and so Identification and separation of such bioactive peptides can lead to
formation of effective immunomodulating products (Mercier & Gauthier, 2004).
Whey protein components like -LA, and -LG, -Lactorphin and -lactorphin act as
angiotensin converting enzyme inhibitors (Mullally et al., 1996). Enzymatic hydrolysis of -LA
yields to components that having the capability to bind with copper, iron, calcium, magnesium,
manganese, phosphorus and zinc. In mammals, lactoferrin plays a crucial role in iron regulation.
Furthermore, it has examined that usage of iron-saturated LF did not develop any side effects
associated with iron supplements like cramps or stomach pain (Uchida et al., 2006).
3. Anticancinogenic Properties
Cancer patients going through chemotherapy usually are struggling to meet their daily nutritional
needs because of lack of appetite and nausea. Whey protein is readily digestible and quite gentle
to the system, thus is an exceptional protein choice for cancer patients (Bounous et al., 1991).
Some cancers can also be prevented with the help of whey proteins and peptides along with other
whey products. Various studies show that, this anticancer activity of whey protein may be
associated with the Sulphur amino acid contents like methionine and cysteine (McIntosh et al.,
1998).
Whey protein is beneficial in terms of inhibiting growth of intestinal tumors. Diet
containing whey protein have been revealed to lessen mammary, intestinal and colon cancers
(Hakkak et al., 2001). Whey protein has certain other important components which are beneficial
to health. Its less weight molecular peptides act as natural antioxidants potentiators that are
protective against aging of body tissues and some cancers (Bounous et al., 2000).
One of a vitro study shows whey protein increased the efficiency of anticancer drug. In
experimental animals, who have been given chemical carcinogens, bovine lactoferrin when given
orally in the post-initiation stage, has been shown to considerably inhibit colon, lung, esophagus
and bladder cancers (Akin, 2010). Other experiments also show that sphingomyelin and other
sphingolipids inhibit development of colon tumor (Schmelz et al., 2000).
4. Cardiovascular Health
Whey proteins significantly improve cardiovascular health. Milk proteins assist in lowering high
blood pressure. Fermented milk containing whey protein concentrate causes triglyceride levels in
blood to be lowered (Kawase et al., 2000). Moreover, whey protein improves vascular function
and blood pressure among obese and overweight people. It has been reported that -LG is able to
bind with cholesterol. Also, lactoferrin potentially prevent accumulation of cholestery esters and
lowers blood pressure (Wang et al., 1997).
Whey protein hinders the activity of ACE. ACE basically converts inactive hormone
angiotensin I into angiotensin II which causes contraction of smooth muscle, therefore increase
blood pressure. So blood pressure reduces upon inhibition of ACE. Dose of 20 g hydrolyzed
whey protein, lowers blood pressure and raises white blood cells. It also lowers down level of
low-density lipoprotein (LDL) cholesterol (Pins & Keenan, 2002).
5. Physical Performance
According to the review, whey and whey products offer various benefits for those who have
physically active lifestyles (Ha & Zemel, 2003). Branched chain amino acids are abundant in
whey protein and consider highest in any of the natural food source. BCAAs get directly
metabolized into muscle tissue and are the first ones to utilize during exercise or resistance
training, thus branched chain amino acids are important for athletes. Branched chain amino acids
provided by whey protein in the body, restore lowered levels and start rebuilding and repairing
lean muscle tissue. In elderly people, essential amino acids and whey peptides are likewise
effective in stimulating synthesis of muscle protein (Paddon-Jones et al., 2005). These amino
acids act as energy source in the time of endurance exercise and allow athletes to get themselves
trained intensively for longer time periods (Layman, 2003).
Furthermore, whey protein is rich source of essential amino acid i.e. leucine. Leucine is
vital for athletes since it has a key role in the promotion of muscle growth and muscle protein
synthesis. It has been shown by the researches that diet containing high amount of leucine are
beneficial for individuals who exercise, as it helps in gaining more lean muscle tissues and less
body fat comparatively to those who have lower levels of leucine in their diet. It is easily
digestible protein and get absorbed in the body efficiently. Whey protein is also termed as fast
protein due to their ability to provide nourishment to muscles rapidly. Whey protein is abundant
in arginine and lysine amino acids, which may upsurge release of growth hormone, and act as a
stimulator for muscle growth (Cribb et al., 2007).
