Whey

Whey is the liquid remaining after milk has been curdled and strained. It is a byproduct of the manufacture of cheese or casein and has several commercial uses. Sweet whey is a byproduct resulting from the manufacture of rennet types of hard cheese, like cheddar or Swiss cheese. Acid whey (also known as sour whey) is a byproduct brought out during the making of acid types of dairy products, such as cottage cheese or strained yogurt.

For other uses, see Whey (disambiguation).
Sweet whey, fluid
Whey collecting as newly made cheese drains
Nutritional value per 100 g (3.5 oz)
Energy112 kJ (27 kcal)
5.14 g
Sugars5.14 g
0.36 g
0.85 g
MineralsQuantity %DV†
Calcium
5%
47 mg
Other constituentsQuantity
Water93.12 g
†Percentages are roughly approximated using US recommendations for adults.
Source: USDA Nutrient Database

Whey proteins consist of α-lactalbumin, β-lactoglobulin, serum albumin, immunoglobulins, and proteose peptones.[1]

Composition

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,[2] whereas the protein in human milk is 70% whey and 30% casein.[3] 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.[4] These are soluble in their native forms, independent of pH.

The amino acid cysteine in whey protein is a substrate for the synthesis of glutathione in the body which is a 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.[5]

Production

To produce cheese, rennet or an edible acid is added to heated milk. This makes the milk coagulate or curdle, separating the milk solids (curds) from the liquid whey.[6] Sweet whey is the byproduct of rennet-coagulated cheese, and acid whey (also called sour whey) is the byproduct of acid-coagulated cheese. Sweet whey has a pH greater than or equal to 5.6; acid whey has a pH less than or equal to 5.1.[7]

Whey is left over when milk is coagulated during the process of cheese production and contains everything that is soluble from milk after the pH is dropped to 4.6 during the coagulation process.[8] It is a 5% solution of lactose in water, with some minerals and lactalbumin.[9] The fat is removed and then processed for human foods.[9] Processing can be done by simple drying, or the relative protein content can be increased by removing lipids and other non-protein materials.[10] For example, spray drying after membrane filtration separates the proteins from whey.[11]

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.[10] Heat-denatured whey can still cause allergies in some people.[12]

Uses

Whey is used to produce whey cheeses such as ricotta, brunost, and whey butter and many other products for human consumption. The fat content of whey is low; for example 1,000 kg of whey are required to make typically 1 kg of whey butter.[13] It is also an additive in many processed foods, including breads, crackers, and commercial pastry, and in animal feed. Whey proteins consist primarily of α-lactalbumin and β-lactoglobulin. Depending on the method of manufacture, whey may also contain glycomacropeptides (GMP). It is also an abundant source of lactose which can further be used for the synthesis of lactose-based bioactive molecules.[14]

Dairy whey remaining from home-made cheesemaking has many uses. It is a flour conditioner and can be substituted for skim milk in most baked good recipes that require milk (bread, pancakes, muffins, etc.).

Throughout history, whey was a popular drink in inns and coffee houses. When Joseph Priestley was at college at Daventry Academy, 1752–1755, he records that, on the morning of Wednesday, 22 May 1754, he "went with a large company to drink whey."[15] This was probably "sack whey" or "wine whey".

Another use of whey is to make "cream of tartar whey": "Put a pint of blue milk [skim milk] over the fire, when it begins to boil, put in two tea spoonfuls of cream of tartar, then take it off the fire, and let it stand till the curd settles to the bottom of the pan, then put it into a basin to cool, and drink it milk warm.”[16]

In areas where cheese is made, excess whey byproduct is sometimes sprayed over hay fields as a fertilizer.

Historically whey, being a byproduct of cheese making, was considered a waste product and was pumped into rivers and streams in the U.S. Containing protein, this practice led to the growth of large concentrations of algae. These were deemed to be a hazard to the ecosystem because they prevented sunlight and oxygen from reaching the water. The government eventually prohibited this practice which led to a disposal problem for producers. Their first solution was to use it as a cheap filler in the production of ice cream. Whey eventually found its way into many other products as a filler and ultimately into a number of health food products where it remains a popular supplement.

