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Whey Protein - Wikipedia, The Free Encyclopedia

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W hey pr otei n - W i ki pedia, the fr ee encyclopedi a

Whey protein From Wikipedia, the free encyclopedia

Whey protein is a mixture of globular proteins isolated from whey, the liquid liquid material created as a by-product of cheese  production.

Whey protein protein is commonly commonly marketed and ingested as a dietary supplement, and and various various health claims have been attributed to it in the alternative medicine comm community.[1] Although whey  proteins are responsible responsible for some milk aller gies, gies, the major  major  allergens in milk milk are the caseins.[2][3]

Contents

Containers of whey protein being sold at a health food store.

1 Production 2 Composition 3 Major forms 4 Health effects 5 R eferences eferences 6 External links

Production  Main article: Whey Whey is left over when milk is coagulated during the process process of cheese production, and contains co ntains everything that is soluble from milk after the pH pH is dropped to 4.6 during during the coagulation process.[4] It is It is a 5% solution of lactose lactose in water, with some minerals and lactalbumin. lactalbumin.[5] The fat is removed and then processed processed for  human foods.[5] Processing can be done by simple drying, or the protein content can be increased increased by removing removing lipids  lipids and other non-protein materials. materials.[6] For example, example, spray drying after membr ane ane filtration separates the proteins from whey.[7] Whey can be denatured by heat. High heat (such as the sustained high temperatures above 72 °C associated with the pasteurization process) denatures whey proteins. While native whey protein does not aggregate upon renneting or acidification of milk, denaturing the whey protein triggers hydrophobic interactions with other proteins, and the formation of a protein gel.[6] Heat-denatured whey can still cause allergies in some  people.[8]

Composition https://en.wi ki pedia.or g/wi ki/W hey_pr otei n#Heal th_effects

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Whey protein is the collection of globular proteins isolated from whey. The protein in cow's milk is 20% whey protein and 80% casein protein,[9] whereas the protein in human milk is 60% whey and 40% casein.[10] The protein fraction in whey constitutes approximately 10% of the total dry solids in whey. This  protein is typically a mixture of beta-lactoglobulin (~65%), alpha-lactalbumin (~25%), bovine serum albumin (~8%)(see also serum albumin), and immunoglobulins.[11] These are soluble in their native forms, independent of pH. Being a by-product of the cheese making process, and likelihood of animal rennet use, whey protein as well as casein products may not be suitable for consumption by lacto-vegetarians or observers of kosher dietary laws. There are, however, specialty producers of vegetarian-approved whey protein products produced using non-animal "rennet" (enzymes). These products are often also labeled as kosher and halal approved. The amino acid cysteine in whey protein is a substrate for the synthesis of glutathione in the body which is an ubiquitous cellular antioxidant; laboratory experiments have suggested that whey protein and its components might reduce the risk of cancer in animals, suggesting an avenue for future medical research.[12]

Major forms Whey protein typically comes in four major forms: concentrate (WPC), isolate (WPI), hydrolysate (WPH) and Native Whey. Concentrates have typically a low (but still significant) level of fat and cholesterol but, in general, compared to the other forms of whey protein, have higher levels of bioactive compounds, and carbohydrates in the form of lactose — they are 29%–89% protein by weight. Isolates are processed to remove the fat, and lactose, but are usually lower in bioactivated compounds as well — they are 90%+ protein by weight. Like whey protein concentrates, whey protein isolates are mild to slightly milky in taste. Hydrolysates are whey proteins that are predigested and partially hydrolyzed for the purpose of easier  metabolizing, but their cost is generally higher.[6] Highly hydrolysed whey may be less allergenic than other forms of whey.[8]  Native whey protein, the purest form of whey protein which has been extracted from skim milk and not a by product of cheese production, produced as a concentrate and isolate.

Health effects The use of whey protein as a source of amino acids and its effect on reducing the risks of diseases such as heart disease, cancer and diabetes has been the focus of ongoing research as of 2007.[13] Whey is an abundant source of branched-chain amino acids (BCAAs),[14] which are used to stimulate protein synthesis.[15] When leucine is ingested in high amounts, such as with whey protein supplementation, there is greater stimulation of protein synthesis, which may speed recovery and adaptation to stress (exercise).[16] Whey has approximately three grams of leucine per serving and the threshold for optimal protein synthesis is three grams.[17] As with other forms of protein, consumption of whey protein shortly after vigorous exercise can boost muscle hypertrophy.[18] https://en.wi ki pedia.or g/wi ki/W hey_pr otei n#Heal th_effects

