CHARACTERISTICS AND BIOLOGICAL PROPERTIES OF WHEY PROTEINS

Ôªø CHARACTERISTICS AND BIOLOGICAL PROPERTIES OF WHEY PROTEINS Reference Docs - Characteristics and Biological Properties of Whey Proteins

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Victory Nutrition Reference

Characteristics and Biological Properties of Whey Proteins
Courtesy Bioplex Nutrition

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Whey is a reliable source of high quality and biologically active proteins, carbohydrates and minerals. Whey proteins are easily digested and contain an amino acid profile that meets all the essential amino acid requirements set by the Food and Agriculture Organization/World Health Organization (FAO/WHO). Individual whey proteins contain a variety of functional and nutritional attributes, which are related to the structure and biological functions of these proteins.
β-lactoglobulin
β-lactoglobulin is approximately 50% of the total whey protein content. This protein has numerous binding sites for minerals, fat soluble vitamins and lipids, and acts as a transport protein for desirable lipophilic compounds such as tocopherol and vitamin A.1,2 Modification of β-lactoglobulin results in products that have strong antiviral activity against human immunodeficiency virus types 1 and 2.3
α-lactalbumin
α-lactalbumin comprises about 25% of the total whey protein content. This protein possesses an excellent amino acid profile, which is rich in lysine, leucine, threonine, tryptophan and cystine. The main known biological function of α-lactalbumin is to modulate the synthesis of lactose in the mammary gland.4 Addition of this protein is strongly advocated in the formulation of "humanized" infant formulas and to create other products for people with limited or restricted protein intakes. Limited work has suggested that α-lactalbumin may be effective as an anti-cancer agent in several different types of cancer.5
Immunoglobulins
Immunoglobulins are a complex group of proteins that make a significant contribution to the protein content as well as exerting an important immunological function. They are well recognized to provide disease protection to newborns through passive immunity and there is evidence that the immunoglobulins also may have a role in disease control in adults. It is known that whey protein concentrates from mixed milk supplies generally contain sufficient antibody to E. coli K-99 to meet the requirements of the USDA to serve as a colostrum supplement.
Bovine serum albumin
Bovine serum albumin (BSA) has a good essential amino acid profile. BSA binds free fatty acids, other lipids and flavor compounds.6 BSA's primary function has been associated with its lipid binding properties.7 It may play a role in mediating lipid oxidation.8,9 Denatured BSA might reduce the probability of a person acquiring certain diseases, such as insulin dependant diabetes or auto-immune disease.10
Lactoferrin
Lactoferrin is an iron binding protein and has the potential capability of acting as an antimicrobial agent related to its iron chelating ability, thus depriving microorganisms of a source of iron. Most recently, it has been shown to have a number of other physiological and biological functions. The biological activities of lactoferrin include iron transport,11 antimicrobial activity,12 antifungal activity,13 antiviral activity,14 anticancer activity,15,16 toxin binding properties,17 immunomodulating effects,18 wound and wound healing,19 and anti-inflammatory activity.20
Lactoperoxidase
Lactoperoxidase has been identified as an antimicrobial agent in milk, saliva and tears.21 The lactoperoxidase system has been proven to be both bactericidal and bacteriostatic to a wide variety of microorganisms, while having no effect on the proteins and enzymes of the organisms producing it.22 Clinical studies have supported the possibility that plaque accumulation, gingivitis and early onset carries may be reduced by appropriate lactoperoxidase preparations.
Glycomacropeptide
Glycomacropeptide (GMP), the glycosylated portion of caseinomacropeptide (CMP), is present in sweet whey formed following the κ-casein cleavage and casein precipitation by rennin; it is absent from acid whey. The biological and physiological properties that have been attributed to GMP or peptides derived from it include: reduction in gastric secretion, dental plaque and dental caries inhibition, growth promoting activity for Bifidobacteria, product for control of phenylketunoria, inhibition of platelet aggregation and others.23,24 GMP can supress appetite via stimulation of the pancreatic hormone cholecystokinin (CCK) release. It alters pigment production in melanocytes, acts as prebiotic and has immunomodulatory actions. Physiologic activity of GMP depends on its glycosylation.
REFERENCES:
1. Perez, M.D. and Calvo, M. (1995) Interaction of beta lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein; a review. J. Dairy Sci. 78:978-988.

2. Hambling, S.C., McAlpine, A.S. and Sawyer, L. (1992) Beta-lactoglobulin. In Advanced Dairy Chemistry Vol. 1. Proteins. (Fox, P.F., ed.), pp. 141-190. Elsevier Applied Science. London and New York.

3. Swart, P.J., Kuipers, M.E., Smit, C., Pauwels, R., DeBethune, M.P., DeCleroq, E., Meijer, D.K. and Huisman, J.G. (1996) Antiviral effects of milk proteins; acylation results in polyanionic compounds with portent activity against human immunodeficiency virus types 1 and 2 in vitro. Aids Res. Human Retroviruses 12:769-775.