6. Bone Health
There are several components of milk effective for healthy bones. Milk protein stimulate
formation of bones and suppresses resorption of bone among healthy adults. This basic protein of
milk is found in whey protein fraction. 300 mg of milk basic protein increases serum Osteocalcin
concentrations in the serum is increased by intake of 300 mg milk basic protein. Milk basic
protein helps bone formation and prevents bone resorption (Toba et al., 2003). Milk basic protein
in whey is in active form and activates osteoblast. Lactoferrin effectively regulate activity of
bone cells and promotes bone formation. LF decreases breakdown of bone and increases
differentiation of osteoblasts to form new bones (Lorget et al., 2002). LF has strong anti-
apoptotic, anabolic and differentiating effects on osteoblasts, and it impedes osteoclastogenesis.
It is a crucial therapeutic target in bone disorders like osteoporosis and probably the important
physiological regulator in bone growth (Naot et al., 2005).
Glycomacropeptide enhances teeth enamel remineralization and prevent enamel
demineralization activity (Johanson, 2002). Some components of whey protein like proteose-
peptones could protect demineralization of tooth tissue and other components of whey, due to
having immunostimulatory effects, might show advantageous effects on dental plaque (Van Der
Mast & Fekkes, 2000)
7. Other Health Benefits
Imbalanced brain serotonin levels could cause negative effects in body such as delirium, fatigue
and chronic stress (Markus et al., 2002). Whey protein containing -LA with high tryptophan
levels (which act as precursor of serotonin) effectively work for cognitive performance
especially in stress-vulnerable people. So whey protein having high content of -LA boost up
serotonin activity, when -LA is fed to the stressed individuals (Jonkman et al., 2005).
Furthermore, it reduces tiredness and helps to be attentive. infant formula having
hydrolyzed whey protein (predigested) is beneficial in order that it reduces the risk of developing
allergies later as it may possible in standard infant formula (Rosaneli et al., 2002).
After surgery and burn therapy, physicians often recommended to have high protein
products with more of the whey more of the whey protein content. Since, whey protein
comprises of many such components that are found in human breast milk too, so due to this
reason, it is a prime ingredient in most of the infant formulas, including premature infants too.
Whey protein also prevents gastric mucosa from ethanol damage (Boirie et al., 1997).
Conclusion
The health benefits of whey protein and whey proteins have been a subject of growing
commercial interest in the context of health-promoting functional foods. Whey components,
particulary the proteins and peptides, will incresingly be preferred as ingredients for functional
foods and nutraceuticals as active medical agents. They built upon the strong consumer trends
for health and wellbeing, and continuing discovery and substantiation of the biological
functionalty of whey constituents. As a result, we are likely see major developments by the food
and healthcare sectors in the widespread application of whey proteins and their associated
peptides as functional food ingredients, nutraceuticals, and dietary supplements.
References
1. F.V. Kosikowski, Whey and whey foods, in: F.V. Kosikowski (Eds.), Cheese and
Fermented Milk Foods, Edwards Brothers, New York, 1982, pp. 446-469.
2. J.N. De Wit, Nutritional and functional characteristics of whey proteins in food products,
J. Dairy Sci. 81 (1998) 597-608.
3. A.K. Shoveller, B. Stoll, R.O. Ball, D.G. Burrin, Nutritional and functional importance of
intestinal sulphur acid metabolism, J. Nutr. 135 (2005) 1609-1612.
4. R.L. Walzem, C.J. Dillard, J.B. German, Whey components: Millenia of evolution create
functionalities for mammalian nutrition: What we know and what we may be
overlooking, Critical Reviews in Food Science and Nutrition 42 (2002) 353-375.
5. G. Bounous, F. Gervais, V. Amer, G. Batist, P. Gold, The influence of dietary whey
protein on tissue glutathione and disease of aging, Clin. Invest. Med. 12 (1989) 343-349.
6. J.C. Anthony, Signalling pathway involved in the translocational control of protein
synthesis in skeletal muscle by leucine, J. Nutr. 131 (2001) 856-860.
7. S.R. Kimball, L.S. Jefferson, Control of protein synthesis by amino acid availability,
Curr. Opin. Clin. Nutr. Metab. Care 5 (2002) 63-67.
8. B. Bulut Solak, N. Akn, Nutritional value and health benefits of whey proteins,
International Scientific Conference on Nutraceuticals and Functional Foods, Zilina,
Slovakia, June 9th-11th, 2009, p. 18.