Whey protein
Main article: Protein quality
Containers of whey protein being sold at a health food store

Whey protein is commonly marketed as a dietary supplement, and various health claims have been attributed to it in the alternative medicine community.[17] Although whey proteins are responsible for some milk allergies, the major allergens in milk are the caseins.[18][19] It is sold as a nutritional supplement.[20]

Whey is the primary ingredient in most protein powders, which are used primarily by athletes and bodybuilders to obtain the necessary amounts of protein on a daily basis. Whey protein has a high level of leucine,[21] one of the three branched-chain amino acids, making it ideal for muscle growth and repair. The whey is then pasteurized, just like any milk, to assure that no harmful bacteria are breeding in the liquid. It is heated to 70–80 °C (158–176 °F) and is then cooled back down to 4 °C (39 °F). Studies have shown that this process of using extreme temperatures eliminates 99.7% of bacteria without coagulating the protein into a solid mass. Next, the whey must be filtered, and so is loaded into a massive web of ceramic filters and stainless steel turbines. These machines work to separate out the lactose as well as the fats, leaving a liquid of 90% whey protein.[22]

Hydrolysates are whey proteins that are predigested and partially hydrolyzed for the purpose of easier metabolizing, but their cost is generally higher.[10] Highly hydrolysed whey may be less allergenic than other forms of whey.[12]

Native whey protein is extracted from skim milk, not obtained as a byproduct of cheese production, and is produced as a concentrate and isolate.[23][24][25]

Whey cream and butter

Cream can be skimmed from whey. Whey cream is saltier, tangier, and "cheesier" than ("sweet") cream skimmed from milk, and can be used to make whey butter. Due to the low fat content of whey the yield is not high, with typically two to five parts of butter manufactured from 1,000 parts of whey.[13] Whey cream and butter are suitable for making butter-flavoured food, as they have a stronger flavour of their own. They are also cheaper to manufacture than sweet cream and butter.

Health

Because whey contains lactose, it should be avoided by those who are lactose intolerant. When used as a food additive, whey can contribute to quantities of lactose far above the level of tolerance of most lactose-intolerant individuals.

Liquid whey contains lactose, vitamins, protein, and minerals, along with traces of fat.[26]

In 2005 researchers at Lund University in Sweden found that whey can help regulate and reduce spikes in blood sugar levels in people with type 2 diabetes by increasing insulin secretion.[27]

People can be allergic to whey or other milk proteins (this is an allergy, not lactose intolerance). As whey proteins are altered by high temperatures, whey-sensitive people may be able to tolerate evaporated, boiled, or sterilized milk. Hard cheeses are high in casein, but low in whey proteins, and are the least allergenic for those allergic to whey proteins. However, casein proteins (which are heat-stable) are the most important allergens in cheese, and an individual may be allergic to either or both types of protein.[28]

Unsupported health claims

In 2010 a panel of the European Food Safety Authority examined health claims made for whey protein. For the following claims either no references were provided for the claimed effect or the provided studies did not test the claims, or reported conflicting results:[17]

  • Increase in satiety leading to a reduction in energy intake
  • Contribution to the maintenance or achievement of a normal body weight
  • Growth or maintenance of muscle mass
  • Increase in lean body mass during energy restriction and resistance training
  • Reduction of body fat mass during energy restriction and resistance training
  • Increase in muscle strength
  • Increase in endurance capacity during the subsequent exercise bout after strenuous exercise
  • Skeletal muscle tissue repair
  • Faster recovery from muscle fatigue after exercise.

On the basis of the data presented, the 2010 panel concluded that a cause and effect relationship between the consumption of whey protein and these claims had not been established.

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gollark: Unpaid taxes, obviously.