4. Yadav, S. and Brew, K. (1991) Structure and function in galactosyltransferase. Sequence locations of alpha-lactalbumin binding site, thiol groups and di-sulfide bond. J. Biol. Chem. 266:698-703.

5. Ganjam, L.S., Thornton, W.H. Jr., Marshall, R.T. and MacDonald, R.S., (1997) J. Dairy Sci. 80 (10):2325-2329.

6. Kinsella, J.E. and Whitehead, D.M. (1989) Proteins in whey: Chemical, physical and functional properties. Adv. Food Nutr. Res. 33:343-438.

7. Fox, P.F. and Flynn, A.F. (1992) In Advanced Dairy Chemistry Vol. I. Proteins. (Larson, B.L. ed.), pp. 255-281. Elsevier Applied Science, London and New York.

8. Smith, C., Halliwell, B. and Aruoma, O.I. (1992) Protection of albumin against the pro-oxidant actions of phenolic dietary components. Food Chem. Toxicol. 30:483-489.

9. Koisumi, C. and Nonaka, J. (1975) Comparison of catalytic function of oxymyoglobin and metmyoglobin for the oxidation of linoleate in aqueous emulsions. Bull Jap. Soc. Sci. Fish. 41:1053-1061.

10. Strand, F.T. (1995) Denatured bovine serum albumin milk products and method therefore. US patent 5 473 050.

11. Nagasako, Y., Saito, H., Tamura, Y., Shimamura, S. and Tomita, M. (1993) Iron binding properties of bovine lactoferrin in iron rich solution. J. Dairy Sci. 76:1876-1881.

12. Denisove, I. I., Gennadeva, T.I., Zhdanova, T.V., Hristova, M. and Khazenson, L.B. (1996) The action of lactoperoxidase, lactoferrin and lactoglobulin on Shigella sonnei in an in vivo experiment. Ahurnal Mikrobiol. Epidemil. Immunogiol. 1:66-69.

13. Bellamy, W., Yamauchi, K., Wakabayashi, H., Takakura, N., Shimamura, S. and Tomita, M. (1994) Antifungal properties of lactoferricin B, a peptide from the N-terminal region of lactoferrin. Letters Appl. Microbiol. 18:230-233.

14. Swart, P.J., Kuipers, M.E., Smit, C., Van der Strate, B.W., Harmsen, M.C. and Meijer, D.K. (1998) Lactoferrin: Antiviral activity of lactoferrin. Adv. Exp. Med. Biol. 443:205-13.

15. Uchida, Y., Sekine, K., Kuhara, T., Takasuka, N., Ligo, M. and Tsuda, H. (1998) Inhibitory effects of bovine lactoferrin on intestinal polyposi in the Apc(min) mouse. Cancer Letters 134:141-145.

16. Uchida, Y., Sekine, K., Kuhara, T., Takasuka, N., Ligo, M., Maeda, M. and Tsuda, H. (1999) Possible chemopreventative effects of bovine lactoferrin on esophagus and lung carcinogensis in the rat. Jap. J. Cancer Res. 90:262-267.

17. Mattsby-Baltzer, I., Roseanu, A., Motas, C., Elveerfors, J., Engberg, I. and Hanson, L.A. (1996) Lactoferrin or a fragment thereof inhibits the endotoxin induced interleukin-6 response in human monocytic cells. Ped. Res. 40:257-262.

18. Shinoda, I., Takase, M., Fukuwateri, Y., Shimamura, S., Koller, M. and Konig, W. (1996) Effect of lactoferrin and lactoferricin on the release of interleukcin 8 from human polymorphonuclear leukocytes. Biotechnol. Biochem. 60:521-523.

19. Bockman R., and Guidon, P. (1996) Methods of enhancing wound healing and tissue repair. U.S. Patent 5 556 645.

20. Bayeye, S., Elass, E., Nazuruier, J., Spik, G. and Legrqnd, D. (1999) Lactoferrin, a multifunctional glycoprotein involved in the modulation of the inflammatory process. Clinical Chem and Lab. Med. 37:281-286.

21. Reiter, B. and Perraudin, J.P. (1991) Lactoperoxidase: Biological functions in Peroxydases in Chemistry and Biology. CRC Press Inc. pp. 143-180.

22. Bjorck, L. (1992) Lactoperoxidase. In Advanced Dairy Chemistry Vol. I. Proteins. (Larson, B.L., ed.), pp. 331-336. Elsevier Applied Science. London and New York.

23. El Salam, M. H., El Shibiny, A. and Buchheim, W. (1996) Characteristics and Potential Uses of the Casein Macropeptide. Int. Dairy J. 6(4):327-341.

24. Dziuba, J. and Minkiewicz, P. (1996) Influence of glycosylation on micelle-stabilizing ability and biological properties of the C-terminal fragments of cow¬¥s ‘†-casein. Int. Dairy J. 6:1017-1044.

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