9. H. Wakabayashi, N. Takakura, S. Teraguchi, Y. Tamura, Lactoferrin feeding augments
peritoneal macrophage activities in mice intraperitoneally injected with inactivated
Candida albicans, Microbiol. Immunol. 47 (1) (2003) 37-43.
10. R. Floris, I. Recio, B. Berkhout, S. Visser, Antibacterial and antiviral effects of milk
proteins and derivatives thereof, Curr. Pharm. Design 9 (2003) 1257-1275.
11. H. Kokuba, L. Aurelian, A.R. Neurath, 3-Hydroxyphthaloyl--lactoglobulin: IV.
Antiviral activity in the mouse model of genital herpesvirus infection, Antivir. Chem.
Chemother. 9 (1998) 353-357.
12. Y. Pan, B. Shiell, J. Wan, M.J. Coventry, H. Roginski, A. Lee, et al., Antiviral properties
of milk proteins and peptides, Int. Dairy J. 16 (2006) 1252-1261.
13. R. Yamauchi, E. Wada, D. Yamada, M. Yoshikawa, K. Wada, Effect of lactotensin on
acute stress and fear memory, Peptides 27 (12) (2006) 3176-3182.
14. J. Collins, A. Ali-Ibrahim, D.T. Smoot, Antibiotic therapy for Helicobacter pylori, Med.
Clinics of North America 90 (6) (2006) 1125-1140.
15. F.M. Wolber, Supplemental whey protein concentrate reduces rotavirus-induced disease
symptoms in suckling mice, J. Nutr. 135 (2005) 1470-1474.
16. W.M. Bruck, S.L. Kelleher, G.R. Gibson, K.E. Nielsen, D.E.W. Chatterton, B.
Lnnerdal, rRNA probes used to quantify the effects of glycomacropeptide and alpha
lactalbumin supplementation on the predominant groups of intestinal bacteria of infant
rhesus monkeys challenged with enteropathogenic Escherichia coli, J. Pediatr.
Gastroenterol. Nutr. 37 (3) (2003) 273-280.
17. J. Tnevuo, Clinical application of antimicrobial host proteins lactoperoxidase, lysozyme
and lactoferrin in xerostomia, efficacy and safety, Oral Diseases 8 (2002) 23-29.
18. H. Wei, V. Loimaranta, J. Tenovuo, S. Rokka, E.L. Syvaoja, H. Korhonen, Stability and
activity of specificantibodies against Streptococcuc mutans and Streptococcus sobrinus in
bovine milk fermented with Lactobacillus rhamnosusstrain GG or treated at ultra high
temperature, Oral Microbo. Immunol. 17 (2002) 9-15.
19. W.J. Harper, Biological properties of whey components: A review, The American Dairy
Products Institute, Chicago, IL, 2004, 2001 with updates 2003.
20. L.R. Bucci, L. Unlu, Protein and aminoacids in exercise and sport, in: J. Driskell, I.
Wolinsky (Eds.), Energy Yielding Macronutrients and Energy Metabolism in Sports
Nutrition, CRC press, Boca Raton, FL., 2000, pp. 197-200.
21. H. Wakabayashi, M. Takase, M. Tomita, Lactoferricin derived from milk protein
lactoferrin, Curr. Pharm. Design 9 (2003) 1277-1287.
22. A. Mercier, S.F. Gauthier, I. Fliss, Immunomodulating effects of whey proteins and their
enzymatic digests, Int. Dairy J. 14 (3) (2004) 175-183.
23. M.M. Mullally, H. Meisel, R.J. FitzGerald, Synthetic peptides corresponding to -
lactalbumin and -lactoglobulin sequences with angiotensin-I-converting enzyme
inhibitory activity, Biol. Chem. Hoppe-Seyler 377 (4) (1996) 259-260.
24. T. Uchida, T. Oda, K. Sato, H. Kawakami, Availability of lactoferrin as a natural
solubilizer of iron for food products, Int. Dairy J. 16 (2) (2006) 95-101.
25. G. Bounous, P. Citation, P. Gold, The biological activity of undenatured dietary whey
proteins: Role of glutathione, Clin. Invest. Med. 14 (4) (1991) 296-309.
26. G.H. McIntosh, P.J. Royle, R.K. Le Leu, G.O. Regester, M.A. Johnson, R.L. Grinsted, et
al., Whey proteins as functional food ingredients, Int. Dairy J. 8 (1998) 425-434.