See also

References
  1. Farrell, H.M.; Jimenez-Flores, R.; Bleck, G.T.; Brown, E.M.; Butler, J.E.; Creamer, L.K.; Hicks, C.L.; Hollar, C.M.; Ng-Kwai-Hang, K.F. (2004-06-01). "Nomenclature of the Proteins of Cows' Milk – Sixth Revision". Journal of Dairy Science. 87 (6): 1641–1674. doi:10.3168/jds.s0022-0302(04)73319-6. ISSN 0022-0302. PMID 15453478.
  2. Jay R. Hoffman & Michael J. Falvo (2004). "Protein – Which is best?". Journal of Sports Science and Medicine (3): 118–130.
  3. Luhovyy BL, Akhavan T, Anderson GH (2007). "Whey proteins in the regulation of food intake and satiety". Journal of the American College of Nutrition. 26 (6): 704S–712S. doi:10.1080/07315724.2007.10719651. PMID 18187437. Archived from the original on 2011-03-26.
  4. Haug A, Høstmark AT, Harstad OM, A; Høstmark, AT; Harstad, OM (25 September 2007). "Bovine milk in human nutrition – a review". Lipids Health Dis. 6: 25. doi:10.1186/1476-511X-6-25. PMC 2039733. PMID 17894873.CS1 maint: multiple names: authors list (link)
  5. P.W. Parodi (2007). "A Role for Milk Proteins and their Peptides in Cancer Prevention". Current Pharmaceutical Design. 13 (8): 813–828. doi:10.2174/138161207780363059. ISSN 1873-4286. PMID 17430183.
  6. Wiley, Andrea S. (2014). Cultures of Milk: The Biology and Meaning of Dairy Products in the United States and India. Cambridge, Massachusetts: Harvard University Press. p. 11. ISBN 978-0-674-72905-6.
  7. Miller, Gregory D. (2006). Handbook of Dairy Foods and Nutrition (Third ed.). CRC Press. p. 39. ISBN 978-1-420-00431-1.
  8. Spurlock, D. "Isolation and Identification of Casein From Milk Course Notes". Archived from the original on 16 June 2014. Retrieved 27 June 2014.
  9. "Whey." The Encyclopædia Britannica. 15th ed. 1994
  10. Foegeding, EA; Davis, JP; Doucet, D; McGuffey, MK (2002). "Advances in modifying and understanding whey protein functionality". Trends in Food Science & Technology. 13 (5): 151–159. doi:10.1016/S0924-2244(02)00111-5.
  11. Tunick MH (2008). "Whey Protein Production and Utilization." (abstract). In Onwulata CI, Huth PJ (eds.). Whey processing, functionality and health benefits. Ames, Iowa: Blackwell Publishing; IFT Press. pp. 1–13.
  12. Lee YH (November 1992). "Food-processing approaches to altering allergenic potential of milk-based formula". J. Pediatr. 121 (5 Pt 2): S47–50. doi:10.1016/S0022-3476(05)81406-4. PMID 1447634.
  13. Full text of "Whey butter". Washington, D.C. : U.S. Dept. of Agriculture, Bureau of Animal Industry. 1910.
  14. Karimi Alavijeh, M.; Meyer, A.S.; Gras, S.L.; Kentish, S.E. (February 2020). "Simulation and economic assessment of large-scale enzymatic N-acetyllactosamine manufacture". Biochemical Engineering Journal. 154: 107459. doi:10.1016/j.bej.2019.107459.
  15. Tony Rail and Beryl Thomas; Joseph Priestley's Journal while at Daventry Academy, 1754, transcribed from the original shorthand; Enlightenment and Dissent (University of Wales, Aberystwyth), 1994, 13, 49–113.
  16. Raffald, Elizabeth (1782). The Experienced English Housekeeper (Eighth ed.). London: R. Baldwin. p. 314.
  17. EFSA Panel on Dietetic Products, Nutrition and Allergies (October 2010). "Scientific Opinion on the substantiation of health claims related to whey protein". EFSA Journal. 8 (10): 1818. doi:10.2903/j.efsa.2010.1818.
  18. Wal JM (November 2004). "Bovine milk allergenicity". Ann. Allergy Asthma Immunol. 93 (5 Suppl 3): S2–11. doi:10.1016/S1081-1206(10)61726-7. PMID 15562868.
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  27. Frid, Anders H.; Nilsson, Mikael; Holst, Jens Juul; Björck, Inger M.E. (2005). "Effect of whey on blood glucose and insulin responses to composite breakfast and lunch meals in type 2 diabetic subjects". American Journal of Clinical Nutrition. 82 (1): 69–75. doi:10.1093/ajcn.82.1.69. PMID 16002802.
  28. ALLSA, 2014. Food-milk allergy and intolerance retrieved from https://web.archive.org/web/20150324103838/http://www.allergysa.org/c_ol_food_015.asp (archived)
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