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Scientific evidence has shown that proteins high in essential amino acids (EAA), branched chain amino acids (BCAA), and particularly leucine (Leu) are associated with increased muscle protein synthesis, weight loss, body fat loss, and decreased plasma insulin and triglyceride profile.[19] A study done by Hulmi et al (2009) had subjects either consume a whey protein drink or placebo, the results showed that the whey  protein sample had a three percent increase in the cross section area of the vastus lateralis muscle and a five  percent increase in the muscle force of the isometric leg extension. However there was no convincing evidence that comparative upper body muscle mass or strength was increased nor was there any significant increase in quadriceps femoris other than the vastus lateralis. [17]

References 1. Marshall, Mars hall, K (2004). "Therapeutic applications applications of whey protein".  Alternative  Alternative Medicine Review Review 9 (2): 136–156. PMID 15253675 (https://www.ncbi.nlm.nih.gov/pubmed/15253675). 2. Wal JM (November (November 2004). 2004). "Bovine "B ovine milk allergenicity". allergenicity".  Ann. Allergy As thma Immunol. Immunol. 93 (5 Suppl 3): S2–11. doi:10.1016/S1081-1206(10)61726-7 (https://dx.doi.org/10.1016%2FS1081-1206%2810%2961726-7). PMID 15562868 (https://www.ncbi.nlm.nih.gov/pubmed/15562868). 3. Burks W, W , Helm R, Stanley S, Bannon GA (June (J une 2001). "Food allergens". allergens". Curr Opin Allergy Clin Immunol  1 (3): 243–8. doi:10.1097/01.all.0000011021.73682.01 (https://dx.doi.org/10.1097%2F01.all.0000011021.73682.01). PMID 11964696 (https://www.ncbi.nlm.nih.gov/pubmed/11964696). 4. Spurlock, D. "Isolation and Identification of Casein From Milk Course Cours e Notes" (http://homepages.ius.edu/dspurloc/c122/casein.htm). Retrieved 27 June 2014. 5. "Whey." The Encyclopædia Encyclopædia Britannica. 15th ed. 1994 6. Foegeding, EA; Davis, Davis, JP; J P; Doucet, Doucet, D; McGuffey, MK (2002). "Advances "Advances in modifying and and understanding whey whey  protein functionality functionality". ". Trends in Food Science & Technology 13  (5): 151–9. doi:10.1016/S0924-2244(02)00111-5 (https://dx.doi.org/10.1016%2FS0924-2244%2802%2900111-5). 7. Tunick MH (2008). "Whey "W hey Protein Production and and Utilization.". Utilization.". In Onwulata Onwulata CI, Huth PJ. Whey processing,  functiona  functionality lity and health health benefits benefits   (http://www.ars.usda.gov/research/publications/Publications.htm? seq_no_115=209388) (abstract). Ames, Iowa: Blackwell Publishing; IFT Press. pp. 1–13. 8. Lee YH (November 1992). 1992). "Food-processing "Food- processing approaches to altering allergenic allergenic potential potential of milk-based formula.".  J. Pediatr. Pediatr. 121  (5 Pt 2): S47–50. doi:10.1016/S0022-3476(05)81406-4 (https://dx.doi.org/10.1016%2FS00223476%2805%2981406-4). PMID 1447634 (https://www.ncbi.nlm.nih.gov/pubmed/1447634). 9. Jay R. Hoffman and and Michae Michaell J. Falvo (2004). "Protein - Which is best?".  Journal  Journal of Sports Science Science and Medicine Medicine (3): 118–130. 10. Luhovyy BL, Akhavan T, Anders Anderson on GH (2007). "Whey " Whey proteins in the regulation of food intake and and satiety" (http://www.jacn.org/cgi/content/full/26/6/704S).  Journal  Journal of the American American Colleg C ollegee of Nutrition 26  (6): 704S–  712S. doi:10.1080/07315724.2007.10719651 (https://dx.doi.org/10.1080%2F07315724.2007.10719651). PMID 18187437 (https://www.ncbi.nlm.nih.gov/pubmed/18187437). 11. Haug A, Høstmark AT, Harstad OM, A; Høstmark, AT; Harstad, OM (25 September September 2007). "Bovine milk in human nutrition – a review" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2039733).  Lipids Health Dis 6: 25. doi:10.1186/1476-511X-6-25 (https://dx.doi.org/10.1186%2F1476-511X-6-25). PMC 2039733 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2039733). PMID 17894873 (https://www.ncbi.nlm.nih.gov/pubmed/17894873). 12. P.W. P.W . Parodi (2007). "A Role for Milk Proteins and their their Peptides in Cancer Prevention" (http://www.benthamdirect.org/pages/content.php?CPD/2007/00000013/00000008/0005B.SGM). Current   Pharmaceutic  Pharmaceutical al Design 13 (8): 813–828. doi:10.2174/138161207780363059 (https://dx.doi.org/10.2174%2F138161207780363059). ISSN 1873-4286 (https://www.worldcat.org/issn/18734286).