27. R. Hakkak, S. Korourian, M.J. Ronis, Dietary whey protein protects against
azoxymethane-induced colon tumors in male rats, Cancer Epidemiol. Biomarkers Prev.
10 (5) (2001) 555-558.
28. G. Bounous, G. Batist, P. Gold, Whey protein concentrate (WPC) and glutathione
modulation in cancer treatment, Anticancer Research 20 (6C) (2000) 4785-4792.
29. N. Akn, Modern Dairy Technology, Damla Ofset, Konya, 2010, pp. 359-413.
30. E.M. Schmelz, M.C. Sullards, D.L. Dillehay, Colonic cell proliferation and aberrant crypt
foci formation are inhibited by dairy glycosphingolipids in 1, 2-dimethylhydrazine-
treated CF1 mice, J. Nutr. 130 (2000) 522-527.
31. M. Kawase, H. Hashimoto, M. Hosoda, H. Morita, A. Hosono, Effect of administration
of fermented milk containing whey protein concentrate to rats and healthy men on serum
lipid and blood pressure, J. Dairy Sci. 83 (2) (2000) 255-263.
32. Q. Wang, J.C. Allen, H.E. Swaisgood, Binding of vitamin D and cholesterol to
lactoglobulin, J. Dairy Sci. 80 (6) (1997) 1054-1059.
33. J.J. Pins, J.M. Keenan, Antihypertensive effects of a hydrolyzed whey protein isolate
supplement (BioZate1), Presented at the 11th International Congress on Cardiovascular
Pharmacotherapy, Montreal, Quebec, Canada, 2002.
34. E. Ha, M.B. Zemel, Functional properties of whey, whey components and essential
amino acids: Mechanisms underlying health benefits for active people: A review, J. Nutr.
Biochem. 14 (5) (2003) 251-258.
35. D. Paddon-Jones, M. Sheffield-Moore, C.S. Katsanos, X. Zhang, R.R. Wolfe, Differential
stimulation of muscle protein synthesis in elderly humans following isocaloric ingestion
of amino acids or whey protein, Experimental Gerontology 42 (2) (2005) 215-219.
36. D. Layman, The role of leucine in weight loss diets and glucose hemeostasis, J. Nutr. 133
(2003) 261-267.
37. P.J. Cribb, A.D. Williams, C.G. Stathis, Effects of whey isolate, creatine and resistance
training on muscle hypertrophy, Med. Sci. in Sports and Exercise 39 (2) (2007) 298-307.
38. Y. Toba, Y. Takada, Y. Matsuoka, Y. Morita, M. Motouri, T. Hirai, et al., Milk basic
protein promotes bone formation and suppresses bone resorption in healthy adult men,
Biosci. Biotechnol. Biochem. Res. Commications 65 (6) (2001) 1353-1357.
39. F. Lorget, J. Clough, M. Oliveira, Lactoferrin reduces in vitro osteoclast differentiation
and resorbing activity, Biochem. Biophys. Res. Commun. 296 (2002) 261-266.
40. D. Naot, A. Grey, I.R. Reid, J. Cornish, LactoferrinA novel bone growth factor, Clin.
Med. Res. 3 (2) (2005) 93-101.
41. I.S. Johanson, Milk and dairy products: Possible effects on dental health, J. Nutr. 46
(2002) 119-122.
42. R.C. Van Der Mast, D. Fekkes, Serotonin and amino acids: Partners in delirium
pathophysiology, Semin. Clin. Neuropsychiatry 5 (2) (2000) 125-131.
43. C.R. Markus, B. Olivier, E.H. de Haan, Whey protein rich in alpha-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, American J. Clin. Nutr. 75
(6) (2002) 1051-1056.
44. C.F. Rosaneli, A.E. Bighetti, M.A. Antnio, J.E. Carvalho, V.C. Sgarbieri, Efficacy of
whey protein concentrate on the inhibition of stomach ulcerative lesions caused by
ethanol ingestion, J. Med. Food 5 (4) (2002) 221-228.
45. Y. Boirie, M. Dangin, P. Gachon, M.P. Vasson, J.L. Maubois, B. Beaufrere, Slow and
fast dietary proteins differently modulate postprandial protein accretion, Proceeding of
the National Academy of Sci. 94 (1997) 14930-14935.