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13. Krissansen Kriss ansen GW (December (December 2007). 2007). "Emerging " Emerging health properties of whey proteins and their their clinical implications" implications" (http://www.jacn.org/cgi/content/full/26/6/713S).  J Am A m Coll C oll Nutr  N utr  26  (6): 713S–23S. doi:10.1080/07315724.2007.10719652 (https://dx.doi.org/10.1080%2F07315724.2007.10719652). PMID 18187438 (https://www.ncbi.nlm.nih.gov/pubmed/18187438). 14. Rieu I, Balage B alage M, Sornet Sor net C et al. al. (April ( April 2007). "Increased "Incr eased availability availability of leucine with leucine-rich leucine-rich whey proteins improves postprandial muscle protein synthesis in aging rats" (http://linkinghub.elsevier.com/retrieve/pii/S08999007(07)00007-X). Nutrition 9007(07)00007-X).  Nutrition 23  (4): 323–31. doi:10.1016/j.nut.2006.12.013 (https://dx.doi.org/10.1016%2Fj.nut.2006.12.013). PMID 17367997 (https://www.ncbi.nlm.nih.gov/pubmed/17367997). 15. Kimball Scott; Jefferson, Jeffer son, LS (2006). "Signaling Pathways Pathways and Molecular Mechanisms Mechanisms through thr ough which which BranchedBranchedChain Amino Acids Mediate Translational Control of Protein Synthesis" (http://jn.nutrition.org/cgi/content/full/136/1/227S). The Journal of Nutrition 136  (1): 227S–31S. PMID 16365087 (https://www.ncbi.nlm.nih.gov/pubmed/16365087). 16. Ha E, Zemel MB (May 2003). "Functional properties of whey, whey components, components, and ess essential ential amino amino acids: acids: mechanisms underlying health benefits for active people (review)".  J. Nutr. Biochem. Biochem. 14  (5): 251–8. doi:10.1016/S0955-2863(03)00030-5 (https://dx.doi.org/10.1016%2FS0955-2863%2803%2900030-5). PMID 12832028 (https://www.ncbi.nlm.nih.gov/pubmed/12832028). 17. Hulmi, J. J.; J .; Kovanen, Kovanen, V.; Selänne, H.; Kraemer, Kraemer, W. J.; J .; Häkkinen, K.; K.; Mero, A. A. (2009). ( 2009). "Acute and and longterm effects of resistance exercise with or without protein ingestion on muscle hypertrophy and gene expression" (http://www.ncbi.nlm.nih.gov/pubmed/18661258).  Amino Acids 37  (2): 297–308. doi:10.1007/s00726-008-0150-6 (https://dx.doi.org/10.1007%2Fs00726-008-0150-6). ""The change of the average QF CSA was higher in the  protein group (9.9 (9. 9 ± 7.4%)compare 7.4%)compared d to placebo placebo (7.5 ± 4.8%) but the difference difference did not rea r each ch statistica s tatisticall significance (P[0.05)....The average increase in the VL muscle (VL1–4) was significantly higher in the protein group (relative increase: 14.8 ± 6.8%) compared to the placebo (11.2 ± 5.6%) (P\0.05)....However, compared to the control group (8.0 ± 9.5%, P[0.05), isometric leg extension increased significantly only in the protein group (a relative increase of 24.3 ± 12.3%, difference between the groups P = 0.02), whereas the increase was not significant in the placebo group (19.3 ± 15.5%, P = 0.23)." 18. Phillips SM (February 2011). "The "T he science science of muscle muscle hypertr hypertrophy: ophy: making making dietary dietary protein count". count".  Proc Nutr Soc (Review) 70 (1): 100–3. doi:10.1017/S002966511000399X (https://dx.doi.org/10.1017%2FS002966511000399X). PMID 21092368 (https://www.ncbi.nlm.nih.gov/pubmed/21092368). 19. Etzel. "Manufacture and and use of dairy protein fractions". fractions" .  J. Nutr. 134: 996S–1002S.

External links Whey protein resources (http://www.nationaldairycouncil.org/EducationMaterials/HealthProfessionalsEducationKits/Pages/ WheyProtein.aspx), National Dairy Council Whey Protein Healthnotes (http://myhealth.ucsd.edu/library/healthguide/en-us/Cam/topic.asp? hwid=hn-2933008), University of California, San Diego What does science say about whey protein and muscle building? (http://www.efsa.europa.eu/en/efsajournal/pub/1818.htm), European Food Safety Authority on whey  protein claims Retrieved from "https://en.wikipedia.org/w/index.php?title=Whey_protein&oldid=680496656" Categories: Categories: Bodybuilding Bodybuilding supplements supplements Dietary supplements supplements Proteins

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